MOLECULAR RECOGNITION REAGENTS FOR INFECTIONS IN MARINE ORGANISMS, AND DEVICES, SYSTEMS, AND METHODS FOR USING CROSS REFERENCE TO RELATED APPLICATION [0001] This application claims priority to U.S. Provisional Application Serial No. 63/382,360 filed November 4, 2022, the disclosure of which is incorporated herein by reference. REFERENCE TO SEQUENCE LISTING [0001] This application contains a Sequence Listing submitted via EFS-Web. The entire contents of the sequence listing in XML file entitled “4925- 17US04P1_Sequence_Listing.XML” created on November 3, 2022, and having a size of 29 kilobytes, is incorporated herein by reference. TECHNICAL FIELD [0002] This invention relates to fish harvesting, testing, aquaculture, and diagnostic molecules including antibodies and aptamers. BACKGROUND [0003] One of the most prominent challenges in aquaculture for safe production and maintaining animal welfare is controlling infectious diseases. In aquaculture, up to 50% of production loss is caused by infectious diseases, resulting in multibillion-dollar annual losses. The result is significant epidemics in fish and great financial loss to the associated industries. Besides bacterial, fungal, and viral diseases, parasites can harm finfish aquaculture enterprises. Although usually present in almost all ecosystems, parasites are generally benign for healthy fish. However, parasites can become problematic under stressful conditions inherently found in aquaculture. To maximize aquaculture productivity, high stocking densities and less-than-ideal water quality are typical and provide optimal conditions for the infestation of parasites. [0004] Dinoflagellates are a diverse group of aquatic protozoans and some members are parasitic, infesting the skin and gills of marine organisms. Amyloodiniosis, caused by Amyloodinium ocellatum (AO) in temperate and tropical marine fish is one of the most common and devastating parasitic diseases. Although less common and less pathogenic, Piscinoodiniosis, caused by Piscinoodinium pillulare (PP), is the freshwater version of AO in temperate and tropical freshwater fish and has convergent evolution with AO. Both are responsible for “velvet disease”, and are economically problematic in the fish aquaculture industries due to their ability to reproduce large numbers of infectious agents quickly and difficulties in detecting such agents before the onset of morbidity and mortality. In closed systems, such as recirculation aquaculture systems (RAS) or aquariums, these parasites can rapidly reproduce and cause catastrophic mortalities in fish and elasmobranchs. [0005] Most parasitic species infect invertebrates, but those belonging to the genera Amyloodinium and Piscinoodinium infest the skin and gills of susceptible marine, brackish, or freshwater fish causing velvet disease. Velvet disease infestation causes damage to the host fish through the parasite rhizoids that penetrate deep into the epithelial cells of the skin and gills to obtain nutrition leading to cell death. Infections and mass mortalities of marine fish in tropical aquaria by AO have been documented since the 1930s across nearly every teleost taxa investigated. All fish within the wide environmental range of velvet disease are highly susceptible to a lethal infection when kept in captivity. The exact economic impact of AO is unclear, but once a facility has become infected, a large portion of the fish may succumb before the infection can be tamed. Eradication of velvet disease is both time- consuming and costly and may prevent a business from becoming financially successful. [0006] Velvet disease lifecycle consists of three main stages: trophant (parasitic, feeding stage), tomont (encysted, reproductive stage), and dinospore (free-swimming, infective stage). The trophants firmly anchor to the fish and feed on its epithelia using rhizoids. After feeding for 4-5 days (temperature dependent) and growing in size from ~12um to 100um, trophants loosen their attachment and drop from the fish. They then encyst on the substratum, transform into tomonts, and divide. Reproduction peaks in a few days (again temperature dependent) with the release of as many as 256 infective, highly motile dinospores from each tomont. Upon finding a teleost host, the dinospores begin the lifecycle again. Dinospores remain infective for at least a week, with evidence that lower temperatures and non-piscine hosts may be exploited to prolong survival for up to a month. Dinospores have even been found to survive freezing temperatures and can be aerosolized over a distance of 2.5m or more. Since the lifecycle can be completed in as little as three days at 20°C, parasite load can increase rapidly and cause severe, acute mortality and infections that are very difficult to remove and control. [0007] Mortalities from both AO and PP parasites are usually attributed to anoxia, associated with severe gill hyperplasia, inflammation, hemorrhage, and necrosis in heavy infestations; or with osmoregulatory impairment and secondary microbial infections due to severe epithelial damage in mild infestation, see, e.g., Moreira et al., Physiological responses of reared sea bream (Sparus aurata Linnaeus, 1758) to an Amyloodinium ocellatum outbreak, J Fish Dis.2017 Nov; 40(11):1545-1560. This disease state, common in many cultured fish, is contagious, spreads rapidly, and has a high mortality. Behavioral and physical changes can sometimes be seen just before death, including flashing, rubbing, gasping at the surface, and a velvety appearance of the skin. However, due to its rapid onset, there are often no signs of infection before mortalities begin to appear within a system, making it imperative to diagnose and treat as early as possible [0008] Transmission of velvet disease can be through direct contact with live dinospores via contaminated fish or water, including aerosolized droplets from one culture system to another, through fomites (nets, hands, shoes, equipment, etc.), wildlife, dead fish, biofilms on tank and plumbing surfaces, and even from infected frozen baitfish used as feed. Furthermore, the potential for spreading infectious pathogens is increasing due to enhanced capabilities for transporting live, and possibly infected fish, into other aquaculture farms and systems. [0009] Specific polymerase chain reaction (PCR) assays to detect ribosomal DNA and a loop-mediated isothermal amplification (LAMP) assay for Amyloodinium dinoflagellate identification have been developed, see, e.g., Picón-Camacho et al., Development of a rapid assay to detect the dinoflagellate Amyloodinium ocellatum using loop-mediated isothermal amplification (LAMP), Vet Parasitol. 2013 Sep 23; 196(3-4):265-71. The assays perform equally well in a simple artificial seawater medium and natural seawater containing a plankton community assemblage and are not inhibited by gill tissue. However, this detection technique employs a clinical setting, appropriate laboratory equipment, and expertise to carry out diagnostic assays, which most aquaculture farms will not have. [0010] Because AO can tolerate a wide range of salinities (2 to 50 ppt) and temperatures (15-30°C), manipulations of potential adverse environmental conditions may stop divisions, but they will not kill or control outbreaks of the parasite. Under current chemical mitigation options, only the dinospore life stage is susceptible to drug treatment. Using dip/bath treatments of freshwater, formalin, or hydrogen peroxide on afflicted fish can force attached trophonts to detach, transform into the reproductive tomont cyst, and finally into the free- swimming dinospores that can then be killed using 0.15-0.2 mg/L free copper ion for 2-3 weeks. However, treatments must be repeated multiple times or for a prolonged period to control infection. It is essential during treatment to carefully monitor copper concentration, as copper is lethal to fish at higher concentrations, and if allowed to drop below lethal levels for dinospores, fish can quickly become re-infected with the copper tolerant trophont stage. While effective, freshwater dips or formalin baths, followed by copper treatment, are too harsh to utilize on highly infected or young sensitive fish and are very costly in terms of both time and treatment. Chloroquine is also an effective treatment strategy, but it can only be used on non-food fish. Current best practices may employ freshwater dips followed by numerous tank transfers allowing infected tanks to be thoroughly dried or disinfected between transfers. Drawbacks to this approach include the high cost of labor and time, frequent handling, and consequent extreme stress for the fish. However, these strict, costly, and time-consuming protocols are necessitated by the significant economic consequences of an infestation introduced into a closed system. [0011] Opportunistic parasites play a critical role in influencing global finfish aquaculture enterprises' productivity, sustainability, and economic viability. Without stringent and appropriate control measures, the impacts of these pathogens can often be significant. As global aquaculture continues to expand, the spread of parasites to new environments and the occurrence and severity of parasite infestations may also rise along with the economic fallout from such infections. The potential for climate change affecting environmental conditions may also affect current production practices, interactions between wild and farmed aquatic stocks, parasite life cycles, and transmission pathways. These and other pressures may further constrain production, sustainability, and economic feasibility. [0012] There remains an unmet need for an in-situ rapid diagnostic test (RDT) biosensor to be used by farmers for the early detection of infection and increased viability of fish in the aquaculture industry. SUMMARY [0013] The most common diagnostic technique for identifying infections from AO and PP parasites is the microscopic analysis of mucus, skin, and gills. However, there are several impediments to relying on microscopy to monitor these parasites' presence. First, identifying the parasites can be subjective, leading to potential false positives/negatives. Second, when there is visual or behavioral evidence suggesting the possible disease onset, it is too late for effective treatment and control. A tank-side RDT could ameliorate these impediments by providing growers with a biosensor for early detection of these parasites. [0014] Current methodologies for detecting AO and PP are insufficient to circumvent outbreaks that can occur rapidly and lead to 100% mortality within a few days. Control is most successful when a diagnosis is made while the parasite load is still low. However, the trophonts must be numerous for a robust determination, so that it may be too late for effective treatment strategies. Some fish have been found to develop a specific, antibody- mediated response to AO. Unfortunately, since the immune response is slow to develop, host antibody-based tests are not helpful in the early detection of infection. [0015] AO and PP parasites do not move directly from fish to fish as their immediate mode of transmission and instead first pass through a developmental phase in the water when not attached to a fish host. While trophonts can contaminate an aquaculture system via an infected host fish, both tomonts and infective dinospores can be introduced directly with incoming seawater, becoming a separate source of infection for fish in the system. Consequently, assessing the presence of both trophonts on fish gill and skin tissue and infective tomonts and dinospores in the water will provide a more comprehensive monitoring scheme for the early detection and prevention of velvet disease. Preferably this involves early detection or identification of infected water or fish before introducing either into a closed water system. An RDT biosensor could provide a rapid in-situ low-cost alternative for the detection of AO. With a parasite that reproduces as rapidly as velvet disease, immediate tank-side diagnosis is critical. [0016] Disclosed herein are devices, systems, and methods employing affinity reagents, such as recombinant monoclonal antibodies (rmAbs), aptamers, and other affinity reagents discussed below, selected to target the two infectious life stages of AO, PP, or AO and PP. The disclosed device, system, and method may be used with various sample sources, and an RDT biosensor may be used to detect AO or PP. The samples may, for example, be taken from any naturally occurring or manmade water source or site where fish are reared, housed, or wild-caught, and may, for example, represent water samples taken from an aquaculture water source; water samples taken from an aquaculture facility (e.g., a pond, pen, tank, cage or other fish-rearing enclosure); samples taken from aquaculture effluent; samples taken from fishing vessels (e.g., water samples taken from holding tanks or from seawater); or samples taken from fish (e.g., as fish mucus, fish gill swabs, skin swabs, fish tissue, fish tissue extracts or fish mucus extracts). [0017] In one aspect, the invention provides a binding molecule comprising an aptamer, wherein the aptamer is cross-reactive with one or more Amyloodinium ocellatum (AO) antigens or Piscinoodinium pillulare (PP) antigens. In more specific aspects, the aptamer comprises a sequence having 60% or greater, 65% or greater, 70% or greater, 75% or greater, 80% or greater, 85% or greater, 90% or greater, 95% or greater, 97% or greater, 98% or greater, 99% or greater, or 100% identity to any one of SEQ ID NOs:1-31. [0018] In another aspect, the invention provides a method for detecting an Amyloodinium ocellatum (AO) antigen or a Piscinoodinium pillulare (PP) antigen. The method includes contacting a sample with a binding molecule as described herein, and then determining if the binding molecule binds an AO or PP antigen present in the sample. [0019] In another aspect, the invention provides a method for generating aptamers that bind an Amyloodinium ocellatum (AO) antigen or a Piscinoodinium pillulare (PP) antigen. The method includes step of providing an AO antigen or a PP antigen immobilized on a support, contacting an oligonucleotide library with the support; and then identifying oligonucleotides from the library that specifically bind to the AO or PP antigen. Oligonucleotides that are AO antigen-binding or PP antigen-binding aptamers are identified. [0020] Accordingly, in one aspect, the present invention provides a device for detecting velvet disease infestation in aquaculture and fishing, the device comprising a test plate comprising a support bearing at least one conjugated (detection) affinity reagent and at least one immobilized (capture) affinity reagent that is cross-reactive with one or more AO or PP antigens, the affinity reagents being bound to the support or bound to particles that can migrate along the support. The device may detect AO or PP antigens in the above-described samples. In embodiments, the affinity reagents may be a protein or peptide, a sequence of nucleic acids, such as an aptamer, or another small molecule. In embodiments, the affinity reagents may be antibodies or similar compounds, such as natural antibodies, synthetic antibodies, polyclonal antibodies, monoclonal antibodies, recombinant antibodies, including recombinant monoclonal antibodies (rmAbs), or “chemical antibodies,” including aptamers and other oligos of nucleotides. [0021] In another aspect, the present invention provides a device for detecting velvet disease infestation in aquaculture and fishing. The device comprising a test plate comprising a support bearing i) a sample is taken from an aquaculture water source, aquaculture facility, aquaculture effluent or fish and ii) at least one conjugated (detection) affinity reagent and at least one immobilized (capture) affinity reagent plate that is cross-reactive with one or more velvet disease antigens, the affinity reagent being bound to the support or bound to particles that can migrate along the support. [0022] In another aspect, the present invention provides a system for assessing the presence or absence of velvet disease infestation in aquaculture and fishing. The system comprises a test plate comprising a support bearing i) a sample taken from an aquaculture water source, aquaculture facility, aquaculture effluent or fish and ii) at least one conjugated (detection) affinity reagent and at least one immobilized (capture) affinity reagent that are cross-reactive with one or more AO or PP antigens, the affinity reagents being bound to the support or bound to particles that can migrate along the support; and a detector configured to detect the absence or presence of one or more AO or PP antigens in such sample based on the extent to which such AO or PP antigens become or do not become bound to such conjugated affinity reagents. [0023] In yet another aspect, the present invention provides a system for assessing the presence or absence of velvet disease infestation in aquaculture and fishing, the system comprising a test plate comprising a support bearing i) a sample comprising one or more AO or PP antigens in solution and ii) at least one conjugated (detection) affinity reagent and at least one immobilized (capture) affinity reagent that are cross-reactive with one or more such AO or PP antigens, the affinity reagents being bound to the support or bound to particles that can migrate along the support; a detector configured to detect the absence or presence of velvet disease antigens in the such sample based on the extent to which such antigens become or do not become bound to such conjugated affinity reagents; a processor; storage for a set of sample locations, sample dates and measured velvet disease presence for such samples; and an engine for detecting AO and PP antigens in any one or more such samples. [0024] In another aspect, the present invention provides a method for assessing the presence or absence of velvet disease