METHODS FOR TREATING IMMUNOSUPPRESSION AND DISEASES ASSOCIATED WITH IMMUNOSUPPRESSION CROSS REFERENCE TO RELATED APPLICATION This application claims priority to U.S. Provisional Patent Application No. 62/934,373, entitled “Anti-Immunosuppression Peptides for Sepsis and Trauma” and filed on November 12, 2019, which is incorporated herein by reference. GOVERNMENT SUPPORT CLAUSE This invention was made with government support under (W81XWH-17-1-0577) awarded by the U.S. Department of Defense. The government has certain rights to this invention.37 CFR 401.14(f)(4). FIELD OF THE DISCLOSURE The present disclosure relates to therapeutic molecules and approaches for treating sepsis, trauma, and immunosuppression resulting from sepsis and/or trauma. More specifically, the present disclosure relates to NADPH oxidase 2 (NOX2) decoy peptides for treating sepsis, trauma, and immunosuppression resulting from sepsis and/or trauma. BACKGROUND OF THE DISCLOSURE Trauma, blood loss, infections, and sepsis are life-threatening conditions characterized by exaggerated or aberrant immune responses and multi-organ failure (see C. S. Deutschman et al., Immunity 40, 463-75, 2014). Limited therapeutic interventions are linked to high in-hospital mortality rates among critically ill patients (see R. S. Hotchkiss et al., Nat. Rev. Dis. Primers 2, 16045, 2016 and D. C. Angus and T. van der Poll, N. Engl. J. Med.369, 2063, 2013). This includes patients that initially survived initial insult, but died later during the immunosuppression state (see R. S. Hotchkiss et al., Nat. Rev. Immunol. 13, 862-74, 2013 and J. S. Boomer et al., JAMA 306, 2594-605, 2011). Immunosuppression is regarded as immune dysfunction linked to dissemination of primary infection and increased risk of secondary, often nosocomial, infections which frequently include lung infection (see C. S. Deutschman et al., Immunity 40, 463-75, 2014). Neutrophils are professional phagocytic cells that play a central role in innate immune responses to infection and trauma, as well as wound healing (see E. Kolaczkowska and P. Kubes, Nat. Rev. Immunol. 13, 159-75, 2013). Neutrophil dysfunction has been linked to immunosuppression. The mechanism(s) involved in physiological injury stemming from sepsis, trauma, and immunosuppression resulting from each of the foregoing are not understood. Further, the art is lacking effective treatment for sepsis, trauma, and immunosuppression resulting from sepsis and/or trauma, as well as conditions resulting from the foregoing. The present disclosure provides a solution to the shortcomings of the art by providing compounds, compositions comprising such compounds, and methods of treatment using such compounds and compositions for the treatment of sepsis, trauma, immunosuppression resulting from sepsis, immunosuppression resulting from trauma, and conditions resulting from the foregoing. BRIEF DESCRIPTION OF THE FIGURES The present disclosure same can be better understood, by way of example only, with reference to the following drawings. The elements of the drawings are not necessarily to scale relative to each other, emphasis instead being placed upon clearly illustrating the principles of the disclosure. FIG. 1A shows an outline of a cecum ligation and puncture (CLP) or cecal slurry (CS) procedure in mice, as is used to demonstrate the sepsis-induced immunosuppression to be treated according to one embodiment of the present method. P. aeruginosa (PAK)- induced pneumonia was applied 7 days after CLP or CS. FIG. 1B shows a graphical representation of the extent of PAK killing in lungs of sham and mice subjected to CLP (sepsis), as depicted in FIG.1A. Data presented as mean ± s.e.m., n = 5–6. *P < 0.05 (ANOVA). FIG. 1C shows a representative Western blot of HMGB1 in BALs of indicated groups of mice, where “sepsis” mice have been treated according to the procedure depicted in FIG.1A. FIG. 1D shows a representative optical bend densitometry of HMGB1 in BALs of indicated groups of mice, where “sepsis” mice have been treated according to the procedure depicted in FIG.1A. Mean ± s.e.m., n = 4. *P< 0.05 (ANOVA). FIG.1E shows a representative Western blot of HMGB1 recombinant protein used for intratracheal installation in mice, as well as CFUs from lung homogenates of control and