infestation in aquaculture and fishing. The method comprises the steps of obtaining a sample from an aquaculture water source, aquaculture facility, aquaculture effluent or fish, contacting a test plate with the sample, the test plate comprising a support bearing at least one conjugated (detection) affinity reagent, and at least one immobilized (capture) affinity reagent that is cross-reactive with one or more AO or PP antigens, the affinity reagents being bound to the support or bound to particles that can migrate along the support; and providing either a positive or negative detection of velvet disease infestation based on the extent to which AO or PP antigens that may be in such sample become or do not become bound to such conjugated affinity reagents. [0025] In embodiments, the affinity reagents may be a protein or peptide, a sequence of nucleic acids, such as an aptamer, or another small molecule. In embodiments, the affinity reagents may be antibodies or similar compounds, such as natural antibodies, synthetic antibodies, polyclonal antibodies, monoclonal antibodies, recombinant antibodies, including recombinant monoclonal antibodies (rmAbs), or “chemical antibodies,” including aptamers and other oligos of nucleotides. [0026] An especially desirable embodiment of the disclosed device, system, and method will permit testing on board a ship, at dockside, or in an aquarium, aquaculture facility, or farm. A further especially desirable embodiment of the disclosed device, system, and method will permit testing on water, fish gill, fish mucus, or fish skin swab samples. [0027] The above summary is not intended to describe each illustrated embodiment or every implementation of the subject matter hereof. The figures and the detailed description that follow more particularly exemplify various embodiments. BRIEF DESCRIPTION OF THE DRAWING [0028] Subject matter hereof may be more completely understood in consideration of the following detailed description of various embodiments in connection with the accompanying figures, in which: [0029] Fig.1 is a schematic view of a system for assessing and storing velvet disease detection data; [0030] Fig.2 is a block diagram of a system for sampling and assessing velvet disease presence in water or fish; [0031] Fig.3 is a flowchart of a velvet disease RDT biosensor assay device; [0032] Fig.4 is a block diagram of a velvet disease RDT biosensor assay device in use; [0033] Fig.5 is a block diagram of an example SELEX process; [0034] Fig.6 is an example fluorescence dot blot of AO dinospores immobilized on a PVDF membrane; [0035] Fig. 7 shows nucleic acid sequences for Amyloodinium ocellatum-binding aptamers (“AOBA”) designated AOBA-1 to AOBA-31 (SEQ ID NOs:1-31); [0036] Fig. 8 shows absorbance measurements for aptamers of Fig. 7. Binding specificity of the aptamer to AO dinospores was compared to the negative control. Absorbance (AU) read at 450nm, and sample signal is corrected by deducting the blank control signal. [0037] Fig.9 shows a 2-D modeled structure of AOBA-1; [0038] Fig.10 shows a 2-D modeled structure of AOBA-2; [0039] Fig.11 shows a 2-D modeled structure of AOBA-3; [0040] Fig.12 shows a 2-D modeled structure of AOBA-4; [0041] Fig.13 shows a 2-D modeled structure of AOBA-5; [0042] Fig.14 shows a 2-D modeled structure of AOBA-6; [0043] Fig.15 shows a 2-D modeled structure of AOBA-7; [0044] Fig.16 shows a 2-D modeled structure of AOBA-8; [0045] Fig.17 shows a 2-D modeled structure of AOBA-9; [0046] Fig.18 shows a 2-D modeled structure of AOBA-10; [0047] Fig.19 shows a 2-D modeled structure of AOBA-11; [0048] Fig.20 shows a 2-D modeled structure of AOBA-12; [0049] Fig.21 shows a 2-D modeled structure of AOBA-13; [0050] Fig.22 shows a 2-D modeled structure of AOBA-14; [0051] Fig.23 shows a 2-D modeled structure of AOBA-15; [0052] Fig.24 shows a 2-D modeled structure of AOBA-16; [0053] Fig.25 shows a 2-D modeled structure of AOBA-17; [0054] Fig.26 shows a 2-D modeled structure of AOBA-18; [0055] Fig.27 shows a 2-D modeled structure of AOBA-19; [0056] Fig.28 shows a 2-D modeled structure of AOBA-20; [0057] Fig.29 shows a 2-D modeled structure of AOBA-21; [0058] Fig.30 shows a 2-D modeled structure of AOBA-22; [0059] Fig.31 shows a 2-D modeled structure of AOBA-23; [0060] Fig.32 shows a 2-D modeled structure of AOBA-24; [0061] Fig.33 shows a 2-D modeled structure of AOBA-25; [0062] Fig.34 shows a 2-D modeled structure of AOBA-26; [0063] Fig.35 shows a 2-D modeled structure of AOBA-27; [0064] Fig.36 shows a 2-D modeled structure of AOBA-28; [0065] Fig.37 shows a 2-D modeled structure of AOBA-29; [0066] Fig.38 shows a 2-D modeled structure of AOBA-30; and [0067] Fig.39 shows a 2-D modeled structure of AOBA-31. [0068] While various embodiments are amenable to various modifications and alternative forms, specifics have been shown by example in the drawing and will be described in detail. It should be understood, however, that the intention is not to limit the claimed inventions to the particular embodiments described. On the contrary, the intention is to cover all modifications, equivalents, and alternatives falling within the spirit and scope of the subject matter as defined by the claims. DETAILED DESCRIPTION [0069] Velvet disease is problematic in warm water fresh and marine fisheries and aquaculture due to its ability to produce large quantities of infectious dinospores rapidly and is hard to detect with current technologies (microscopy) until morbidity and mortality have occurred. At that point, treatment and control options are limited, leading to a massive loss of fish products and reduced revenue for the growers. [0070] Commercial disease RDT biosensors, such as for Vibrio cholera, typically employ a lateral flow technology assay (LFA), based on the principles of immunochromatography and nanotechnology, in which the primary components used for detection are antibodies (Abs). Antibody based-biosensors work similarly to enzyme-linked immunosorbent assay (ELISA) where the sensor relies on the ability of the Abs biosensor to recognize its target of interest (the antigen; Ag). An effective Ab-based biosensor should have high specificity in a very complex medium, well-characterized binding properties, high stability, and the potential for low-cost, large-scale production. [0071] A polyclonal Ab (pAb) composition is a heterogeneous antibody mixture derived from the immune response in a host animal species, with each pAb recognizing a different structural region (epitope) of the targeted Ag. While these pAbs can be easily generated, batch-related differences, varying affinity and poly-specificity (reactivity with more than one target) can be potential problems. Monoclonal antibodies (mAbs) can be better at targeting a particular region of an Ag of interest, resulting in higher specificity than pAbs; however, animal-derived, cell line production of mAbs can take up to eight months. [0072] Rather than using pAbs or mAbs, a rmAb assay can be selected and developed in vitro using synthetic genes and a targeted selection strategy. Animals are not required, thereby shortening development time, and production can occur in the bacteria E. coli, providing a continuous source of Abs (unlike in vivo derived pAbs). Using rmAbs for antigen binding can also provide improved specificity and high affinity, which are especially useful in an RDT biosensor. An assay based on appropriate rmAbs can also optimize the binding of both targets in the various life stages. Without being bound by theory, rmAbs may provide enhanced cross-reactivity and thus enhanced detection for any of the AO or PP life stages, allowing for a more thorough and sensitive screening method for fish. [0073] The disclosure provides binding molecules including antibodies and aptamers that are cross-reactive with one or more AO antigens or PP antigens, and recognizes antigens from one or more lifecycle stage(s): trophant, tomont, and dinospore. In some aspects the antibody or aptamer recognizes antigens from all of the three lifecycle stages. The binding molecules of the disclosure including antibodies and aptamers can recognize a cellularly-intact AO or PP organism. [0074] De novo transcriptome sequencing of AO tomonts has been reported by Byadgi et al. (Genes 2020, 11, 1252). A contig analysis (overlapping DNA segments) and BLAST searches for known virulent factors resulted in hits to Rab proteins, AP120, Ribosomal phosphoprotein, Heat-shock protein70, Casein kinases, Plasmepsin IV, and Brucipain. A wide range of peptidases was identified. In particular, the following virulence group/virulence factors were identified: Adhesin/AP120, Invasion/Gp63 (surface metalloprotease), Invasion/P0 (Ribosomal phosphoprotein), Invasion/ROM1 (Rhomboid- like protease), Invasion/RabA, Heat shock protein/Hsp70, Establishment/Casein kinase II, Establishment/Rab7A, Establishment/Vps35 Establishment/Rab11B, Establishment/Vps29, Establishment/Rab5, Establishment/CPSII, Proteases/Brucipain, Proteases/Plasmepsin II, Proteases/Plasmepsin I, and Proteases/Plasmepsin IV. These and other proteins of AO represent actual or potential targets of aptamers of the disclosure or variants thereof. [0075] The advantages described here, and many of the examples discussed in greater detail below, focus on rmAbs. Though rmAbs may represent some advantages over pAbs and mAbs, all three fall under the umbrella of affinity reagents. Other affinity reagents include various other proteins and peptides, as well as aptamers and oligos of nucleic acids. [0076] Like recombinant antibodies, aptamers are a non-animal technology with rapid development time. Unlike antibodies, aptamers are nucleic-acid based, often resulting in a much smaller molecule as they are a short, single-stranded oligo of either DNA or RNA. Despite this material difference, aptamers share antibodies’ ability to bind proteins and modulate their function and are sometimes referred to as “chemical antibodies” due to this antibody-like behavior. Aptamers also share many advantages of rmAbs, including exhibiting high specificity and affinity. Aptamers may also exhibit unique advantages in some situations, such as the ability to access hidden epitopes due to their flexibility. [0077] The disclosure provides aptamers capable of binding one or more Amyloodinium ocellatum (AO) antigen(s) or one or more Piscinoodinium pillulare (PP) antigens. Exemplary AO or PP antigen-binding aptamer sequences are set forth in SEQ ID NOs:1-31 (AOBA 1-31). The disclosure also describes nucleic acid variants SEQ ID NOs:1-31, and derivatives of the aptamers of SEQ ID NOs:1-31 and variants thereof. [0078] As used herein, an “aptamer” is an oligonucleotide (a polymer of nucleic acid residues) that adopts a tertiary configuration that folds into a stable complex capable of binding to an antigen, or antigen. As used herein, an aptamer-based “binding molecule” refers to a compound that includes an aptamer per se, and can optionally include one or other non-nucleic acid moieties, such as detection moieties such as fluorophores, drugs, or other non-nucleic acid polymers. [0079] Processes for the identification of aptamers that bind to target antigens are well known (see, for example, Oliphant et al.1989 Mol. Cell Biol.9, 2944-2949; Tuerk and Gold 1990 Science 249, 505-510; Ellington and Szostak 1990 Nature 346, 818-822). Aptamer selection processes include the systematic evolution of ligands by exponential enrichment (SELEX), selected and amplified binding site (SAAB), and cyclic amplification and selection of targets (CASTing). SELEX can produce oligonucleotides that are either single- stranded DNA or RNA molecules with specific binding properties to one or more target ligands (e.g., antigens). The SELEX process isolates ligand-binding oligonucleotides from large libraries of random synthetic oligonucleotides. This method can produce strong binding aptamers to the desired ligand, similar to the binding affixing of monoclonal antibodies to ligands. [0080] Aspects of the disclosure relate to methods for isolating an aptamer that specifically binds one or more Amyloodinium ocellatum (AO) antigen(s) or one or more Piscinoodinium pillulare (PP) antigens. Exemplary and preferred antigens from AO and PP include OA and PP proteins, OA and PP protein complexes, and portions of OA and PP proteins capable of being recognized by an aptamer. For example, the SELEX method can include providing an AO or PP antigen that has been isolated or is in a mixture of multiple AO or PP antigens. For example, the AO or PP antigen or a mixture of antigens can be immobilized on a solid support. The method also includes providing an oligonucleotide library that includes a plurality of oligonucleotides, wherein among the plurality of oligonucleotides, there are aptamer candidates capable of AO or PP antigen(s); contacting the AO or PP antigen with the oligonucleotide library; and then isolating an AO or PP antigen-binding aptamer. The method may include isolating an AO or PP antigen-binding aptamer and removing oligonucleotides that do not bind to the AO or PP antigen. For example, the SELEX method can include eluting the candidate aptamer from the AO or PP antigen that is immobilized on solid support under increasing stringency and then isolating an eluted AO or PP antigen-binding aptamer having high affinity for the AO or PP antigen. [0081] After the eluted AO or PP antigen-binding aptamer or aptamers have been isolated, the population of these aptamers can be amplified by a process such as a polymerase chain reaction (PCR). This can be accomplished using an oligonucleotide library wherein the oligonucleotides have a standardized 5' end with a specific nucleotide sequence and a standardized 3' end with a specific nucleotide sequence. Primers complementary to these 5’ and 3’ ends can be used in a PCR reaction to amplify the eluted oligonucleotides. [0082] The process can be repeated by applying the eluted aptamers to the solid support with immobilized AO or PP antigen, allowing the aptamers to bind to the support and then eluting the antigens again, but under conditions of increasing stringency. An aptamer is distinguished from an oligonucleotide of the library as a nucleic acid species engineered through repeated selection rounds (e.g., in vitro selection) to bind to an AO or PP antigen. In some practice modes, the amplified oligonucleotides' primer regions can be removed after the desired aptamers are isolated. [0083] From the selection process, an aptamer can be isolated that binds to the AO or PP antigen and has a nucleic acid sequence with one or more unpaired nucleic acid bases and one or more paired nucleic acid bases (such as in the form of base-paired stems) when the aptamer is folded into a double-stranded configuration. One or more unpaired nucleic acid bases can form a binding pocket that can bind to the AO or PP antigen. [0084] Based on analysis of aptamers of the disclosure as exemplified by SEQ ID NOs 1-31, the aptamer can have a number of stems in the range of 1-6, in the range of 1-5, in the range of 1-4, in the range of 1-3, or 2, or 1. In those one or more stems of the aptamer there can be a number of base pairs which form the stem, the number of base pairs being in the range of 1-10, in the range of 1-9, in the range of 1-8, in the range of 1-7, in the range of 1- 6, in the range of 1-5, in the range of 1-4, in the range of 1-3, or 2, or 1. [0085] In stems of the aptamer structures there can be full base pairing or partial base pairing. Full base pairing is when there is A-T and/or G-C pairing in the stem. Partial base pairing can occur when there are mismatches in the stem structure, such as G-T mismatches, along with A-T and/or G-C pairing. Nucleotide mismatching in stem structures of nucleic acids is known in the art (e.g., see Müller, U.R., and Fitch, W.M. The biological significance of G-T/G-U mispairing in nucleic acid secondary structure. J Theor Biol.1985;117:119-26). Reference is made to Figures 11, 13, 14, 22, 31, 38, and 39 showing secondary structure of aptamers with G-C (red) and A-T (blue) base pairing, and G-T (green) mismatches. [0086] Based on analysis of aptamers of the disclosure as exemplified by SEQ ID NOs 1-31, the aptamer can have one or more stems with one or more nucleotide bulges in the stem, the nucleotide bulge being a single nucleotide bulge, or a multiple nucleotide bulge of 2, 3, 4, or 5 nucleotides. [0087] Based on analysis of aptamers of the disclosure as exemplified by SEQ ID NOs 1-31, the aptamer can have one or more unpaired nucleotide region(s) that is a loop extending from a stem, optionally 1, 2, 3, 4 or 5 loops. In the aptamer, the one or more loop(s) can have a nucleotide length in the range of 3-30 nucleotides, 3-25 nucleotides, 3- 20 nucleotides, 3-15 nucleotides, 3-10 nucleotides, 3-8 nucleotides, or 3-6 nucleotides. [0088] The AO or PP antigen-binding aptamer can be a DNA, RNA, or XNA molecule. DNA-based aptamers offer the advantage of being chemically stable and relatively inexpensive to produce. The AO or PP antigen-binding aptamer can alternatively be an RNA aptamer, wherein the presence of the RNA nucleotide provides the aptamer with wider variations on three-dimensional structures relative to a DNA aptamer. Alternatively, the AO or PP antigen-binding aptamer can be formed from Xeno nucleic acids (XNA), synthetic nucleic acid analogs with a different sugar backbone than the natural nucleic acids DNA and RNA. Synthetic nucleic acid analogs include 1,5-anhydrohexitol nucleic acid (HNA), cyclohexene nucleic acid (CeNA), threose nucleic acid (TNA), glycol nucleic acid (GNA), locked nucleic acid (LNA) peptide nucleic acid (PNA), and FANA (fluoro arabino nucleic acid). Optionally, chemically modified, non-natural nucleotides that are resistant to degradation can be used to make the AO or PP antigen-binding aptamer. Such non-natural nucleotides can include sugar-modified cations of nucleoside triphosphates which can increase the resistance of the aptamer to nucleases. Other known modifications to provide nuclease resistance to aptamers include using locked nucleic acids (LNAs), 2'-O- methylation, 2'-fluorination, 2'-amination, phosphorothiolation, and 3'-capping. These modifications can, in turn, improve the aptamer's stability. [0089] Optionally, the aptamer can be conjugated to a non-nucleotide component, such as a polymeric material like polyethylene glycol (PEG), polypropylene oxide (PPO), or polyethylene oxide (PEO). A higher molecular weight compound, like PEG, PPO, and PEO, can increase the stability of the aptamer. The AO or PP antigen-binding aptamer can be attached to a nanomaterial/nanoparticle. A “binding molecule" of the disclosure can include the aptamer per se (i.e., the aptamer portion of the binding molecule) and a non- nucleotide moiety (i.e., the non-aptamer portion of the binding molecule), such as a fluorophore. [0090] The non-nucleotide component can be covalently linked to the aptamer or non- covalently linked to the aptamer. Further, linkers for aptamers can be cleavable or non- cleavable, depending on the application for which the linked moiety is used. In some embodiments, a polymeric material like polyethylene glycol links the aptamer to another molecule, such as a therapeutic agent or a detection reagent. In some embodiments, a bifunctional crosslinker, such as one having EDC/sulfo-NHS coupling chemistry, is used. Other specific types of linker molecules can include fatty acids and pH-cleavable linkers such as the acetal linker 3,9-bis(3-aminopropyl)-2,4,8,10-tetraoxaspiro [5.5]undecane (ATU) (see Shi H. et al. Anal Chem.91:9154–60, 2019), GSH-reducible linkers, photocleavable linkers, acid-labile hydrazone linkers, cathepsin B-labile valine-citrulline dipeptide linker (see Li, F. et al. Nat. Commun.8, 1390.2017), disulfide-based, traceless cleavage linkers, such as 4-nitrophenyl 4-(2-pyridyldithio) benzyl carbonate (NPDBC) and 4-nitrophenyl 2-(2-pyridyldithio) ethyl carbonate (NPDEC). Coupling the aptamer to the desired moiety can also be done by modifying the aptamer with phosphorothioate (PS) at a desired position on the aptamer backbone. See Chen, Y. et al., Chemistries and applications of DNA-natural product conjugate. Front. Chem.10:984916, 2022. [0091] In other embodiments, a non-nucleotide moiety such as a detection reagent or a therapeutic agent is chemically linked to an aptamer strand's three ′- or 5′-terminus. This can be done by modifying the terminus of a DNA strand with an active thiol or primary amine to provide a conjugate with the desired moiety. [0092] Aptamers of the disclosure can also be attached to biotin, desthiobiotin, or digoxigenin at the 3’-end or the 5’-end of an aptamer. Procedures and kits are available for labeling aptamers with these reagents. [0093] An aptamer can be formed by complementary nucleic acid base pairing, which can create secondary structures, for example, a short helical arm and a single-stranded (unpaired) loop. A tertiary structure of the aptamer can result in a combination of secondary structures, folding in a way that can result in antigen binding. The antigen binding can be from van der Waals forces, hydrogen bonding, or electrostatic interaction, which can resemble how amino acid chemical groups of an antibody cause antigen binding. In the tertiary structure, generally, most of the aptamer, or all of the aptamer, folds into a stable complex capable of antigen interaction and binding. [0094] The AO or PP antigen-binding aptamer is generally at least about 15 nucleotides in length, and can be up to about 100, about 150, or even up to about 200 nucleotides in length. For example, the AO or PP antigen-binding aptamer can be at least about 20, at least about 25, at least about 30, at least about 35, at least about 40, at least about 45, at least about 50, at least about 55, or at least about 60 nucleotides in length, and up to about 200, up to about 150, up to about 100, up to about 90, up to about 85, up to about 80, up to about 75, or up to about 70, or within a range of any of the numerical values set forth herein, for example, such as in the range of about 15 to about 200 nucleotides, about 25 to about 150 nucleotides, about 35 to about 100 nucleotides, about 40 to about 90 nucleotides, about 45 to about 80 nucleotides, about 50 to about 75 nucleotides, or about 55 to about 70 nucleotides. [0095] Optionally, the aptamer can include a nucleic acid sequence not involved in binding to the target AO or PP antigen. In other words, this optional nucleic acid sequence is not responsible for forming a tertiary structure that provides antigen binding but serves a secondary function, such as providing for interaction with a target other than the AO or PP antigen. For example, the target may be another oligonucleotide or portion of a nucleic acid that is complementary to the optional nucleic acid sequence of the aptamer. A target nucleic acid can be coupled to a detectable moiety, such as a fluorophore, to detect the aptamer. [0096] The term "detectable moiety" (also known as a “label”) refers to a moiety capable of being detected by an analytical technique. Exemplary labels include radioisotopes, mass tags, fluorescent labels/fluorophores, and luminescent and phosphorescent groups. These are signal-generating reporter groups that can be detected without further modifications. [0097] Radioisotopes commonly include tritium, ³² P, ³³ P, ³⁵ S, and ¹⁴ C. Fluorescent labels/fluorophores ("fluorescent dyes") include molecules that absorb light energy at a defined excitation wavelength and emission of light energy at a different wavelength. Examples include, but are not limited to: Alexa Fluor dyes (Alexa Fluor 350, Alexa Fluor 488, Alexa Fluor 532, Alexa Fluor 546, Alexa Fluor 568, Alexa Fluor 594, Alexa Fluor 633, Alexa Fluor 660 and Alexa Fluor 680), AMCA, AMCA-S, BODIPY dyes (BODIPY FL, BODIPY R6G, BODIPY TMR, BODIPY TR, BODIPY 530/550, BODIPY 558/568, BODIPY 564/570, BODIPY 576/589, BODIPY 581/591, BODIPY 630/650, BODIPY 650/665), Carboxy-rhodamine 6G, carboxy-X-rhodamine (ROX), Cascade Blue, Cascade Yellow, Coumarin 343, Cyanine dyes (Cy3, Cy5, Cy3.5, Cy5.5), Dansyl, Dapoxyl, Dialkylaminocoumarin, 4',5'-Dichloro-2',7'-dimethoxy-fluorescein, DM-NERF, Eosin, Erythrosin, Fluorescein, FAM, Hydroxy-40 coumarin, IRDyes (IRD40, IRD 700, IRD 800), JOE, Lissamine rhodamine B, Marina Blue, Methoxycoumarin, Naphthofluorescein, Oregon Green 488, Oregon Green 500, Oregon Green 514, Pacific Blue, PyMPO, Pyrene, Rhodamine B, Rhodamine 6G, Rhodamine Green, Rhodamine Red, Rhodol Green, 2',4',5',7'-Tetra-bromosulfone-fluorescein, Tetramethyl-rhodamine (TMR), Carboxytetramethyl-rhodamine (TAMRA), Texas Red, and Texas Red-X. [0098] A "mass tag" refers to any moiety that can be uniquely detected by its mass using mass spectrometry (MS) detection techniques. Examples of mass tags include electrophore release tags. See, for example, U.S. Pat. Nos.4,650,750 and 5,650,270. [0099] The aptamer-containing binding molecule of the disclosure can also include a "secondary label," such as a moiety like a biotin and various protein antigens that require the presence of a second intermediate to produce a detectable signal. For biotin, the secondary intermediate may include streptavidin-enzyme conjugates. For antigen labels, secondary intermediates may include antibody-enzyme conjugates.  [0100] Nucleic acid sequences for exemplary aptamers are described herein. The aptamers of the current disclosure can have a nucleic acid sequence that is the same (i.e., 100% identity) as the specific aptamer sequences disclosed herein (i.e., SEQ ID NOs:1-31) or can have a nucleic acid sequence that is not 100% identical (i.e., <100%) to these specifically disclosed sequences. The identity can be calculated over the entire length of the aptamer sequence, referred to herein as “a global identity.” Sequences with lower identity to the specific aptamer sequences disclosed herein can be due to one or more nucleotide changes from the specific aptamer sequences of SEQ ID NOs:1-31 and can be referred to as “variant” or “mutant” aptamer sequences. In exemplary embodiments, a variant aptamer sequence of the disclosure can have a number of nucleotide variation(s) in the range of 1-24, in the range of 1-20, in the range of 1-16, in the range of 1-12, in the range of 1-10, in the range of 1-8, in the range of 1-6, such as 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, or 24 nucleotide changes (nucleotide variations or mutations) as compared to the full-length specific template sequences of SEQ ID NOs:1- 31. The percent identity of a variant sequence is determined by the number of nucleotide changes compared to the original (template) aptamer sequence. For example, a variant aptamer sequence having five nucleotide changes as compared to an original (template) aptamer sequence having a length of 62 nucleotides provides a variant with about 92% identity to the original (template) aptamer sequence (57/62). [0101] Percent (%) identity of a nucleotide sequence is the percentage of nucleotide residues that are identical between a full-length nucleotide candidate (e.g., variant) sequence and full-length template (e.g., any of SEQ ID NOs:1-31) sequence or a selected portion of the candidate and template sequences when the two sequences are aligned. Percent identity can be determined by aligning sequences and, if necessary, introducing gaps for best alignment to achieve the maximum percent sequence identity. Bioinformatic computer programs such as BLAST, BLAST2, ALIGN2, or Megalign (DNASTAR) can align sequences. Those skilled in the art can determine appropriate parameters for measuring alignment, including any algorithms needed to achieve maximal alignment over the length of the sequences being compared. [0102] Embodiments of the disclosure provide aptamer variants have a nucleotide sequences that are at least 60% or greater, 65% or greater, 70% or greater, 75% identical, at least 76% identical, at least 77% identical, at least 78% identical, at least 79% identical, at least 80% identical, at least 81% identical, at least 82% identical, at least 83% identical, at least 84% identical, at least 85% identical, at least 86% identical, at least 87% identical, at least 88% identical, at least 89% identical, at least 90% identical, at least 91% identical, at least 92% identical, at least 93% identical, at least 94% identical, at least 95% identical, at least 96% identical, at least 97% identical, at least 98% identical, or at least 99% identical to any one of SEQ ID NOs:1-31.   [0103] Based on the current disclosure and the knowledge in the art regarding aptamers, it will be appreciated that one of ordinary skill would understand that certain regions of the aptamer are more robust with respect to nucleic acid substitution. For example, variations in stem regions of a secondary or tertiary structure of an aptamer may display less impact on target molecule binding relative to unpaired regions that form an antigen biding pocket, and accordingly a variant aptamer of the disclosure may have substitutions that provide a low degree of identity to an original aptamer sequence, or even no identity in these regions. However, regions of an aptamer that have a secondary or tertiary structure that provides binding to a target antigen may be more sensitive to variation. As such, these regions (e.g., unpaired regions) may have fewer substitutions, additions, or deletions as compared to stem regions. These binding regions can have unpaired nucleic acid bases that form a binding pocket for binding of the target antigen. An unbound nucleic acid pocket can appear in a folding program, or can be recognized by its sequences without using a folding program. [0104] In view of this, variant AO or PP antigen-binding aptamer sequences of the disclosure can optionally be described in terms of “local” identity to portions of the original aptamer sequence (any one of SEQ ID NOs:1-31). For example, there can be one or more nucleotide variations in one or more “regions” of the aptamer, with such regions corresponding to specific 2D structures of the sequence, such as regions of base-pairing (stems), bulges in the stem regions (unpaired nucleotides), and regions of unpaired nucleotide stretches, such as loops extending from a stem region, unpaired nucleotide stretches between stems, and unpaired regions at the 5’ and 3’ ends of the aptamer sequence. These regions are identified as sub-sequences of the full-length aptamer sequence and can be described in terms of nucleotide positions in the aptamer, in a 5’ to 3’ direction. [0105] For example, a variant aptamer can be referred to with reference to specific nucleotide stretches of a SEQ ID NO as described herein, with those specific stretches corresponding to a 2D structure of the aptamer. With reference to a 2D folded structure, a stem of an aptamer can be formed from nucleotide region “b” (positions xx – xx) and nucleotide region “e” (positions xx – xx) of a particular SEQ ID NO, wherein regions “b” and “e” in the aptamer are based paired. In a variant aptamer, the sequence can be changed to replace a “C” in region “b” and a “G” in region “e,” which are base-paired in the stem, with corresponding nucleotides that maintain the base pairings. For example, contemplated replacements are C → A, T, or G in region “b,” and G → T, A, or C in region “e,” respectively. As such, if the stem is completely replaced with alternate base pairs, the stem structure could still be formed, but the nucleotide sequence of an aptamer variant could have 0% identity to the regions “b” and “e” of the aptamer sequence. Accordingly, in embodiments, for regions of a variant aptamer sequence that correspond to based-paired regions, such as stem regions, the variant aptamer can have, for example, 0% identity, at least 10% identity, at least 20% identity, at least 30% identity, at least 40% identity, at least 50% identity, at least 60% identity, at least 70% identity, at least 80% identity, at least 90% identity, or 100% identity to the original aptamer sequence in those regions. [0106] Variations in the stem region can also include variations that either lengthen or shorten a stem region. These variations can be reflected by addition of nucleotides to regions of a SEQ ID NO that form a stem, or deletion of nucleotides to regions of a SEQ ID NO that form a stem. Preferably, if the variant is defined by deletions to the stem, those deletions do not disrupt the ability of the aptamer to form a stem. Longer stems may permit more deletions, while shorter stems may permit less. In embodiments, the aptamer has variations than result in the loss of 2 or less base pairs, or the loss of only one base pair. In other embodiments, the stem can be lengthened by addition/insertion of nucleotides into stem regions of a SEQ ID NO, wherein such nucleotide insertions result in 1, 2, 3, 4 or 5 additional base pairs in the stem region. Such additions may increase the stability of a stem and the tertiary structure of the aptamer. [0107] An aptamer of the disclosure can also have one or more nucleotide variations in regions of the aptamer that are not predicted to be based-paired based on 2D modeling, such as loops extending from a stem region, unpaired nucleotide stretches between stems, and unpaired regions at the 5’ and 3’ ends of the aptamer sequence. Some or all of these regions may have nucleotides that coordinate with the antigen that the aptamer binds to, and therefore there may be less variability of nucleotide sequence in these regions as compared to the stems. For example, regions of a SEQ ID NO that correspond to loops extending from a stem region, unpaired nucleotide stretches between stems. Unpaired regions at the 5’ and 3’ ends of the aptamer sequence can have 75% or greater identity, at least 80% identity, at least 85% identity, at least 90% identity, at least 92% identity, at least 95% identity, at least 96% identity, at least 97% identity, at least 98% identity, or at least 99% identity, or 100% identity to the original aptamer sequence in those regions. [0108] Exemplary variants of the aptamers of SEQ ID NOs:1-31 are described herein and with reference to the 2D structure as shown in the Figures. [0109] For example, with reference to SEQ ID NO:1 (AOBA-1) and Figure 9, the disclosure provides a binding molecule that includes a variant aptamer. The binding molecule includes an aptamer having a sequence including, in a 5’ to 3’ direction: a first region comprising a sequence having 75% or greater, or 100% identity to nucleotides 1-4 of SEQ ID NO:1; a second region having a length in the range of 2-5, or 3-4 nucleotides and comprising a sequence having 0%, 30% or greater, 60% or greater, 90% or greater, or 100% identity to nucleotides 5-7 of SEQ ID NO:1; a third region comprising a sequence having 50% or greater, or 100% identity to nucleotides 8-9 of SEQ ID NO:1; a fourth region having a length in the range of 1 to 4, or 2-3 nucleotides and comprising a sequence having 0%, 50% or greater, or 100% identity to nucleotides 10-11 of SEQ ID NO:1; a fifth region comprising a sequence having 75% or greater, 85% or greater, 90% or greater, 95% or greater, or 100% identity to nucleotides 12-24 of SEQ ID NO:1; a sixth region having a length in the range of 1 to 4, or 2-3 nucleotides and comprising a sequence having 0%, 50% or greater, or 100% identity to nucleotides 25-26 of SEQ ID NO:1; a seventh region comprising a sequence having 0% or greater, or 100% identity to nucleotide 27 of SEQ ID NO:1; an eighth region having a length in the range of 3-6, or 4-5 nucleotides and comprising a sequence having 0%, 25% or greater, 50% or greater, 75% or greater, or 100% identity to nucleotides 28-31 of SEQ ID NO:1; a ninth region comprising a sequence having 75% or greater, 85% or greater, 90% or greater, 95% or greater, or 100% identity to nucleotides 32-40 of SEQ ID NO:1; a tenth region having a length in the range of 3-6, or 4- 5 nucleotides and comprising a sequence having 0%, 25% or