HMGB1-treated mice with PAK-induced pneumonia. Mean ± s.e.m., n = 12 mice per indicated groups. *P < 0.05 (Student’s t-test). FIG. 1F shows a graphical representation of the percent of PAK killing in lungs of control (vehicle) mice and mice subjected to intratracheal injection of HMGB1. Mean ± s.e.m., n = 12. *P < 0.05 (Student’s t-test). FIG.1G shows a graphical representation of traces of NOX2 activity (PMA induced) in mouse peritoneal neutrophils that were incubated with or without recombinant Dis- HMGB1 (disulfide HMGB1; 1 μg/ml) for 20 min. Data is presented as fold untreated, mean ± s.e.m., n = 3 technical repetitions per group. *P < 0.05 (Student’s t-test). FIG. 2A shows (left) representative images of fluorescent patterns of HMGB1 in Tunicamycin-treated AECs (20 μg/ml), for 4 hours, and (right) Western blot analysis of the amounts of HMGB1 in culture media after exposure to indicated concentration of Tunicamycin for 16 hours. Mean ± s.e.m., n = 4. *P < 0.05 (ANOVA). Scale bars, 25 μm. FIG. 2B shows (left) representative images of HMGB1 fluorescence in control and apoptotic, Antimycin A-treated macrophages for 4 hours, and (right) Western blot analysis of the extent of HMGB1 accumulation in culture media from macrophages treated with the indicated concentration of Antimycin A for 16 hours. Data presented as mean ± s.e.m., n = 4. *P < 0.05 (ANOVA). Arrows indicate HMGB1 accumulation in cytosol. FIG.2C shows a schematic representation a NOX2 activity assay, with neutrophils treated with lysates from viable or apoptotic AECs. FIG. 2D shows a graphical representation of rates of NOX2 activation by PMA obtained after neutrophil exposure to lysates (250 μg/ml) from control or apoptotic AECs, as shown in FIG.2C. Data presented as mean ± s.e.m., n = 3. FIG. 2E shows a graphical representation of rates of NOX2 activation after neutrophil exposure to apoptotic lysates that were pre-incubated with HMGB1 neutralizing or control IgG (5 μg/ml) for 20 minutes, as shown in FIG. 2C. Data presented as mean ± s.e.m., n = 3. FIG. 2F shows graphical representations of data from FIG. 2D (left) and FIG. 2E (right) presented as fold changes, mean ± s.e.m., n = 3. P < 0.05 (Student’s t-test). FIG. 3A shows a schematic representation of HMGB1 domain organization and cysteine thiol oxidative modifications via s-glutathionylation. FIG. 3B shows representative Western blots of Bio-GSS-proteins in media from unaltered (control) and BioGEE-loaded mouse peritoneal macrophages that were treated with or without Antimycin A (5 μM) for 16 h (upper) or β-actin (lower). FIG.3C shows representative Western blots of Bio-GSS-HMGB1 adducts in media (upper) and cell lysates (middle) or β-actin (lower). Pull-down with Strepavidin-agarose was performed using cell lysates and media from macrophages that were treated as depicted in FIG.3B. FIG.3D shows representative Western blots of recombinant HMGB1 (disulfide) or Bio-GSS-HMGB1 (50 ng) that was incubated with or without DTT followed by non- reducing SDS-PAGE. Representative Western blots were developed using Streptavidin- HRP (upper) or anti-HMGB1 IgG (lower). FIG. 3E shows a graphical representation of TNF-α levels in media of untreated macrophages and in media of macrophages after incubation with HMGB1 disulfide or oxidized (GSS-HMGB1) for 24 hours, or LPS (3 ng/ml) for 4.5 hours. Mean ± s.e.m., n = 4-5. *P < 0.05 (ANOVA). FIG. 3F shows a graphical representation of traces of PMA-stimulated NOX2 activity in mouse peritoneal neutrophils that were treated with reduced or oxidized HMGB1 (0 or 1 μg/ml) for 20 min. Mean ± s.e.m., n = 3 technical repetitions per indicated groups. *P < 0.05 (ANOVA). FIG.3G shows a graphical representation of traces of PMA-dependent activation of NOX2 in control neutrophils and neutrophils that were treated with reduced or oxidized HMGB1. Data presented as fold control, mean ± s.e.m., n = 3. *P < 0.05 (ANOVA). FIG.4A shows a representative Western blot of 6xHis-HMGB1, before (Input) and after immunoprecipitation (Pull down) with anti-gp91 ^phox IgG. Neutrophils were treated with oxidized 6xHis-HMGB1 (1 μg/ml) for 30 minutes prior to lysate preparation. FIG.4B shows a representative Western blot of endogenous HMGB1 before (Input) or after immunoprecipitation (pull down) with anti-gp91 ^phox IgG. FIG. 4C shows representative Western blots of fluorescence-labeled HMGB1 (HMGB1-FL) that was detected using chemiluminescence, fluorescence and ambient light imaging methods. FIG.4D shows a graphical representation of flow cytometry analysis that indicates time-dependent binding of oxidized HMGB1-FL to viable neutrophils. FIG. 4E shows images show fluorescent patterns of oxidized HMGB1-FL and gp91 ^phox (indirect immunofluorescence) in viable neutrophils. Scale bar, 20 μm. Arrows indicate co-localization between HMGB1-FL and gp91 ^phox . FIG. 5A shows graphical representations of PMA-stimulated NOX2 activity in neutrophils that were incubated with plasma of healthy volunteers (control) or patients with traumatic shock/secondary bacterial lung infection (shock/infection). NOX2 activity rates (left) of control vs. shock presented are shown and presented (right) as fold changes, mean ± s.e.m., n = 3. P < 0.05, (Student’s t-test). FIG.5B shows graphical representations of plasma from trauma-immunosuppressed patients that was incubated with or without gp91 ^phox decoy, followed by measurement of NOX2 activation by PMA. Rates of NOX2 activity of shock/infection or shock/infection + decoy gp91 ^phox are shown (left). Data (right) are presented as fold changes, mean ± s.e.m., n = 3. P < 0.05, (Student’s t-test). FIG. 5C shows schematic representations of neutrophil immunosuppression (left) and gp91 ^phox /NOX2 decoy-induced prevention of the immunosuppressive effect (right). During sepsis-induced immunosuppression, dying and injured cells release DAMPs, including oxidized HMGB1 that decreases neutrophil respiratory burst. HMGB1 binds to gp91 ^phox subunit of NOX2 and diminished respiratory burst. The immunosuppressive effects of plasma is prevented by application of gp91 ^phox /NOX2 decoy strategy. FIG. 6A shows a schematic representation of T/H plasma-dependent inhibition of superoxide production by NOX2 in neutrophils. Gp91 ^phox transmembrane and p22 ^phox subunits are shown, with indication of gp91 external loops 1–3 that were used to design AI peptides. FIG.6B shows a listing of amino acids sequences for AI peptides, as were designed to interact with the gp91 external loops of FIG.6A. FIG. 6C shows a schematic representation of a procedure to test the effects of AI peptides on T/H plasma-dependent inhibition of the neutrophil respiratory burst, bacterial killing and mice survival after lethal peritonitis. FIG. 6D shows a graphical representation of the effects of AI peptides on T/H plasma-mediated inhibition of neutrophil respiratory burst (NOX2 activity). T/H plasma was pre-incubated with AI peptide 1, 2 or 3, (0 or 2.5 μg/plasma), or combined AI peptides, for 30 min, followed by exposure of neutrophils to T/H plasma (with or without peptides) for an additional 30 min. HD plasma (healthy donor, 500 μg/ml) was used as a control. NOX2 activity was determined using cytochrome c reduction assay. Data presented as mean ± s.e.m., n = 5 per each indicated group. *P < 0.05 (ANOVA). FIG.6E shows a graphical representation of bacterial viability (CFUs; fold untreated HD plasma) after incubation of E. coli with neutrophils that were treated with T/H plasma and AI peptides in vitro, as depicted in FIG.6D. Data presented as mean ± s.e.m., n = 5 per each indicated group. *P < 0.05 (ANOVA). FIG.6F shows a graphical representation of HMGB1 (recombinant) and AI peptide complex formation (ELISA). Mean ± s.e.m., n = 3. *P < 0.05 (Student’s t-test). FIG.6G shows a representative Western blot of HMGB1 levels in peritoneal lavages from control or mice subjected to E. coli (2 × 10 ⁸ ; i.p.) -induced peritonitis for 4 hours, n = 4 lavages from indicated groups. FIG. 6H shows a graphical representation of percent survival in mice subjected to peritonitis and intraperitoneal injection of AI peptides (combined AI peptide 1, 2, and 3; 2.5 μg each/mouse; i.p.) or vehicle. Kaplan-Meier survival curve, n = 12 mice/groups. *P < 0.05. DETAILED DESCRIPTION Trauma, sepsis and immunosuppression resulting from sepsis and/or trauma are serious conditions, leading to significant mortality and morbidity for affected subjects. Immunosuppression is regarded as immune dysfunction linked to dissemination of primary infection and increased risk of secondary, often nosocomial, infections. Such