greater, 50% or greater, 75% or greater, or 100% identity to nucleotides 41-44 of SEQ ID NO:1; an eleventh region having a length in the range of 2-5, or 3-4 nucleotides and comprising a sequence having 0%, 30% or greater, 60% or greater, 90% or greater, or 100% identity to nucleotides 45-47 of SEQ ID NO:1; a twelfth region comprising a sequence having 75%, or 100% identity to nucleotides 48-51 of SEQ ID NO:1; a thirteenth region having a length in the range of 1 to 4, or 2-3 nucleotides and comprising a sequence having 0%, 50% or greater, or 100% identity to nucleotides 52-53 of SEQ ID NO:1; a fourteenth region comprising a sequence having 75% or greater, 85% or greater, 90% or greater, 95% or greater, or 100% identity to nucleotides 54-58 of SEQ ID NO:1; a fifteenth region having a length in the range of 1 to 4, or 2-3 nucleotides and comprising a sequence having 0%, 50% or greater, or 100% identity to nucleotides 59-60 of SEQ ID NO:1; and a sixteenth region comprising a sequence having 0% or greater, or 100% identity to nucleotide 61 of SEQ ID NO:1; wherein the second and eleventh regions, the fourth and sixth regions, the eighth and tenth regions, and the thirteenth and fifteenth regions are base-paired to each other. [0110] As another example, and with reference to SEQ ID NO:2 (AOBA-2) and Figure 10, the disclosure provides a binding molecule that includes a variant aptamer. The binding molecule includes an aptamer having a sequence including, in a 5’ to 3’ direction: a first region comprising a sequence having 50% or greater, or 100% identity to nucleotides 1-2 of SEQ ID NO:2; a second region having a length in the range of 2-5, or 3- 4 nucleotides and comprising a sequence having 0%, 30% or greater, 60% or greater, 90% or greater, or 100% identity to nucleotides 3-5 of SEQ ID NO:2; a third region comprising a sequence having 75% or greater, or 100% identity to nucleotides 6-9 of SEQ ID NO:2; a fourth region having a length in the range of 2-5, or 3-4 nucleotides and comprising a sequence having 0%, 30% or greater, 60% or greater, 90% or greater, or 100% identity to nucleotides 10-12 of SEQ ID NO:2; a fifth region comprising a sequence having 75% or greater, 85% or greater, 90% or greater, 95% or greater, or 100% identity to nucleotides 13- 29 of SEQ ID NO:2; a sixth region having a length in the range of 2-5, or 3-4 nucleotides and comprising a sequence having 0%, 30% or greater, 60% or greater, 90% or greater, or 100% identity to nucleotides 30-32 of SEQ ID NO:2; a seventh region comprising a sequence having 75% or greater, 85% or greater, 90% or greater, 95% or greater, or 100% identity to nucleotides 33-42 of SEQ ID NO:2; an eighth region having a length in the range of 2-5, or 3-4 nucleotides and comprising a sequence having 0%, 30% or greater, 60% or greater, 90% or greater, or 100% identity to nucleotides 43-45 of SEQ ID NO:2; and a ninth region comprising a sequence having 75% or greater, 85% or greater, 90% or greater, 95% or greater, or 100% identity to nucleotides 46 to 62 of SEQ ID NO:2; wherein the second and fourth regions, and the sixth and eighth regions are base-paired to each other. [0111] As another example, and with reference to SEQ ID NO:3 (AOBA-3) and Figure 11, the disclosure provides a binding molecule that includes a variant aptamer. The binding molecule includes an aptamer having a sequence including, in a 5’ to 3’ direction: a first region comprising a sequence having 75% or greater, 85% or greater, 90% or greater, 95% or greater, or 100% identity to nucleotides 1 to 27 of SEQ ID NO:3; a second region having a length in the range of 2-5, or 3-4 nucleotides and comprising a sequence having 0%, 30% or greater, 60% or greater, 90% or greater, or 100% identity to nucleotides 28-30 of SEQ ID NO:3; a third region comprising a sequence having 100% identity to nucleotide 31 of SEQ ID NO:3; a fourth region having a length in the range of 2-5, or 3-4 nucleotides and comprising a sequence having 0%, 30% or greater, 60% or greater, 90% or greater, or 100% identity to nucleotides 32-34 of SEQ ID NO:3; a fifth region comprising a sequence having 75% or greater, 85% or greater, 90% or greater, 95% or greater, or 100% identity to nucleotides 35-40 of SEQ ID NO:3; a sixth region having a length in the range of 2-5, or 3- 4 nucleotides and comprising a sequence having 0%, 30% or greater, 60% or greater, 90% or greater, or 100% identity to nucleotides 41-43 of SEQ ID NO:3; a seventh region comprising a sequence having 100% identity to nucleotide 44 of SEQ ID NO:3; an eighth region having a length in the range of 2-5, or 3-4 nucleotides and comprising a sequence having 0%, 30% or greater, 60% or greater, 90% or greater, or 100% identity to nucleotides 45-47 of SEQ ID NO:3; a ninth region comprising a sequence having 75% or greater, 85% or greater, 90% or greater, 95% or greater, or 100% identity to nucleotides 48-52 of SEQ ID NO:3; a tenth region having a length in the range of 1 to 4, or 2-3 nucleotides and comprising a sequence having 0%, 50% or greater, or 100% identity to nucleotides 53-54 of SEQ ID NO:3; an eleventh region comprising a sequence having 60% or greater, or 100% identity to nucleotides 55-57 of SEQ ID NO:3; a twelfth region having a length in the range of 1 to 4, or 2-3 nucleotides and comprising a sequence having 0%, 50% or greater, or 100% identity to nucleotides 58-59 of SEQ ID NO:3; a thirteenth region having a length in the range of 1 to 4, or 2-3 nucleotides and comprising a sequence having 0%, 60% or greater, or 100% identity to nucleotides 60-62 of SEQ ID NO:3; wherein the second and eighth regions are at least partially based paried, and the fourth and sixth regions, and the tenth and twelfth regions are base-paired to each other. [0112] As another example, and with reference to SEQ ID NO:4 (AOBA-4) and Figure 12, the disclosure provides a binding molecule that includes a variant aptamer. The binding molecule includes an aptamer having a sequence including, in a 5’ to 3’ direction: a first region comprising a sequence having 75% or greater, 85% or greater, 90% or greater, 95% or greater, or 100% identity to nucleotides 1 to 13 of SEQ ID NO:4; a second region having a length in the range of 2-5, or 3-4 nucleotides and comprising a sequence having 0%, 30% or greater, 60% or greater, 90% or greater, or 100% identity to nucleotides 14-16 of SEQ ID NO:4; a third region comprising a sequence having 100% identity to nucleotide 17 of SEQ ID NO:4; a fourth region having a length in the range of 3-6, or 4-5 nucleotides and comprising a sequence having 0%, 25% or greater, 50% or greater, 75% or greater, or 100% identity to nucleotides 18-21 of SEQ ID NO:4; a fifth region comprising a sequence having 75% or greater, 85% or greater, 90% or greater, 95% or greater, or 100% identity to nucleotides 22-28 of SEQ ID NO:4; a sixth region having a length in the range of 3-6, or 4- 5 nucleotides and comprising a sequence having 0%, 25% or greater, 50% or greater, 75% or greater, or 100% identity to nucleotides 29-32 of SEQ ID NO:4; a seventh region having a length in the range of 2-5, or 3-4 nucleotides and comprising a sequence having 0%, 30% or greater, 60% or greater, 90% or greater, or 100% identity to nucleotides 33-35 of SEQ ID NO:4; an eighth region comprising a sequence having 75% or greater, 85% or greater, 90% or greater, 95% or greater, or 100% identity to nucleotides 36-62 of SEQ ID NO:4; wherein the second and seventh regions, and the fourth and sixth regions are base-paired to each other. [0113] As another example, and with reference to SEQ ID NO:5 (AOBA-5) and Figure 13, the disclosure provides a binding molecule that includes a variant aptamer. The binding molecule includes an aptamer having a sequence including, in a 5’ to 3’ direction: a first region comprising a sequence having 75% or greater, 85% or greater, 90% or greater, 95% or greater, or 100% identity to nucleotides 1 to 10 of SEQ ID NO:5; a second region having a length in the range of 6-9, or 7-8 nucleotides and comprising a sequence having 0%, 25% or greater, 50% or greater, 75% or greater, or 100% identity to nucleotides 11-17 of SEQ ID NO:5; a third region comprising a sequence having 75% or greater, 85% or greater, 90% or greater, 95% or greater, or 100% identity to nucleotides 18 to 28 of SEQ ID NO:5; a fourth region having a length in the range of 6-9, or 7-8 nucleotides and comprising a sequence having 0%, 25% or greater, 50% or greater, 75% or greater, or 100% identity to nucleotides 29-34 of SEQ ID NO:5; a fifth region comprising a sequence having 75% or greater, 85% or greater, 90% or greater, 95% or greater, or 100% identity to nucleotides 35- 40 of SEQ ID NO:5; a sixth region having a length in the range of 3-6, or 4-5 nucleotides and comprising a sequence having 0%, 25% or greater, 50% or greater, 75% or greater, or 100% identity to nucleotides 41-44 of SEQ ID NO:5; a seventh region comprising a sequence having 100% identity to nucleotide 45 of SEQ ID NO:5; an eighth region having a length in the range of 1-4, or 2-3 nucleotides and comprising a sequence having 0%, 50%, or 100% identity to nucleotides 46-47 of SEQ ID NO:5; a ninth region having a length in the range of 3-6, or 4-5 nucleotides and comprising a sequence having 0%, 25% or greater, 50% or greater, 75% or greater, or 100% identity to nucleotides 41-44 of SEQ ID NO:5; a tenth region having a length in the range of 1 to 4, or 2-3 nucleotides and comprising a sequence having 0%, 50% or greater, or 100% identity to nucleotides 53-54 of SEQ ID NO:5; an eleventh region comprising a sequence having 100% identity to nucleotide 55 of SEQ ID NO:5; a twelfth region having a length in the range of 3-6, or 4-5 nucleotides and comprising a sequence having 0%, 25% or greater, 50% or greater, 75% or greater, or 100% identity to nucleotides 56-59 of SEQ ID NO:5; a thirteenth region comprising a sequence having 75% or greater, 85% or greater, 90% or greater, 95% or greater, or 100% identity to nucleotides 60 to 62 of SEQ ID NO:5; wherein the second and fourth regions are at least partially based paired, the sixth and twelfth regions are at least partially based paired, and the eighth and tenth regions are base-paired to each other. [0114] As another example, and with reference to SEQ ID NO:6 (AOBA-6) and Figure 14, the disclosure provides a binding molecule that includes a variant aptamer. The binding molecule includes an aptamer having a sequence including, in a 5’ to 3’ direction: a first region comprising a sequence having 50% or greater, or 100% identity to nucleotides 1-2 of SEQ ID NO:6; a second region having a length in the range of 7-10, or 8-9 nucleotides and comprising a sequence having 0%, 20% or greater, 40% or greater, 60% or greater, 80% or greater, or 100% identity to nucleotides 3-10 of SEQ ID NO:6; a third region comprising a sequence having 75% or greater, 85% or greater, 90% or greater, 95% or greater, or 100% identity to nucleotides 11-24 of SEQ ID NO:6; a fourth region having a length in the range of 7-10, or 8-9 nucleotides and comprising a sequence having 0%, 20% or greater, 40% or greater, 60% or greater, 80% or greater, or 100% identity to nucleotides 25-32 of SEQ ID NO:6; a fifth region comprising a sequence having 75% or greater, 85% or greater, 90% or greater, 95% or greater, or 100% identity to nucleotides 33-43 of SEQ ID NO:6; a sixth region having a length in the range of 4-7, or 5-6 nucleotides and comprising a sequence having 0%, 20% or greater, 40% or greater, 60% or greater, 80% or greater, or 100% identity to nucleotides 44-48 of SEQ ID NO:6; a seventh region comprising a sequence having 75% or greater, 85% or greater, 90% or greater, 95% or greater, or 100% identity to nucleotides 49-53 of SEQ ID NO:6; an eighth region having a length in the range of 4-7, or 5-6 nucleotides and comprising a sequence having 0%, 20% or greater, 40% or greater, 60% or greater, 80% or greater, or 100% identity to nucleotides 54-58 of SEQ ID NO:6; a ninth region comprising a sequence having 75% or greater, 85% or greater, 90% or greater, 95% or greater, or 100% identity to nucleotides 59 to 62 of SEQ ID NO:6; wherein the second and fourth regions, and the sixth and eighth regions are at least partially based paired to each other. [0115] As another example, and with reference to SEQ ID NO:7 (AOBA-7) and Figure 15, the disclosure provides a binding molecule that includes a variant aptamer. The binding molecule includes an aptamer having a sequence including, in a 5’ to 3’ direction: a first region comprising a sequence having 75% or greater, 85% or greater, 90% or greater, 95% or greater, or 100% identity to nucleotides 1 to 27 of SEQ ID NO:7; a second region having a length in the range of 2-5, or 3-4 nucleotides and comprising a sequence having 0%, 30% or greater, 60% or greater, 90% or greater, or 100% identity to nucleotides 28-30 of SEQ ID NO:7; a third region comprising a sequence having 100% identity to nucleotide 31 of SEQ ID NO:7; a fourth region having a length in the range of 2-5, or 3-4 nucleotides and comprising a sequence having 0%, 30% or greater, 60% or greater, 90% or greater, or 100% identity to nucleotides 32-34 of SEQ ID NO:7; a fifth region comprising a sequence having 75% or greater, 85% or greater, 90% or greater, 95% or greater, or 100% identity to nucleotides 35-40 of SEQ ID NO:7; a sixth region having a length in the range of 2-5, or 3- 4 nucleotides and comprising a sequence having 0%, 30% or greater, 60% or greater, 90% or greater, or 100% identity to nucleotides 41-43 of SEQ ID NO:7; a seventh region comprising a sequence having 100% identity to nucleotide 44 of SEQ ID NO:3; an eighth region having a length in the range of 2-5, or 3-4 nucleotides and comprising a sequence having 0%, 30% or greater, 60% or greater, 90% or greater, or 100% identity to nucleotides 45-47 of SEQ ID NO:7; a ninth region comprising a sequence having 75% or greater, 85% or greater, 90% or greater, 95% or greater, or 100% identity to nucleotides 48-52 of SEQ ID NO:7; a tenth region having a length in the range of 1 to 4, or 2-3 nucleotides and comprising a sequence having 0%, 50% or greater, or 100% identity to nucleotides 53-54 of SEQ ID NO:7; an eleventh region comprising a sequence having 60% or greater, or 100% identity to nucleotides 55-57 of SEQ ID NO:7; a twelfth region having a length in the range of 1 to 4, or 2-3 nucleotides and comprising a sequence having 0%, 50% or greater, or 100% identity to nucleotides 58-59 of SEQ ID NO:7; and a thirteenth region having a length in the range of 1 to 4, or 2-3 nucleotides and comprising a sequence having 0%, 60% or greater, or 100% identity to nucleotides 60-62 of SEQ ID NO:7; wherein the second and eighth regions, the fourth and sixth regions, and the tenth and twelfth regions are base-paired to each other. [0116] Using a similar approach, aptamer variants of SEQ ID NOs:8-31 can be described. [0117] As another example, and with reference to SEQ ID NO:10 (AOBA-10) and Figure 18, the disclosure provides a binding molecule that includes a variant aptamer. The binding molecule includes an aptamer having a sequence including, in a 5’ to 3’ direction: a first region comprising a sequence having 0%, or 100% identity to nucleotide 1 of SEQ ID NO:10; a second region having a length in the range of 2-5, or 3-4 nucleotides and comprising a sequence having 0%, 30% or greater, 60% or greater, 90% or greater, or 100% identity to nucleotides 2-4 of SEQ ID NO:10; a third region comprising a sequence having 75% or greater, 85% or greater, 90% or greater, 95% or greater, or 100% identity to nucleotides 5-9 of SEQ ID NO:10; a fourth region having a length in the range of 2-5 or 3- 4 nucleotides and comprising a sequence having 0%, 30% or greater, 60% or greater, 90% or greater, or 100% identity to nucleotides 10-12 of SEQ ID NO:10; a fifth region comprising a sequence having 75% or greater, or 100% identity to nucleotides 13-16 of SEQ ID NO:10; a sixth region having a length in the range of 4-7 or 5-6 nucleotides and comprising a sequence having 0%, 20% or greater, 40% or greater, 60% or greater, 80% or greater, or 100% identity to nucleotides 17-21 of SEQ ID NO:10; a seventh region comprising a sequence having 75% or greater, or 100% identity to nucleotides 22-25 of SEQ ID NO:10; an eighth region having a length in the range of 4-7, or 5-6 nucleotides and comprising a sequence having 0%, 20% or greater, 40% or greater, 60% or greater, 80% or greater, or 100% identity to nucleotides 26-30 of SEQ ID NO:10; a ninth region comprising a sequence having 75% or greater, or 100% identity to nucleotides 31-33 of SEQ ID NO:10; a tenth region having a length in the range of 3-6 or 4-5 nucleotides and comprising a sequence having 0%, 25% or greater, 50% or greater, 75% or greater, or 100% identity to nucleotides 34-37 of SEQ ID NO:10; an eleventh region comprising a sequence having 75% or greater, 85% or greater, 90% or greater, 95% or greater, or 100% identity to nucleotides 38-54 of SEQ ID NO: 10; a twelfth region having a length in the range of 3-6 or 4-5 nucleotides and comprising a sequence having 0%, 25% or greater, 50% or greater, 75% or greater, or 100% identity to nucleotides 55-58 of SEQ ID NO:10; a thirteenth region comprising a sequence having 75% or greater, or 100% identity to nucleotides 59-62of SEQ ID NO:10; and wherein the second and fourth regions, the sixth and eighth regions, and the tenth and twelfth regions are base-paired to each other. [0118] As another example, and with reference to SEQ ID NO:11 (AOBA-11) and Figure 19, the disclosure provides a binding molecule that includes a variant aptamer. The binding molecule includes an aptamer having a sequence including, in a 5’ to 3’ direction: a first region comprising a sequence having 75% or greater, 85% or greater, 90% or greater, 95% or greater, or 100% identity to nucleotides 1-23 of SEQ ID NO:11; a second region having a length in the range of 2-5, or 3-4 nucleotides and comprising a sequence having 0%, 30% or greater, 