secondary infections target a variety of organs, including the lungs. When secondary lung infections occur, such infections can lead to a variety of conditions, including, but not limited to, acute respiratory distress syndrome (ARDS), lung fibrosis, and chronic obstructive pulmonary disease (COPD). The mechanism(s) involved in physiological injury stemming from sepsis, trauma, and immunosuppression resulting from each of the foregoing are not understood and effective treatments are lacking. Damage Associated Molecular Patterns (DAMPs) proteins and alarmins are host- derived inflammatory mediators released during cell damage or cell death that affect immune responses to sepsis, infection and trauma, but also contribute to autoimmune disorders and carcinogenesis (see C. M. Gorgulho et al., Frontiers in Immunology 10, 1561, 2019). High Mobility Group Box 1 (HMGB1), one of the first discovered DAMPs, has been implicated in regulating innate and adaptive immunity, severity of organ injury, as well as the wound healing process (see H. Wang et al., Am. J. Respir. Crit. Care Med.164, 1768- 73, 2001, and U. Andersson and K. J. Tracey, Annu. Rev. Immunol.29, 139-62, 2011). In sepsis, the extent of HMGB1 accumulation in plasma has been correlated with severity and mortality among critically ill patients (see H. Wang et al., Science 285, 248-51, 1999). While HMGB1 is known mediator of lethality in severe infections and trauma, its contribution to development of immunosuppression and susceptibility to secondary infections is less understood. Neutrophils are professional phagocytic cells that play a central role in innate immune responses to infection and trauma, as well as wound healing (see E. Kolaczkowska and P. Kubes, Nat. Rev. Immunol. 13, 159-75, 2013). Neutrophil dysfunction has been linked to immunosuppression. The respiratory burst, a rapid production and release of reactive oxygen species (ROS), is a primary mechanism by which neutrophils utilize nicotinamide adenine dinucleotide phosphate oxidase (NADPH) oxidase (NOX) 2 to eradicate pathogenic microbes (see J. El-Benna et al., Immunological reviews 273, 180-93, 2016). NOX2 is a membrane-bound enzyme complex that consist of several subunits, including transmembrane gp91 ^phox and p22 ^phox (flavocytochrome b558), cytosolic p40 ^phox , p47 ^phox , p67 ^phox and regulatory Rac2 (see S. A. Belambriet al., Eur. J. Clin. Invest.48 Suppl 2, e12951, 2018). NOX2 is activated through several mechanisms, including by bacterial peptide formyl-Met- Leu-Phe that stimulates rapid production of superoxide (O2•‒) via NADPH-dependent oxygen reduction. NOX2 inactivation causes a disadvantage for the host immune system, as seen in hereditary chronic granulomatous disease (CGD) (see N. Strydom and S. M. Rankin, J. Innate Immun.5, 304-14, 2013, and A. W. Segal et al., Lancet 2, 446-9, 1978). Similarly, NOX2 deficiency compromises the host’s ability to kill bacteria in experimental models of polymicrobial intra-abdominal sepsis (see T. A. Chessa et al., Blood 116, 6027-36). Interestingly, loss of NOX2 activity has also been implicated in increased severity of endotoxin-induced acute lung injury (ALI) (see L. C. Whitmore et al., Am. J. Physiol. Lung Cell Mol. Physiol. 307, L71-82, 2014, and L. C. Whitmore et al., J. Innate Immun. 5, 565-80, 2013). Although NOX2 activity is diminished during immunosuppression, including immunosuppression occurring after sepsis, infection, and trauma, the mechanism(s) involved in NOX2 inactivation in neutrophils remain to be determined. The present disclosure shows that DAMPS, alarmins, and other host-derived inflammatory mediators impact the immune response leading to immunosuppression. Specifically, HMGB1 In is shown to contribute to immunosuppression through decreasing NOX2 activity in neutrophils. Blocking the HMGB1/gp91 ^phox interaction decreased HMGB1-mediated inhibition of NOX2 activity and decreased immunosuppression. Summary of the Disclosure Post-sepsis immunosuppression is frequently associated with reoccurring infections and poses a high risk of secondary lung infections and respiratory failure. The present disclosure demonstrates that DAMPs, and in particular HMGB1, decreases innate immune capacity to kill pathogenic bacteria, such as, but not limited