60% or greater, 90% or greater, or 100% identity to nucleotides 24-26 of SEQ ID NO:11 ; a third region comprising a sequence having 0%, or 100% identity to nucleotide 27 of SEQ ID NO:11; a fourth region having a length in the range of 4-7, or 5-6 nucleotides and comprising a sequence having 0%, 20% or greater, 40% or greater, 60% or greater, 80% or greater, or 100% identity to nucleotides 28-32 of SEQ ID NO:11; a fifth region comprising a sequence having 75% or greater, 85% or greater, 90% or greater, 95% or greater, or 100% identity to nucleotides 33-41 of SEQ ID NO:11; a sixth region having a length in the range of 4-7, or 5-6 nucleotides and comprising a sequence having 0%, 20% or greater, 40% or greater, 60% or greater, 80% or greater, or 100% identity to nucleotides 42-46 of SEQ ID NO:11; a seventh region comprising a sequence having 0%, or 100% identity to nucleotide 47 of SEQ ID NO:11; an eighth region having a length in the range of 2-5, or 3-4 nucleotides and comprising a sequence having 0%, 30% or greater, 60% or greater, 90% or greater, or 100% identity to nucleotides 48-50 of SEQ ID NO:11; a ninth region comprising a sequence having 0%, or 100% identity to nucleotide 51 of SEQ ID NO:11; a tenth region having a length in the range of 1 to 4, or 2-3 nucleotides and comprising a sequence having 0%, 50% or greater, or 100% identity to nucleotides 52-53of SEQ ID NO:11 ; an eleventh region comprising a sequence having 75% or greater, 85% or greater, 90% or greater, 95% or greater, or 100% identity to nucleotides 54-58 of SEQ ID NO: 11 ; a twelfth region having a length in the range of 1 to 4, or 2-3 nucleotides and comprising a sequence having 0%, 50% or greater, or 100% identity to nucleotides 59-60 of SEQ ID NO:11; a thirteenth region comprising a sequence having a 50% or greater, or 100% identity to nucleotides 61-62 of SEQ ID NO:11; and wherein the second and eighth regions, the fourth and sixth, and the tenth and twelfth regions are base- paired to each other. [0119] As another example, and with reference to SEQ ID NO:12 (AOBA-12) and Figure 20, the disclosure provides a binding molecule that includes a variant aptamer. The binding molecule includes an aptamer having a sequence including, in a 5’ to 3’ direction: a first region comprising a sequence having 75% or greater, 85% or greater, 90% or greater, 95% or greater, or 100% identity to nucleotides 1-5 of SEQ ID NO: 12; a second region having a length in the range of 3-6, or 4-5 nucleotides and comprising a sequence having 0%, 25% or greater, 50% or greater, 75% or greater, or 100% identity to nucleotides 6-9 of SEQ ID NO: 12; a third region comprising a sequence having 75% or greater, 85% or greater, 90% or greater, 95% or greater, or 100% identity to nucleotides 10-15 of SEQ ID NO: 12; a fourth region having a length in the range of 3-6, or 4-5 nucleotides and comprising a sequence having 0%, 25% or greater, 50% or greater, 75% or greater, or 100% identity to nucleotides 16-19 of SEQ ID NO: 12; a fifth region comprising a sequence having 75% or greater, 85% or greater, 90% or greater, 95% or greater, or 100% identity to nucleotides 20-33 of SEQ ID NO: 12; a sixth region having a length in the range of 1 to 4, or 2-3 nucleotides and comprising a sequence having 0%, 50% or greater, or 100% identity to nucleotides 34-35 of SEQ ID NO: 12; a seventh region comprising a sequence having 0% or greater, or 100% identity to nucleotide 36 of SEQ ID NO: 12; an eighth region a length in the range of 1 to 4, or 2-3 nucleotides and comprising a sequence having 0%, 50% or greater, or 100% identity to nucleotides 37-38 of SEQ ID NO: 12; a ninth region comprising a sequence having 0% or greater, or 100% identity to nucleotide 39 of SEQ ID NO: 12; a tenth region having a length in the range of 1 to 3, or 1 or 2 nucleotides and comprising a sequence having 0%, or 100% identity to nucleotide 41 of SEQ ID NO: 12; an eleventh region comprising a sequence having 75% or greater, 85% or greater, 90% or greater, 95% or greater, or 100% identity to nucleotides 41-45 of SEQ ID NO: 12; a twelfth region having a length in the range of 1 to 3, or 1 or 2 nucleotides and comprising a sequence having 0%, or 100% identity to nucleotide 46 of SEQ ID NO: 12; a thirteenth comprising a sequence having 0% or greater, or 100% identity to nucleotide 47 of SEQ ID NO: 12; a fourteenth region having a length in the range of 1 to 4, or 2-3 nucleotides and comprising a sequence having 0%, 50% or greater, or 100% identity to nucleotides 48-49 of SEQ ID NO: 12; a fifteenth region comprising a sequence having 0% or greater, or 100% identity to nucleotide 50 of SEQ ID NO: 12; a sixteenth region having a length in the range of 1 to 4, or 2-3 nucleotides and comprising a sequence having 0%, 50% or greater, or 100% identity to nucleotides 51-52 of SEQ ID NO: 12; a seventeenth region comprising a sequence having a 75% or greater, 85% or greater, 90% or greater, 95% or greater, or 100% identity to nucleotides 53-62 of SEQ ID NO: 12; and wherein the second and fourth regions, the sixth and sixteenth regions, the eighth fourteenth regions, and the tenth and twelfth regions, are base-paired to each other. [0120] As another example, and with reference to SEQ ID NO:15 (AOBA-15) and Figure 23, the disclosure provides a binding molecule that includes a variant aptamer. The binding molecule includes an aptamer having a sequence including, in a 5’ to 3’ direction: a first region comprising a sequence having 75% or greater, 85% or greater, 90% or greater, 95% or greater, or 100% identity to nucleotides 1-6 of SEQ ID NO:15; a second region having a length in the range of 2-5 or 3-4 nucleotides and comprising a sequence having 0%, 30% or greater, 60% or greater, 90% or greater, or 100% identity to nucleotides 7-9 of SEQ ID NO:15; a third region comprising a sequence having 75% or greater, or 100% identity to nucleotides 10-13 of SEQ ID NO:15; a fourth region having a length in the range of 2-5, or 3-4 nucleotides and comprising a sequence having 0%, 30% or greater, 60% or greater, 90% or greater, or 100% identity to nucleotides 14-16 of SEQ ID NO:15; a fifth region comprising a sequence having 75% or greater, 85% or greater, 90% or greater, 95% or greater, or 100% identity to nucleotides 17-36 of SEQ ID NO:15; a sixth region comprising a sequence having 75% or greater, or 100% identity to nucleotides 37-39 of SEQ ID NO:15; a seventh region comprising a sequence having 0%, or 100% identity to nucleotide 40 of SEQ ID NO:15; an eighth region having a length in the range of 2-5, or 3- 4 nucleotides and comprising a sequence having 0%, 30% or greater, 60% or greater, 90% or greater, or 100% identity to nucleotides 41-43 of SEQ ID NO:15; a ninth region comprising a sequence having 75% or greater, 85% or greater, 90% or greater, 95% or greater, or 100% identity to nucleotides 44-49 of SEQ ID NO:15; a tenth region having a length in the range of 2-5, or 3-4 nucleotides and comprising a sequence having 0%, 30% or greater, 60% or greater, 90% or greater, or 100% identity to nucleotides 50-52 of SEQ ID NO:15; an eleventh region comprising a sequence having 50% or greater, or 100% identity to nucleotides 53-54 of SEQ ID NO: 15; a twelfth region having a length in the range of 1 to 4, or 2-3 nucleotides and comprising a sequence having 0%, 50% or greater, or 100% identity to nucleotides 55-57 of SEQ ID NO:15; and a thirteenth region comprising a sequence having 75% or greater, 85% or greater, 90% or greater, 95% or greater, or 100% identity to nucleotides 58-62 of SEQ ID NO:15; and wherein the second and fourth regions, the sixth and twelfth regions, and the eight and tenth and regions are base-paired to each other. [0121] As another example, and with reference to SEQ ID NO:17 (AOBA-17) and Figure 25, the disclosure provides a binding molecule that includes a variant aptamer. The binding molecule includes an aptamer having a sequence including, in a 5’ to 3’ direction: a first region comprising a sequence having 75% or greater, or 100% identity to nucleotides 1-4 of SEQ ID NO: 17; a second region having a length in the range of 3-6, or 4-5 nucleotides and comprising a sequence having 0%, 25% or greater, 50% or greater, 75% or greater, or 100% identity to nucleotides 5-8 of SEQ ID NO: 17; a third region comprising a sequence having 75% or greater, 85% or greater, 90% or greater, 95% or greater, or 100% identity to nucleotides 9-18 of SEQ ID NO: 17; a fourth region having a length in the range of 3-6, or 4-5 nucleotides and comprising a sequence having 0%, 25% or greater, 50% or greater, 75% or greater, or 100% identity to nucleotides 19-22 of SEQ ID NO: 17; a fifth region comprising a sequence having 50% or greater, or 100% identity to nucleotides 23-24 of SEQ ID NO: 17; a sixth region having a length in the range of 2-5, or 3-4 nucleotides and comprising a sequence having 0%, 30% or greater, 60% or greater, 90% or greater, or 100% identity to nucleotides 25-27 of SEQ ID NO: 17; a seventh region comprising a sequence having 75% or greater, or 100% identity to nucleotides 28-31 of SEQ ID NO: 17; an eighth region having a length in the range of 2-5, or 3-4 nucleotides and comprising a sequence having 0%, 30% or greater, 60% or greater, 90% or greater, or 100% identity to nucleotides 32-34 of SEQ ID NO: 17; a ninth region comprising a sequence having 75% or greater, 85% or greater, 90% or greater, 95% or greater, or 100% identity to nucleotides35- 48 of SEQ ID NO: 17; a tenth region having a length in the range of 2-5, or 3-4 nucleotides and comprising a sequence having 0%, 30% or greater, 60% or greater, 90% or greater, or 100% identity to nucleotides 49-51 of SEQ ID NO: 17; an eleventh region comprising a sequence having 75% or greater, 85% or greater, 90% or greater, 95% or greater, or 100% identity to nucleotides 52-56 of SEQ ID NO: 17; a twelfth region having a length in the range of 2-5, or 3-4 nucleotides and comprising a sequence having 0%, 30% or greater, 60% or greater, 90% or greater, or 100% identity to nucleotides 57-59 of SEQ ID NO: 17; a thirteenth region comprising a sequence having 75% or greater, or 100% identity to nucleotides 60-62 of SEQ ID NO: 17; and wherein the second and fourth regions, the sixth and the eighth regions, the tenth and twelfth are base-paired to each other. [0122] As another example, and with reference to SEQ ID NO:19 (AOBA-19) and Figure 27, the disclosure provides a binding molecule that includes a variant aptamer. The binding molecule includes an aptamer having a sequence including, in a 5’ to 3’ direction: a first region comprising a sequence having 75% or greater, 85% or greater, 90% or greater, 95% or greater, or 100% identity to nucleotides 1-5 of SEQ ID NO:19; a second region having a length in the range of 2-5, or 3-4 nucleotides and comprising a sequence having 0%, 30% or greater, 60% or greater, 90% or greater, or 100% identity to nucleotides 6-8 of SEQ ID NO:19; a third region comprising a sequence having 75% or greater, 85% or greater, 90% or greater, 95% or greater, or 100% identity to nucleotides 9-17 of SEQ ID NO:19; a fourth region having a length in the range of 2-5, or 3-4 nucleotides and comprising a sequence having 0%, 30% or greater, 60% or greater, 90% or greater, or 100% identity to nucleotides 18-20 of SEQ ID NO:19; a fifth region comprising a sequence having 75% or greater, 85% or greater, 90% or greater, 95% or greater, or 100% identity to nucleotides 21- 26 of SEQ ID NO:19; a sixth region having a length in the range of 2-5, or 3-4 nucleotides and comprising a sequence having 0%, 30% or greater, 60% or greater, 90% or greater, or 100% identity to nucleotides 27-29 of SEQ ID NO:19; a seventh region comprising a sequence having 75% or greater, 85% or greater, 90% or greater, 95% or greater, or 100% identity to nucleotides 30-45 of SEQ ID NO:19; an eighth region comprising a sequence having 75% or greater, or 100% identity to nucleotides 46-48 of SEQ ID NO:19; a ninth region comprising a sequence having 75% or greater, 85% or greater, 90% or greater, 95% or greater, or 100% identity to nucleotides 49-62 of SEQ ID NO:19; and wherein the second and fourth regions, the sixth and the eight regions are base-paired to each other. [0123] As another example, and with reference to SEQ ID NO:20 (AOBA-20) and Figure 28, the disclosure provides a binding molecule that includes a variant aptamer. The binding molecule includes an aptamer having a sequence including, in a 5’ to 3’ direction: a first region comprising a sequence having 75% or greater, 85% or greater, 90% or greater, 95% or greater, or 100% identity to nucleotides 1-15 of SEQ ID NO:20; a second region having a length in the range of 3-6, or 4-5 nucleotides and comprising a sequence having 0%, 25% or greater, 50% or greater, 75% or greater, or 100% identity to nucleotides 16- 19 of SEQ ID NO:20; a third region comprising a sequence having 75% or greater, 85% or greater, 90% or greater, 95% or greater, or 100% identity to nucleotides 20-25 of SEQ ID NO:20; a fourth region having a length in the range of 3-6, or 4-5 nucleotides and comprising a sequence having 0%, 25% or greater, 50% or greater, 75% or greater, or 100% identity to nucleotides 26-29 of SEQ ID NO:20; a fifth region comprising a sequence having 75% or greater, or 100% identity to nucleotides 30-33 of SEQ ID NO:20; a sixth region having a length in the range of 1 to 4, or 2-3 nucleotides and comprising a sequence having 0%, 50% or greater, or 100% identity to nucleotides 34-35 of SEQ ID NO:20; a seventh region comprising a sequence having 75% or greater, 85% or greater, 90% or greater, 95% or greater, or 100% identity to nucleotides 36-40 of SEQ ID NO:20; an eighth region having a length in the range of 1 to 4, or 2-3 nucleotides and comprising a sequence having 0%, 50% or greater, or 100% identity to nucleotides 41-42 of SEQ ID NO:20; a ninth region comprising a sequence having 75% or greater, 85% or greater, 90% or greater, 95% or greater, or 100% identity to nucleotides 43-51 of SEQ ID NO:20; a tenth region having a length in the range of 1 to 4, or 2-3 nucleotides and comprising a sequence having 0%, 50% or greater, or 100% identity to nucleotides 52-53 of SEQ ID NO:20; an eleventh region comprising a sequence having 75% or greater, 85% or greater, 90% or greater, 95% or greater, or 100% identity to nucleotides 54-58 of SEQ ID NO: 20; a twelfth region having a length in the range of 1 to 4, or 2-3 nucleotides and comprising a sequence having 0%, 50% or greater, or 100% identity to nucleotides 59-60 of SEQ ID NO:20; a thirteenth region comprising a sequence having 50% or greater, or 100% identity to nucleotides 61-62 of SEQ ID NO:20; and wherein the second and fourth regions, the sixth and eight regions, and the tenth and twelfth regions are base-paired to each other. [0124] As another example, and with reference to SEQ ID NO:21 (AOBA-21) and Figure 29, the disclosure provides a binding molecule that includes a variant aptamer. The binding molecule includes an aptamer having a sequence including, in a 5’ to 3’ direction: a first region comprising a sequence having 75% or greater, 85% or greater, 90% or greater, 95% or greater, or 100% identity to nucleotides 1-11 of SEQ ID NO:21; a second region having a length in the range of 1 to 4, or 2-3 nucleotides and comprising a sequence having 0%, 50% or greater, or 100% identity to nucleotides 12-13 of SEQ ID NO:21 ; a third region comprising a sequence having 75% or greater, 85% or greater, 90% or greater, 95% or greater, or 100% identity to nucleotides 14-18 of SEQ ID NO:21; a fourth region having a length in the range of 1 to 4, or 2-3 nucleotides and comprising a sequence having 0%, 50% or greater, or 100% identity to nucleotides 19-20 of SEQ ID NO:21; a fifth region comprising a sequence having 75% or greater, 85% or greater, 90% or greater, 95% or greater, or 100% identity to nucleotides 21-25 of SEQ ID NO:21; a sixth region having a length in the range of 3-6, or 4-5 nucleotides and comprising a sequence having 0%, 25% or greater, 50% or greater, 75% or greater, or 100% identity to nucleotides 26- 29 of SEQ ID NO:21; a seventh region comprising a sequence having 75% or greater, or 100% identity to nucleotides 30-32 of SEQ ID NO:21 ; an eighth region having a length in the range of 3-6, or 4-5 nucleotides and comprising a sequence having 0%, 25% or greater, 50% or greater, 75% or greater, or 100% identity to nucleotides 33-36 of SEQ ID NO:21; a ninth region comprising a sequence having 75% or greater, 85% or greater, 90% or greater, 95% or greater, or 100% identity to nucleotides37-45of SEQ ID NO:21 ; a tenth region having a length in the range of 2-5, or 3-4 nucleotides and comprising a sequence having 0%, 30% or greater, 60% or greater, 90% or greater, or 100% identity to nucleotides 46-48 of SEQ ID NO:21; an eleventh region comprising a sequence having 75% or greater, 85% or greater, 90% or greater, 95% or greater, or 100% identity to nucleotides 49-57 of SEQ ID NO: 21; a twelfth region having a length in the range of 2-5, or 3-4 nucleotides and comprising a sequence having 0%, 30% or greater, 60% or greater, 90% or greater, or 100% identity to nucleotides 58-60 of SEQ ID NO:21 ; a thirteenth region comprising a sequence having 50% or greater, or 100% identity to nucleotides 61-62 of SEQ ID NO:21; and wherein the second and fourth regions, the sixth and the eighth regions, the tenth and twelfth are base-paired to each other. [0125] As another example, and with reference to SEQ ID NO:22 (AOBA-22) and Figure 30, the disclosure provides a binding molecule that includes a variant aptamer. The binding molecule includes an aptamer having a sequence including, in a 5’ to 3’ direction: a first region comprising a sequence having 0%, or 100% identity to nucleotide 1 of SEQ ID NO: 22; a second region having a length in the range of 3-6, or 4-5 nucleotides and comprising a sequence having 0%, 25% or greater, 50% or greater, 75% or greater, or 100% identity to nucleotides 2-5 of SEQ ID NO: 22; a third region comprising a sequence having 75% or greater, 85% or greater, 90% or greater, 95% or greater, or 100% identity to nucleotides 6-10 of SEQ ID NO: 22; a fourth region having a length in the range of 3-6, or 4-5 nucleotides and comprising a sequence having 0%, 25% or greater, 50% or greater, 75% or greater, or 100% identity to nucleotides 11-14of SEQ ID NO: 22; a fifth region comprising a sequence having 75% or greater, 85% or greater, 90% or greater, 95% or greater, or 100% identity to nucleotides 15-53 of SEQ ID NO of SEQ ID NO: 22; a sixth region having a length in the range of 1 to 4, or 2-3 nucleotides and comprising a sequence having 0%, 50% or greater, or 100% identity to nucleotides 54-55 of SEQ ID NO: 22; a seventh region comprising a sequence having 75% or greater, or 100% identity to nucleotides 56-59 of SEQ ID NO: 22; an eighth region having a length in the range of 1 to 4, or 2-3 nucleotides and comprising a sequence having 0%, 50% or greater, or 100% identity to nucleotides 60-61 of SEQ ID NO: 22; a ninth region comprising a sequence having 0%, or 100% identity to nucleotide 62 of SEQ ID NO: 22; and wherein the second and fourth regions, and the sixth and eighth regions are base-paired to each other. [0126] As another example, and with reference to SEQ ID NO:23 (AOBA-23) and Figure 31, the disclosure provides a binding molecule that includes a variant aptamer. The binding molecule includes an aptamer having a sequence including, in a 5’ to 3’ direction: a first region comprising a sequence having 50% or greater, or 100% identity to nucleotides 1-2 of SEQ ID NO:23; a second region having a length in the range of 2-5, or 3-4 nucleotides and comprising a sequence having 0%, 30% or greater, 60%, 90% or greater, or 100% identity to nucleotides 3-5 of SEQ ID NO:23; a third region comprising a sequence having 0%, or 100% identity to nucleotide 6 of SEQ ID NO:23; a fourth region having a length in the range of 4-7, or 5-6 nucleotides and comprising a sequence having 0%, 20% or greater, 40% or greater, 60% or greater, 80% or greater, or 100% identity to nucleotides 7-11 of SEQ ID NO:23; a fifth region comprising a sequence having 75% or greater, or 100% identity to nucleotides 12-15 of SEQ ID NO:23; a sixth region having a length in the range of 4-7, or 5-6 nucleotides and comprising a sequence having 0%, 20% or greater, 40% or greater, 60% or greater, 80% or greater, or 100% identity to nucleotides 16-20 of SEQ ID NO: 23; a seventh region comprising a sequence having 75% or greater, or 100% identity to nucleotides 21-23 of SEQ ID NO:23; an eighth region having a length in the range of 2- 5, or 3-4 nucleotides and comprising a sequence having 0%, 30% or greater, 60% or greater, 90% or greater, or 100% identity to nucleotides 24-26 of SEQ ID NO:23; a ninth region comprising a sequence having 75% or greater, or 100% identity to nucleotides 27-29 of SEQ ID NO:23 ; a tenth region having a length in the range of 2-5, or 3-4 nucleotides and comprising a sequence having 0%, 30% or greater, 60% or greater, 90% or greater, or 100% identity to nucleotides 30-32 of SEQ ID NO:23; an eleventh region having a length in the range of 3-6, or 4-5 nucleotides and comprising a sequence having 0%, 25% or greater, 50% or greater, 75% or greater, or 100% identity to nucleotides 33-36 of SEQ ID NO: 23; a twelfth region comprising a sequence having 75% or greater, or 100% identity to nucleotides 37-40 of SEQ ID NO:23; a thirteenth region having a length in the range of 3-6, or 4-5 nucleotides and comprising a sequence having 0%, 25% or greater, 50% or greater, 75% or greater, or 100% identity to nucleotides 41-44 of SEQ ID NO:23; a fourteenth region comprising a sequence having 0%, or 100% identity to nucleotide 45 of SEQ ID NO:23; a fifteenth region having a length in the range of 2-5, or 3-4 nucleotides and comprising a sequence having 0%, 30% or greater, 60% or greater, 90% or greater, or 100% identity to nucleotides 46-48 of SEQ ID NO: 23; a sixteenth region comprising a sequence having 75% or greater, or 100% identity to nucleotides 49-52 of SEQ ID NO:23; a seventeenth region having a length in the range of 1 to 4, or 2-3 nucleotides and comprising a sequence having 0%, 50% or greater, or 100% identity to nucleotides 53-54 of SEQ ID NO:23; an eighteenth region comprising a sequence having 75% or greater, or 100% identity to nucleotides 55-57 of SEQ ID NO: 23; a nineteenth region having a length in the range of 1 to 4, or 2-3 nucleotides and comprising a sequence having 0%, 50% or greater, or 100% identity to nucleotides 58-59 of SEQ ID NO:23; a twentieth region comprising a sequence having a 75% or greater, or 100% identity to nucleotides 61-62 of SEQ ID NO:23; and wherein the second and eighth regions, the fourth and the sixth regions are at least partially based paired, and the tenth and fifteenth regions, the eleventh and thirteenth regions, and the seventeenth and nineteenth regions are base-paired to each other. [0127] As another example, and with reference to SEQ ID NO:25 (AOBA-25) and Figure 33, the disclosure provides a binding molecule that includes a variant aptamer. The binding molecule includes an aptamer having a sequence including, in a 5’ to 3’ direction: a first region having a length in the range of 3-6, or 4-5 nucleotides and comprising a sequence having 0%, 25% or greater, 50% or greater, 75% or greater, or 100% identity to nucleotides 1-4 of SEQ ID NO:25; a second region comprising a sequence having 75% or greater, 85% or greater, 90% or greater, 95% or greater, or 100% identity to nucleotides 5- 9 of SEQ ID NO:25 ; a third region having a length in the range of 3-6, or 4-5 nucleotides and comprising a sequence having 0%, 25% or greater, 50% or greater, 75% or greater, or 100% identity to nucleotides 10-13 of SEQ ID NO:25 ; a fourth region comprising a sequence having 75% or greater, 85% or greater, 90% or greater, 95% or greater, or 100% identity to nucleotides 14-23 of SEQ ID NO:25; a fifth region having a length in the range of 6-9, or 7-8 nucleotides and comprising a sequence having 0%, 15% or greater, 29% or greater, 43% or greater, 58% or greater, 72% or greater, 86% or greater, or 100% identity to nucleotides 24-30 of SEQ ID NO:25; a sixth region comprising a sequence having 0%, or 100% identity to nucleotide 31 of SEQ ID NO:25; a seventh region having a length in the range of 1 to 4, or 2-3 nucleotides and comprising a sequence having 0%, 50% or greater, or 100% identity to nucleotides 32-33 of SEQ ID NO:25 ; an eighth region comprising a sequence having 0%, or 100% identity to nucleotide 34 of SEQ ID NO:25; a ninth region having a length in the range of 3-6, or 4-5 nucleotides and comprising a sequence having 0%, 25% or greater, 50% or greater, 75% or greater, or 100% identity to nucleotides 35-38 of SEQ ID NO:25; a tenth region comprising a sequence having 75% or greater, 85% or greater, 90% or greater, 95% or greater, or 100% identity to nucleotides 39-46 of SEQ ID NO:25; an eleventh region having a length in the range of 3- 6, or 4-5 nucleotides and comprising a sequence having 0%, 25% or greater, 50% or greater, 75% or greater, or 100% identity to nucleotides 47-50 of SEQ ID NO: 25; a twelfth region having a length in the range of 1 to 4, or 2-3 nucleotides and comprising a sequence having 0%, 50% or greater, or 100% identity to nucleotides 51-52 of SEQ ID NO:25 ; a thirteenth region comprising a sequence having 0%, or 100% identity to nucleotide 53 of SEQ ID NO:25; a fourteenth region having a length in the range of 6-9, or 7-8 nucleotides and comprising a sequence having 0%, 15% or greater, 29% or greater, 43% or greater, 58% or greater, 72% or greater, 86% or greater, or 100% identity to nucleotides 54-60 of SEQ ID NO:25; a fifteenth region comprising a sequence having 50% or greater, or 100% identity to nucleotides 61-62 of SEQ ID NO: 25; and wherein the first and third regions, the fifth and fourteenth regions, the seventh and twelfth regions, and the ninth and eleventh regions are base-paired to each other. [0128] As another example, and with reference to SEQ ID NO:28 (AOBA-28) and Figure 36, the disclosure provides a binding molecule that includes a variant aptamer. The binding molecule includes an aptamer having a sequence including, in a 5’ to 3’ direction: a first region comprising a sequence having 0%, or 100% identity to nucleotide 1 of SEQ ID NO: 28; a second region having a length in the range of 2-5, or 3-4 nucleotides and comprising a sequence having 0%, 30% or greater, 60% or greater, 90% or greater, or 100% identity to nucleotides 2-4 of SEQ ID NO: 28; a third region comprising a sequence having 75% or greater, or 100% identity to nucleotides 5-7 of SEQ ID NO: 28; a fourth region having a length in the range of 2-5, or 3-4 nucleotides and comprising a sequence having 0%, 30% or greater, 60% or greater, 90% or greater, or 100% identity to nucleotides 8-10 of SEQ ID NO: 28; a fifth region comprising a sequence having 75% or greater, or 100% identity to nucleotides 11-14 of SEQ ID NO: 28; a sixth region having a length in the range of 3-6, or 4-5 nucleotides and comprising a sequence having 0%, 25% or greater, 50% or greater, 75% or greater, or 100% identity to nucleotides 15-18 of SEQ ID NO: 28; a seventh region comprising a sequence having 75% or greater, or 100% identity to nucleotides 19-22 of SEQ ID NO: 28; an eighth region having a length in the range of 3-6, or 4-5 nucleotides and comprising a sequence having 0%, 25% or greater, 50% or greater, 75% or greater, or 100% identity to nucleotides 23-26 of SEQ ID NO: 28; a ninth region comprising a sequence having 75% or greater, 85% or greater, 90% or greater, 95% or greater, or 100% identity to nucleotides 27-39 of SEQ ID NO: 28; a tenth region having a length in the range of 1 to 4, or 2-3 nucleotides and comprising a sequence having 0%, 50% or greater, or 100% identity to nucleotides 40-41 of SEQ ID NO: 28; an eleventh region comprising a sequence having 75% or greater, or 100% identity to nucleotides 42-45 of SEQ ID NO: 28; a twelfth region having a length in the range of 1 to 4, or 2-3 nucleotides and comprising a sequence having 0%, 50% or greater, or 100% identity to nucleotides 46-47 of SEQ ID NO: 28; a thirteenth region comprising a sequence having a 75% or greater, or 100% identity to nucleotides 48- 50 of SEQ ID NO: 28;a fourteenth region having a length in the range of 2-5, or 3-4 nucleotides and comprising a sequence having 0%, 30% or greater, 60% or greater, 90% or greater, or 100% identity to nucleotides 51-53 of SEQ ID NO: 28; a fifteenth region comprising a sequence having 75% or greater, or 100% identity to nucleotides 54-57 of SEQ ID NO: 28; a sixteenth region having a length in the range of 2-5, or 3-4 nucleotides and comprising a sequence having 0%, 30% or greater, 60% or greater, 90% or greater, or 100% identity to nucleotides 58-60 of SEQ ID NO: 28; a seventeenth region comprising a sequence having a 50% or greater, or 100% identity to nucleotides 61-62 of SEQ ID NO: 28; and wherein the second and fourth regions, the sixth and eight regions, the tenth and twelfth regions, and the fourteenth and sixteenth regions are base-paired to each other. [0129] As another example, and with reference to SEQ ID NO:30 (AOBA-30) and Figure 38, the disclosure provides a binding molecule that includes a variant aptamer. The binding molecule includes an aptamer having a sequence including, in a 5’ to 3’ direction: a first region comprising a sequence having 75% or greater, 85% or greater, 90% or greater, 95% or greater, or 100% identity to nucleotides 1-14 of SEQ ID NO:30; a second region having a length in the range of 4-7, or 5-6 nucleotides and comprising a sequence having 0%, 20% or greater, 40% or greater, 60% or greater, 80% or greater, or 100% identity to nucleotides 15-19 of SEQ ID NO:30; a third region comprising a sequence having 75% or greater, 85% or greater, 90% or greater, 95% or greater, or 100% identity to nucleotides 20- 24 of SEQ ID NO:30; a fourth region having a length in the range of 4-7, or 5-6 nucleotides and comprising a sequence having 0%, 20% or greater, 40% or greater, 60% or greater, 80% or greater, or 100% identity to nucleotides 25-29 of SEQ ID NO:30; a fifth region comprising a sequence having 75% or greater, 85% or greater, 90% or greater, 95% or greater, or 100% identity to nucleotides 30-37 of SEQ ID NO:30; a sixth region having a length in the range of 5-8, or 6-7 nucleotides and comprising a sequence having 0%, 17% or greater, 34% or greater, 50% or greater, 67% or greater, 84% or greater, or 100% identity to nucleotides 38-43 of SEQ ID NO:30; a seventh region comprising a sequence having 75% or greater, 85% or greater, 90% or greater, 95% or greater, or 100% identity to nucleotides 44-56 of SEQ ID NO:30; an eighth region having a length in the range of 5-8, or 6-7 nucleotides and comprising a sequence having 0%, 17% or greater, 34% or greater, 50% or greater, 67% or greater, 84% or greater, or 100% identity to nucleotides 57-62 of SEQ ID NO:30; and wherein the second and fourth regions are at least partially based paired, and the sixth and the eighth regions are base-paired to each other. [0130] As another example, and with reference to SEQ ID NO:31 (AOBA-31) and Figure 39, the disclosure provides a binding molecule that includes a variant aptamer. The binding molecule includes an aptamer having a sequence including, in a 5’ to 3’ direction: a first region comprising a sequence having 75% or greater, 85% or greater, 90% or greater, 95% or greater, or 100% identity to nucleotides 1-10 of SEQ ID NO:31; a second region having a length in the range of 2-5, or 3-4 nucleotides and comprising a sequence having 0%, 30% or greater, 60% or greater, 90% or greater, or 100% identity to nucleotides 11-13 of SEQ ID NO:31; a third region comprising a sequence having 75% or greater, or 100% identity to nucleotides 14-17 of SEQ ID NO:31; a fourth region having a length in the range of 2-5, or 3-4 nucleotides and comprising a sequence having 0%, 30% or greater, 60% or greater, 90% or greater, or 100% identity to nucleotides 18-20 of SEQ ID NO:31; a fifth region comprising a sequence having 75% or greater, or 100% identity to nucleotides 21-23 of SEQ ID NO:31; a sixth region having a length in the range of 5-8, or 6-7 nucleotides and comprising a sequence having 0%, 17% or greater, 34% or greater, 50% or greater, 67% or greater, 84% or greater, or 100% identity to nucleotides 24-29 of SEQ ID NO:31; a seventh region comprising a sequence having 75% or greater, 85% or greater, 90% or greater, 95% or greater, or 100% identity to nucleotides 30-34 of SEQ ID NO:31; an eighth region having a length in the range of 5-8, or 6-7 nucleotides and comprising a sequence having 0%, 17% or greater, 34% or greater, 50% or greater, 67% or greater, 84% or greater, or 100% identity to nucleotides 35-40 of SEQ ID NO:31; a ninth region comprising a sequence having 75% or greater, 85% or greater, 90% or greater, 95% or greater, or 100% identity to nucleotides 41-62 of SEQ ID NO:31; and wherein the second and fourth regions are base-paired to each other, and the sixth and the eight regions are at least partially based paired to each other. [0131] Variant aptamers can be designed, generated, and tested according to the disclosure according techniques known in the art. Solid phase synthesis of oligonucleotides using phosphoramidite-based procedures is well-known and typically used to synthesize oligonucleotides up to about 120 in length. (Roy S., Caruthers M. Synthesis of DNA/RNA and their analogs via phosphoramidite and H-phosphonate chemistries. Molecules 18 14268–14284, 2013; Kosuri S., Church G. M. Large-scale de novo DNA synthesis: technologies and applications. Nat. Methods 11499–507, 2014. In some embodiments, variants can be generated by directed evolution and then isolated using art-known methods such as described in references like Sanger et al. (1991) Gene 97(1), 119-123; Link et al. (2007) Nature Reviews 5(9), 680-688; and Ghadessy et al. (2001) Proc Natl Acad Sci USA 98(8) 4552-4557. Using any of the aptamer sequences according to SEQ ID NOs:1-32, one skill in the art could generate a large number of nucleotide variants having a specified identity to the starting aptamer sequences (for example, variant sequences having 75% or greater, 80% or greater, 85% or greater, 90% or greater, 95% or greater, or 98% or greater identity to any one of SEQ ID NOs:1-32) and test the variants for binding to the desired antigen, such as an AO antigen or a PP antigen. [0132] Nucleic acid sequences including the aptamers of the disclosure can also be generated and manipulated according to molecular biology protocols using standard techniques known in the art (see, e.g., Sambrook and Russel (2006) Condensed Protocols from Molecular Cloning: A Laboratory Manual, Cold Spring Harbor Laboratory Press, ISBN-10: 0879697717; Ausubel et al. (2002) Short Protocols in Molecular Biology, 5th ed., Current Protocols, ISBN-10: 0471250929; Sambrook and Russel (2001) Molecular Cloning: A Laboratory Manual, 3d ed., Cold Spring Harbor Laboratory Press, ISBN-10: 0879695773; Elhai, J. and Wolk, C. P.1988. Methods in Enzymology 167, 747-754; Studier (2005) Protein Expr Purif.41(1), 207-234; Gellissen, ed. (2005) Production of Recombinant Proteins: Novel Microbial and Eukaryotic Expression Systems, Wiley-VCH, ISBN-10: 3527310363; Baneyx (2004) Protein Expression Technologies, Taylor & Francis, ISBN-10: 0954523253). [0133] The AO or PP antigen-binding aptamer can optionally be described in terms of the binding affinity to the AO or PP antigen. In some embodiments, the AO or PP antigen- binding aptamer has an equilibrium constant (Kd) of about 1 pM up to about 10.0 μΜ; about 1 pM up to about 1.0 μΜ; about 1 pM up to about 100 nM; about 100 pM up to about 10.0 μΜ; about 100 pM up to about 1.0 μΜ; about 100 pM up to about 100 nM; or about 1.0 nM up to about 10.0 μΜ; about 1.0 nM up to about 1.0 μΜ; about 