to, P. aeruginosa, in lungs of sepsis-immunosuppressed mice. Oxidative stress associated with macrophage and alveolar epithelial apoptosis promote HMGB1 oxidation via GSS-HMGB1 adduct formation (s- glutathionylation), and extracellular release. Interaction between GSS-HMGB1 and gp91 ^phox , a major transmembrane subunit of NOX2, results in decreased neutrophil respiratory burst and bacterial killing. Furthermore, the present disclosure demonstrates that this immunosuppressive effect is reduced by preventing, reducing, or inhibiting the binding of GSS-HMBG1 and gp91 ^phox . In certain embodiments, peptides that mimic an extracellular portion of gp91phox (including the compounds of the disclosure and analogs thereof) prevent, reduce, or inhibit the binding of GSS-HMBG1 and gp91 ^phox . As such, the compounds of the disclosure (particularly peptides SEQ ID NOS: 1-3 and analogs thereof) are useful in treating bacterial infection, neutrophil dysfunction, sepsis, trauma, immunosuppression associated with sepsis and/or trauma, organ injury associated with any of the foregoing (such as, but not limited to, ARDS, lung fibrosis, and COPD), or a symptom of any of the foregoing. In addition, the compounds of the disclosure (particularly peptides SEQ ID NOS: 1-3 and analogs thereof) are useful in reducing immunosuppression, reducing NOX2 inhibition, increasing neutrophil respiratory burst, and preventing DAMP-mediated inactivation of NOX2 in a subject. The use of a peptide to prevent the binding of GSS-HMBG1 and gp91 ^phox may be described herein as a peptides having the sequence of SEQ ID referred to herein as a gp91 ^phox /NOX2 decoy strategy. The present disclosure provide for the use of the compounds of the disclosure (particularly peptides SEQ ID NOS: 1-3 and analogs thereof) in therapeutic treatment applications. This strategy has therapeutic potential to prevent DAMPs-mediated inactivation of NOX2 in neutrophils during immunosuppression. Specifically, gp91 ^phox /NOX2 decoy strategy effectively disrupt the immunosuppressive action of DAMPs that have been activated in response a variety of initiators, such as, but not limited to, infection, sepsis, and trauma/hemorrhage, reducing the induction of immunosuppression. In vitro, the compounds of the disclosure reduced the ability of trauma/hemorrhage (T/H) patient plasma in inactivate NOX2. In vivo, the compounds of the disclosure improved survival of mice subjected to lethal peritonitis. Therefore, the compounds of the disclosure may be used therapeutically to treat bacterial infection, neutrophil dysfunction, sepsis, trauma, immunosuppression associated with sepsis and/or trauma, organ injury associated with any of the foregoing (such as, but not limited to, ARDS, lung fibrosis, and COPD), or a symptom of any of the foregoing. Definitions All patent applications, patents, and printed publications cited herein are incorporated herein by reference in the entireties, except for any definitions, subject matter disclaimers or disavowals, and except to the extent that the incorporated material is inconsistent with the express disclosure herein, in which case the language in this disclosure controls. The articles “a” and “an” are used herein to refer to one or to more than one (i.e., to at least one) of the grammatical object of the article. By way of example, “an element” means one element or more than one element. As used herein, the term “about” is used to mean approximately, around, or roughly. When the term “about” is used in conjunction with a numerical range, it modifies that range by extending the boundaries above and below the numerical values set forth. In general, the term “about” is used herein to modify a numerical value above and below the stated value by a variance of 20 percent up or down (higher or lower). The term “acid” contemplates all pharmaceutically acceptable inorganic or organic acids. Inorganic acids include mineral acids such as hydrohalic acids, such as hydrobromic and hydrochloric acids, sulfuric acids, phosphoric acids and nitric acids. Organic acids include all pharmaceutically acceptable aliphatic, alicyclic and aromatic carboxylic acids, dicarboxylic acids, tricarboxylic acids, and fatty acids. Preferred acids are straight chain or branched, saturated or unsaturated