1 nM up to about 200 nM; about 1.0 nM up to about 100 nM; about 500 nM up to about 10.0 μΜ; or about 500 nM up to about 1.0 μΜ. [0134] Binding compounds that include the disclosure's AO or PP antigen-binding aptamers can be used as analytical tools in various assay formats. For example, the aptamer- based AO or PP antigen-binding compounds can be used in solution-based assays or attached to a support surface for immobilized assays. [0135] Aptamer usage in diagnostics is well known (for example, see, Jayasena 1999 Clin Chem 45:1628-1650; Mascini 2009 Aptamers in Bioanalysis, Wiley-Interscience, ISBN-10: 0470148306). Aptamer-based binding molecules of the disclosure can be used in two-site binding assays, also known as sandwich assays. Generally, in this technique, an AO or PP antigen is sandwiched between a capture ligand and a detector ligand, with at least one of the ligands being the aptamer-based binding molecule. In some modes of practice, an aptamer-based binding molecule specific for AO or PP recognizes the AO or PP antigen, and another aptamer-based binding molecule specific for AO or PP that is coupled to a fluorophore is used for binding and detection. The assay can be performed in solution without immobilization of either aptamer-based binding molecule. [0136] Aptamer-based binding molecules specific for AO or PP can also be immobilized on solid supports such as beads. Such solid support immobilized aptamers can also be used in sandwich assay formats to capture the AO or PP antigen. [0137] Aptamer-based binding molecules specific for AO or PP can also be immobilized on other types of surfaces suitable for diagnostic applications, such as nanoparticles made from polymeric materials, metal nanoparticles, including paramagnetic nanoparticles, gold films, gold particles, silicates, silicon oxides, quantum dots, carbon nanotubes, and carbohydrates (for example, see Famulok et al. 2007 Chemical Reviews 107(9), 3715-3743; and Lee et al.2010 Advanced Drug Delivery Systems 62(6), 592-605). Aptamer-based binding molecules specific for AO or PP can be used in fluorescent, colorimetric, magnetic resonance imaging, or electrochemical sensor detection methods (for example, see Lee et al. Advanced Drug Delivery Systems 62:592-605, 2010). An aptamer described herein can be used to detect a target molecule in a sample. [0138] In some aspects of the disclosure, the aptamer-based binding molecules specific for AO or PP are used in a lateral flow assay (LFA). An aptamer-based LFAs include an antigen-aptamer binding reaction combined with lateral fluid flow through a membrane. LFAs can utilize a sandwich format, where two aptamer probes are used for target immobilization and detection. In another embodiment, the LFA arrangement is the competitive format, in which the native antigen competes with an antigen immobilized on a solid support or an ssDNA strand complementary to the aptamer. [0139] The disclosure also provides kits with an aptamer-based binding molecule specific for AO or PP. Kits can facilitate methods of detection of AO or PP. Kit components, including the aptamer-containing binding molecules of the disclosure, detection reagents, and optionally other materials, can be packaged in separate containers and admixed immediately before use. If desired, such packaging of the components can be presented in a pack or dispenser device, which may contain one or more unit dosage forms containing the composition. The pack may, for example, comprise metal or plastic foil, such as a blister pack. Such packaging of the components separately can also, in certain instances, permit long-term storage without losing the activity of the components. Kits may also include reagents in separate containers. Exemplary containers include test tubes, vials, flasks, bottles, syringes, and the like. In embodiments, kits can be supplied with instructional materials, such as directions for kit use that are printed on paper or other substrates or may be supplied as an electronically readable medium, such as a floppy disc, mini-CD-ROM, CD-ROM, DVD-ROM, Zip disc, videotape, audio tape, and the like. Alternatively, a user may be directed to an Internet website specified by the manufacturer or distributor of the kit. [0140] Another aspect of the disclosure relates to using aptamers and therapeutic components for treating infection in marine organisms. In particular, the disclosure also provides conjugates of aptamer-based AO or PP antigen-binding compounds and one or more therapeutic agent(s). Of particular use are therapeutic agents, such as anti-parasitic drugs, that can be used to treat AO or PP infections in marine organisms and, more particularly, fish in aquaculture. Information regarding considerations for the use of antiparasitic drugs in aquaculture is available (see, for example, Shinn, A.P., and Bron, J.E., Considerations for the use of antiparasitic drugs in aquaculture, Ed. (s): Brian Austin, In Woodhead Publishing Series in Food Science, Technology and Nutrition, Infectious Disease in Aquaculture, Woodhead Publishing, 2012, pages 190-217; and Orobets, V., et al., IOP Conf. Ser.: Earth Environ. Sci.403012065, 2019). [0141] Antiparasitic compounds include pyrethroids, cypermethrin, deltamethrin, and other antiparasitics such as praziquantel, mebendazole, albendazole, ivermectin, and levamisole. Other therapeutic agents might be helpful if the marine organism has a secondary infection. In these cases, other therapeutic agents may be used, including organophosphates, benzoylureas, neonicotinoids, amidines, phenols, imidazoles, chloramine-T, methylene blue, beta-lactams, aminoglycosides, tetracyclines, macrolides, chloramphenicol, sulfonamides, potentiated sulfonamides, nitrofurans, quinolones, and fluoroquinolones. See, for example, WO2022087757A1. [0142] Although some of the examples discussed herein are discussed in terms of rmAbs, it is to be understood that another affinity reagent may be used while preserving the advantages and functionality of the disclosure as described herein. [0143] Thus, the above-described losses from velvet disease may be mitigated by using rmAbs, or another affinity reagent, selected to provide early detection of AO and PP (using, e.g., an RDT employing at least one conjugated (detection) rmAb or other affinity reagents, and at least one immobilized (capture) rmAb, or other affinity reagents) to test waters or fish present in, or to be introduced into, aquaculture fish farms. Doing so can prevent infection or reinfection and permit effective treatment and control before widespread disease occurs. [0144] According to its manufacturer, the HuCAL Human Combinatorial Antibody Libraries from BioRad Laboratories, Inc. are designed to select and generate “highly specific, fully human, recombinant monoclonal antibodies in Fab and full immunoglobulin f.”mat.” However, rather than using HuCAL to generate fully human antibodies, the library may generate rmAbs for AO, PP, or AO and PP detection. Doing so does not require the use of animals and can generate valuable rmAbs in less than 12 weeks. In contrast to traditional pAbs and mAbs, HuCAL rmAbs are developed in vitro, and production occurs in the bacteria E. coli. This can provide a continuous source of Abs, unlike in vivo-derived Abs. Further, using the HuCAL library and rmAb technology can optimize the binding of dinospore and trophont Ags, a distinct advantage over traditional Ab development technology. HuCAL rmAbs may provide enhanced detection for a plurality of parasite life stages, resulting in a more thorough and sensitive screening method for both the trophonts in infected fish and the trophonts and dinospores in tank water. [0145] Referring to Fig. 1, representative system 100 for processing and determining the presence of velvet disease is shown. Automated instrument 101 supports a microtiter plate 102 containing sample wells 104 and is positioned atop movable stage 106. Once loaded with samples, stage 106 passes into housing 108, where incubation, washing, antibody addition, and absorbance measurement are performed. Control of instrument 101 can be performed, and the results for selected samples can be displayed using touch panel 110. The results may be stored and processed for analysis using a suitable engine. The term engine as used herein is defined as a real-world device, component, or arrangement of components implemented using hardware, such as by an application-specific integrated circuit (ASIC) or field-programmable gate array (FPGA), for example, or as a combination of hardware and software, such as by a microprocessor system and a set of program instructions that adapt the engine to implement the desired functionality, which while being executed may transform a microprocessor system into a special-purpose device. The measurement mentioned above may be stored within instrument 101, in a nearby or networked separate storage location (not shown in Fig. 1), or remotely stored using cloud storage facility 112. The engine mentioned above may reside within instrument 101, within a nearby or networked separate processing device (not shown in Fig.1), or may be remotely processed for analysis using, for example, a remote engine and processor 114. [0146] A block diagram 200 of steps employed in the disclosed method is shown in Fig. 2. A sample is collected 202 from water or a subject (e.g., a marine or freshwater fish) and optionally processed 204 to obtain release AO or PP organisms into the sampling solution. The sample is optionally transported 206 to a measurement instrument where measurements are obtained 208 to determine the presence of velvet disease. The measurements are stored 210 along with other previously or subsequently stored measurements for samples from the same population or region, using, for example, onboard, nearby, networked, or cloud storage. The stored measurements are analyzed 212 using, for example, onboard, nearby, networked or cloud computing. Based on analysis 212, an alternative 214 is followed, namely to delay or forego 216 any introduction of water or fish into a facility or any harvest, transport, or sale of fish from such facility for a given time and to instead continue monitoring or treatment of such fish, or to permit harvest 218, transport, or sale of the fish. [0147] A block diagram 300 demonstrating the general principles of the disclosed RDT biosensor assay device is shown in Fig. 3. A biosensor element containing one or more conjugated (detection) rmAbs and one or more immobilized (capture) rmAbs that are cross- reactive with one or more AO or PP antigens, is present in the assay device. In one embodiment, the capture rmAbs is immobilized 302 and treated or applied to the surface of sensor 304 on support. The capture rmAbs antibodies may be immobilized on sensor 304 by a measure such as absorption, entrapment, covalent coupling, affinity, binding proteins, chemical binding to polypeptide strands, or any other binding method. The binding method may be selected and configured to optimize exposure of the paratope after binding to permit unimpaired antibody-antigen complex formation. In embodiments, the capture rAbs may be self-immobilizing. The conjugated (detection) rmAbs are also bound to the support or particles that can migrate along the support. [0148] In another embodiment, the conjugated (detection) rmAbs are immobilized on sensor 304, and the capture rmAbs are also bound to the support or are bound to particles that can migrate along the support. [0149] For the various embodiments mentioned above, a target analyte, e.g., a sample containing AO or PP organisms, interacts 306 with the biosensor element (viz., the detection and capture rmAbs) to cause analyte recognition 308 and conversion to a signal by transducer 310. The resulting signal may depend upon the nature of the biosensor employed (e.g., an electrochemical, electronic, optical, piezoelectric, gravimetric, pyroelectric, or another suitable biosensor). The signal is amplified 312 and converted to a readout 314, e.g., converted to a numerical output using an algorithm, and the readout is displayed 316. Depending on the needs of the user and the system, the output data 316 may be used as feedback to improve the sensor and improve the selection of the biosensor components 302. Results may be cross-analyzed for verification with a standard or from another well-known assay, such as ELISA. [0150] A block diagram 400 demonstrating a detection process for the disclosed biosensor is shown in Fig.4. A transducer 402 may be prepared for biosensor function by applying a surface treatment 404 containing a mixture 406 (and in some embodiments not shown in Fig.4, successive layers) of those mentioned above immobilized or particle-bound detection rmAbs and capture rmAbs. AO or PP organisms 408 interact with the rmAbs 406, producing a biosignal 410, which is converted into an electrical signal 412 by the transducer 402. Transducer 402 may use various physicochemical processes to transform the biosignal 410. For example, transducer 402 may be optical, piezoelectric, electrochemical, electrochemiluminescent, etc. After amplification and conversion, signal 412 generates a display output of 414. [0151] The disclosed analysis may be performed using a variety of engines, each of which is constructed, programmed, configured, or otherwise adapted to carry out a function or set of functions autonomously. An engine can also be implemented as a combination of the two, with certain functions facilitated by hardware alone and other functions facilitated by a combination of hardware and software. In certain implementations, at least a portion, and in some cases, all, of an engine can be executed on the processor(s) of one or more computing platforms that are made up of hardware (e.g., one or more processors, data storage devices such as memory or drive storage, input/output facilities such as network interface devices, video devices, keyboard, mouse or touchscreen devices, etc.) that execute an operating system, system programs, and application programs, while also implementing the engine using multitasking, multithreading, distributed (e.g., cluster, peer-peer, cloud, etc.) processing where appropriate, or other such techniques. Accordingly, each engine may be realized in various physically realizable configurations and should generally not be limited to any implementation discussed or exemplified herein unless such limitations are expressly called out. In addition, an engine can be composed of more than one sub-engine, each of which can be regarded as an engine in its own right. An engine or a variety of engines may correspond to a defined autonomous functionality; however, it should be understood that in other contemplated embodiments, each functionality can be distributed to more than one engine. Likewise, in other contemplated embodiments, multiple defined functionalities may be implemented by a single engine that performs those multiple functions, possibly alongside other functions, or distributed differently among a set of engines than specifically discussed herein. [0152] Various embodiments of the disclosed system, and the corresponding methods of configuring and operating the disclosed system, may be performed using cloud computing, client-server, or other networked environments, or any combination thereof. The components of the system can be located in a singular “cloud” or network or spread among many clouds or networks. End-user knowledge of the system's physical location and configuration of components is not required. [0153] As will be readily understood by one of skill in the art, the disclosed system may be implemented using at least one processor and operably coupled memory. The processor can be any programmable device that accepts digital data as input, is configured to process the input according to instructions or algorithms, and provides results as outputs. In an embodiment, a processor can be a central processing unit (CPU) configured to carry out the instructions of a computer program. A processor is therefore configured to perform at least basic arithmetical, logical, and input/output operations. [0154] Memory operably coupled to the processor can include volatile or non-volatile memory as required by the coupled processor to not only provide space to execute the instructions or algorithms but to provide the space to store the instructions themselves. In embodiments, volatile memory can include random access memory (RAM), dynamic random-access memory (DRAM), or static random-access memory (SRAM), for example. In embodiments, non-volatile memory can include read-only memory, flash memory, ferroelectric RAM, hard disk, floppy disk, magnetic tape, or optical disc storage. The foregoing lists in no way limit the type of memory that can be used, as these embodiments are given only by example and are not intended to limit the scope of the disclosed system. The disclosed storage component generally includes electronic storage for data concerning, for example, the locations, dates, and optionally the times at which samples have been taken and a name, number, or other identifiers for each sample. In an embodiment, the disclosed storage may be a general-purpose database management storage system (DBMS) or relational DBMS as implemented by, for example, Oracle, IBM DB2, Microsoft SQL Server, PostgreSQL, MySQL, SQLite, Linux, or Unix solutions, and for which SQL calls may be utilized for storage and retrieval. In another embodiment, the disclosed storage, engine, or both may employ a cloud computing service such as the Amazon Web Services (AWS) cloud computing service. [0155] The invention is further illustrated in the following non-limiting examples: all parts and percentages are by weight unless otherwise indicated. EXAMPLES Example 1 Natural culturing of AO for antigen isolation [0156] A source of antigen (Ag) is necessary for using the HuCAL phage library to select and develop the disclosed rmAbs. To maintain a natural source of AO-Ag (trophont and dinospore) for use in the immunoassays of this project, AO is cultured in a biosecure aquaculture facility under approved protocols and the supervision of a veterinarian. Culturing AO with naïve host fish allows for a higher infection intensity and increases the yield of trophonts and dinospores. Culturing of trophont and dinospores is performed according to published methods, using a 500-L tank containing artificial seawater equipped with appropriate aeration, biofilters, and filtration for the culturing of AO. The temperature and salinity are maintained for the desired rearing of AO at 25°C and 26 ppt, respectively. All water quality parameters, including DO, temperature, pH, salinity, ammonia, and nitrite, are monitored daily. Previously AO-infected fish obtained from aquaculture facilities are frozen, sent to a lab, and examined via microscopy for the presence of AO, followed by PCR confirmation. Excised gills from frozen infected fish are used to obtain the trophonts for inoculation of the culture tank. Naive pinfish (Lagodon rhomboids) obtained from local aquaculture farms are introduced to the inoculated tank and observed until evidence of significant infection is displayed by the fish (air gulping, erratic swimming, side scraping). The fish are removed, their gill arches excised, placed in glass dishes with artificial seawater, and gently agitated to dislodge trophonts. A subsample of seawater with the detached trophonts is passed through a 150µm mesh filter, and the filtrate is centrifuged at 200 x g for 10 mins. The trophont pellet is sonicated to disrupt the cellular tissue and stored at -80°C to be used as a first Ag in HuCAL screening for AO-rmAbs. The remaining excised gill arches are allowed to settle for 20-30 min to allow the trophonts to transform into the tomont phase. The seawater is filtered twice, once with 200 µm and then with a 60 µm filter to remove any material larger than the tomont. The filtered tomonts are washed three times with sterile water, placed in a 25 ml glass tube along with additional gill material as a substrate, and incubated at 22°C for 72 hours to transform into dinospores. The dinospores are transferred to a clean centrifuge tube and centrifuged for 10 mins at 200xg to pellet the tissue, followed by sonication. The sonicated dinospores are stored at -80°C as a second Ag in HuCAL screening for AO-rmAbs. Example 2 HuCAL library screening for identification of two AO-rmAbs [0157] Clownfish immunized with sonicated dinospores were able to generate an immune response that recognized both the dinospore and trophont sonicated antigens (Ags). However, the tomont was not recognized due to rapid encysting, which reduced Ag exposure. This suggests that the dinospore and trophont life stages may possess similar Ags allowing for the development of rmAbs having the ability to detect both these infective life stages. Therefore, free-swimming dinospores (sonicated) and parasitic trophont (sonicated) are used to screen the HuCAL library for AO-rmAbs and create an AO-RDT for monitoring AO on fish bodies and in water. In order to identify AO-rmAbs, guided selection for epitope recognition of the dinospore and trophont Ags is performed. Selection of Abs using HuCAL technology is made in vitro, which enables greater flexibility for Ab generation than conventional methods based on animal immunization. Guided selection strategies involving either blocking steps or using two or more Ags are employed for the isolation of epitope- specific Abs or for Abs that recognize different epitopes of the same Ag. Initial selection involves the presentation of the HuCAL Ab library to the sonicated dinospore immobilized on a solid support. Abs identified by the first selection round is then presented to the sonicated trophont immobilized on a solid support. Three or more selection rounds may be performed to enrich the Ab library for specific dinospore and trophont binding. Activity and specificity of the AO-rmAbs are tested using quality control (QC) ELISA, in which the AO- rmAbs are tested on three non-related standards Ags and all positive and negative control Ags. A primary criterion for selecting the rmAbs is their ability to detect the whole AO organism at various life stages. The rmAbs that pass all initial tests with the sonicated dinospores and trophonts are then tested with intact dinospores, tomonts, and trophonts as a final selection process. Example 3 ELISA testing to determine AO-rmAbs pairings, QA and QC [0158] Twenty rmAbs are selected from the HUCAL Library for potential use in an AO- RDT. The RDT employs a lateral flow assay (LFA) based on a sandwich ELISA format that requires two rmAbs, one serving as the “capture” rmAb and the other serving as the “detector” rmAb. Some Abs will work better as the capture and others as the detector. To determine which mAbs work best as capture or detector, pairing the rmAbs is performed using several captures or detector combinations and evaluated against traditional ELISA assay tests. The ELISA tests used as positive Ags the whole and sonicated forms of the trophonts and dinospores obtained in Example 1, with phosphate-buffered saline (PBS) and bovine serum albumin (BSA) serving as negative controls. For diagnostic purposes, the ELISA and RDT assays are treated as qualitative assays requiring a simple positive or negative response for the presence of AO. For the evaluation of a negative response, optical density (OD) measurements obtained from the negative controls are used to determine the upper limit of negativity with a 99.9% confidence limit. A positive response value is set based on the mean OD of the negative controls plus three standard deviations of the mean. [0159] Further optimization is performed by comparing and correlating ELISA results with conventional microscopy results. Twenty or more positive and negative samples analyzed by ELISA are validated by microscopy and PCR for the presence or absence of AO. Once optimized, the ELISA assay is used for at least three independent experiments to determine the reproducibility of the AO-rmAb ELISA assay. Example 4 ELISA testing for PP cross-reactivity and species specificity [0160] To investigate whether rmAbs that target AO may also detect the freshwater parasite PP by cross-reactivity to PP, freshwater fish naturally infested with PP is obtained from a collaborating aquaria facility. The investigation is based upon the common shared phylogeny (class Dinophyceae) of the AO and PP ectoparasites and their morphologic and developmental similarities. Gill microscopy is used to validate the presence of PP with confirmation by PCR through the amplification of ribosomal DNA (rDNA). The trophonts and dinospores are isolated using the method described in Example 1. The PP trophont and PP dinospore, as well as the proteins isolated by sonication from each life stage, are tested with AO-rmAb pairs by sandwich ELISA. The criteria employed in Example 3 are used to determine a positive and negative response to the presence of PP. In addition, the AO-rmAbs pairs are evaluated for species specificity to other related and non-related dinoflagellate species. Example 5 rmAbs Validation [0161] Before the natural culturing of the AO trophont and dinospore for use as Ags, as described in Example 1, the gills of the naturally infected fish are excised. Initial identification of the trophont is performed using microscopy, followed by confirmation using AO-specific PCR detection of the rDNA highly. Activity and specificity of the AO- rmAbs are tested using quality control (QC) ELISA, in which the AO-rmAbs are tested on three non-related standards Ags and on the positive and negative control Ags described in Example 2. Sandwich ELISA optimization for the best pairing of capture and detector AO- rmAbs is performed and compared and correlated to the optimized AO-rmAbs pair ELISA results obtained using conventional microscopy to evaluate the presence of AO as described in Example 3. The AO-rmAbs are tested for cross-reactivity with PP to determine the utility of the AO-rmAbs as a tool for detecting PP in freshwater fish species. Cross-reactivity of the AO-rmAbs with other dinoflagellates is carried out to determine species specificity as described in Example 4. Example 6 Data Analysis and Interpretation [0162] In order to compare and correlate results from ELISA, microscopy and PCR, data were correlated and evaluated using linear regression, variance and Spearman rank correlation analyses in R statistics. Example 7 Amyloodinium Ocellatum Aptamer Selection [0163] Aptamers were generated to develop a lateral flow Amyloodinium ocellatum (AO) biosensor (aptasensor). Aptamers were generated using an entirely in vitro process called Systematic Evolution of Ligands by Exponential enrichment (SELEX). The SELEX procedure involves presenting a random DNA library to the target (AO) in multiple rounds of binding, partitioning, recovery, and amplification until the DNA library is fully enriched for binders to the target. Fig.5 is a block diagram of an example SELEX process. [0164] This highly selective and rigorous process can generate aptamers with superior sensitivity and specificity compared to equivalent target protein antibodies. Once a target aptamer sequence is known, it becomes virtually immortalized through chemical synthesis, resulting in minimal to no batch-to-batch variation (a common problem with antibodies). This characteristic confers a significant advantage over conventional antibodies because they can be synthesized with 100%, or nearly 100%, reproducibility. The aptasensor relies on the ability of the aptamer (receptor) to recognize its target of interest (ligand), i.e., Amyloodinium. Once identified, the aptamer(s) may be used to create an in situ lateral flow immunoassay for the early detection of the AO dinospore life stage in water samples. [0165] A pure culture of AO dinospores was used as the target for aptamer selection through the SELEX process. The dinospores immobilized on a WHATMAN™ glass fiber membrane were exposed to an aptamer library (with a starting diversity of approximately 10 ¹⁵ individual candidate sequences, for example). The library was added to the membrane in solution and incubated. The membrane was then washed to remove non-binding candidates, and the bound candidates eluted from the membrane. The bound candidates were amplified by polymerase chain reaction (PCR) and converted back to ssDNA and used as the input library pool for the next round of SELEX. The SELEX was performed over ten rounds while the stringency was increased, reducing the time allowed for binding or increasing the number of post-binding washes performed. Adverse selection was made using a plain membrane without dinospores, which ensures that the aptamers were not binding to the filter. At the end of the SELEX, Next-generation Sequencing (NGS) was performed on the sequence pools, such as from rounds 2, 4, 6, 8, and 10. Using NGS, bioinformatics, or a proprietary method, 24-candidate AO dinospore binding aptamers were identified in an example execution. [0166] A fluorescence dot blot analysis was performed to visualize aptamer binding to the AO dinospores. Fig. 6 is an example fluorescence dot blot of AO dinospores immobilized on a PVDF membrane. The AO dinospore samples were loaded on polyvinylidene fluoride (PVDF) membrane, while the aptamer pools were fluorescently dyed by amplification with a Cy5-labelled PCR primer. AO samples and aptamer pools were incubated to stain the dots in separate wells. Stained dots were scanned for Cy5 fluorescence using a GENEPIX™ microarray scanner. An example execution of this analysis indicate that the aptamers bind to the AO dinospores, however, at or slightly above the background, as demonstrated by the intensity of AO/aptamer pool dots compared to the Cy5 primer background dot. A lack of signal in the no stain (no Cy5) well, along with the lack of a visible dot in the EtOH only (no AO), Cy5 primer confirms that AO was successfully dotted onto the membrane. Visible dots also confirm that some staining was achieved. [0167] Using the selection techniques described in this example, aptamer sequences identified as AOBA-1 to AOBA-31 (SEQ ID NOs: 1-31) are shown in FIG. 7 and in the Sequence Listing accompanying this Application were selected based on SELEX results for further validation, as discussed below. Example 8 Aptamer Validation [0168] In embodiments, the aptamers were validated for specific binding in a cell-based assay using a direct Enzyme-Linked Aptamer Sorbent Assay (ELASA). To validate, cells were seeded into a 96-well microplate at 1.0x10 ⁵ /ml and left to adhere overnight. An equal volume of 8% paraformaldehyde (PFA) solution was added to fix and crosslink the cells to the microplate and incubated for 15 minutes before cells were washed with Phosphate- buffered saline (PBS) (0.1 M sodium phosphate, 0.15 M sodium chloride, pH 7.2). The microplate wells were blocked with 300 µl of 1X PBS with 3% non-fat milk containing non- related sequences per well (a blocking buffer) at 4 ^o C overnight. The wells were washed three times with 1X PBST (PBS containing 0.05% Tween®-20 Detergent). Like those listed in FIG.7, one or more aptamers were labeled with biotin on the 5’ end of the sequence and dissolved in 1 µM PBS.100 µl of the aptamer solution was added to each microplate well and incubated on a shaker for 1 hour at room temperature and then at four ℃ overnight. [0169] The aptamer solution was then removed from the microplate wells, and 100 µl of streptavidin-HRP conjugate (1 mg/ml, 1:2500) was added to the plate and incubated at room temperature for 30 minutes. The conjugates were discarded, and the plate was washed five times with PBST. 100 µl of 1Thermo Scientific -step Ultra TMB-ELISA was added and gently mixed for 45 minutes at room temperature.100 µl of H2SO4 was added to each well to stop the reaction, and the absorbance of each well was measured at 450 nanometers. [0170] Several aptamers were tested for absorbance, which was demonstrated in cell- based experiments. Subsequently, all of the aptamers of Figure 7 were re-synthesized, subjected to stringent cleaning, and 5’-biotinylated, and the again tested for binding. [0171] The re-synthesized, 5’-biotinylated aptamers were tested for binding to whole cell AO dinospores as the analyte. Microplate wells were seeded with 100 µL of 8X10 ⁵ cells/mL* AO dinospores or E. coli K12 as a control by allowing cells to adhere overnight at 4 ^o C. Afterwards, the plates were fixed with 100 µL of 8% paraformaldehyde solution followed by a blocking step to prevent nonspecific binding. Fixed and blocked plates were incubated with the biotinylated aptamer candidates (1 µM) for 1 hour at room temperature and then 4 ^o C for overnight. The plates were then washed with PBS-Tween20 and then incubated for 30 minutes with streptavidin-HRP (0.4 µg/mL). After another washing step, 100 µL of TMB substrate was added to each well and incubated for 45 minutes at room temperature in the dark. The Enzyme-substrate reaction was quenched by adding 100 µL of 2M sulphuric acid to each well and the absorbance measured at 450 nm and 540 nm. [0172] Figure 8 shows absorbance readings for aptamers from FIG. 7, demonstrating binding specificity of the aptamer candidates to AO dinospores compared to the negative control. Absorbance (AU) was read at 450nm, and the sample signal was corrected by deducting the blank control signal. [0173] Various embodiments of systems, devices, and methods have been described herein. These embodiments are given only by example and are not intended to limit the scope of the claimed inventions. It should be appreciated, moreover, that the various features of the embodiments that have been described may be combined in various ways to produce numerous additional embodiments. Moreover, while various materials, dimensions, shapes, configurations, locations, etc., have been described with disclosed embodiments, others may be utilized without exceeding the scope of the claimed inventions. [0174] Persons of ordinary skill in the relevant arts will recognize that the subject matter hereof may comprise fewer features than illustrated in any individual embodiment described above. The embodiments described herein are not meant to be an exhaustive presentation of how the various features of the subject matter hereof may be combined. Accordingly, the embodiments are not mutually exclusive combinations of features; instead, the various embodiments can comprise a combination of different individual features selected from different individual embodiments, as understood by persons of ordinary skill in the art. Moreover, elements described with respect to one embodiment can be implemented in other embodiments even when not described in such embodiments unless otherwise noted. [0175] Although a dependent claim may refer in the claims to a specific combination with one or more other claims, other embodiments can also include a combination of the dependent claim with the subject matter of each other dependent claim or a combination of one or more features with other dependent or independent claims. Such combinations are proposed herein unless it is stated that a specific combination is not intended. [0176] Any incorporation by reference to the documents above is limited such that no subject matter is incorporated contrary to the explicit disclosure herein. Any incorporation by reference to the documents above is further limited such that no claims included in the documents are incorporated by reference herein. Any incorporation by reference of documents above is yet further limited such that any definitions provided in the documents are not incorporated by reference herein unless expressly included herein. [0177] For purposes of interpreting the claims, it is expressly intended that the provisions of 35 U.S.C. § 112(f) are not to be invoked unless the specific terms “means for” or “step for” are recited in a claim.