C1-C20 aliphatic carboxylic acids, which are optionally substituted by halogen or by hydroxyl groups, or C6-C12 aromatic carboxylic acids. Examples of such acids are carbonic acid, formic acid, fumaric acid, acetic acid, propionic acid, isopropionic acid, valeric acid, alpha-hydroxy acids, such as glycolic acid and lactic acid, chloroacetic acid, benzoic acid, methane sulfonic acid, and salicylic acid. Examples of dicarboxylic acids include oxalic acid, malic acid, succinic acid, tataric acid and maleic acid. An example of a tricarboxylic acid is citric acid. Fatty acids include all pharmaceutically acceptable saturated or unsaturated aliphatic or aromatic carboxylic acids having 4 to 24 carbon atoms. Examples include butyric acid, isobutyric acid, sec-butyric acid, lauric acid, palmitic acid, stearic acid, oleic acid, linoleic acid, linolenic acid, and phenylsteric acid. Other acids include gluconic acid, glycoheptonic acid and lactobionic acid. The term “AI peptide” as used herein refers to a peptide having a sequence at least 50% identical (such as, 80%, 90%, 95%, or 99% identical) to the amino acid sequence of an external domain (such as, but not limited to, an external transmembrane domain) of a component of NOX2, such as, but not limited to, gp91 ^phox , p22 ^phox , p40 ^phox , p47 ^phox , p67 ^phox and Rac2. In certain preferred aspects, the term “AI peptide” as used herein refers to a peptide having a sequence at least 50% identical (such as, 80%, 90%, 95%, or 99% identical) to the amino acid sequence of an external domain (such as, but not limited to, an external transmembrane domain) of the gp91 ^phox subunit of NOX2. In a further preferred embodiment, the extracellular domain of gp91 ^phox is one or more of loops 1, 2, or 3 of gp91 ^phox . The term “bodily fluid(s)” as used herein means a fluid or secretion of the body, including, but not limited to, intracellular fluids (such as, but not limited to, the cytosol), blood, blood plasma, blood serum, mucous, cerebrospinal fluid, bronchoalveolar lavage (BAL), urine, saliva, tears, sputum, or a combination of the foregoing. In a particular embodiment, the term refers to blood, blood plasma, blood serum, or a combination thereof. The term “carrier” refers to a diluent or vehicle with which a compound is administered. Preferably, the carrier is a pharmaceutically acceptable carrier. Examples of suitable pharmaceutical carriers are described in “Remington's Pharmaceutical Sciences” by E. W. Martin. The term “compound(s) of the disclosure” as used herein means an AI-polypeptide, an AI- analog thereof, or a pharmaceutically acceptable form of the foregoing. In certain aspects, a compound of the disclosure is AI-polypeptide 1, 2 or 3 as described herein, an analog thereof, or a pharmaceutically acceptable form of the foregoing. The term “Damage Associated Molecular Patterns (DAMPs)” refers to host-derived biomolecules that affects and/or mediates an immune response in a subject. DAMPs may also be referred to as danger-associated molecular patterns, danger signals, and alarmins. DAMPs may originate in the extracellular matrix or intracellularly from the cytosol, nucleus, mitochondria, endoplasmic reticulum, plasma membrane, or granules. An exemplary DAMP is HMGB1. The term an “effective amount,” “sufficient amount” or “therapeutically effective amount” as used herein is an amount of a compound of the disclosure that is sufficient to achieve a beneficial or desired result, including clinical results. In one embodiment, the “effective amount” is sufficient, for example, to treat a bacterial infection, neutrophil dysfunction, sepsis, trauma, immunosuppression associated with sepsis and/or trauma, organ injury associated with any of the foregoing, or a symptom of any of the foregoing. In another embodiment, the “effective amount” is sufficient, for example, to treat a disease or condition related to a bacterial infection, neutrophil dysfunction, sepsis, trauma, immunosuppression associated with sepsis and/or trauma, organ injury associated with any of the foregoing, or a symptom of any of the foregoing. In another embodiment, the “effective amount” is sufficient, for example, to enhance or otherwise improve the prophylactic or therapeutic effect(s) of another therapy, such as treatment with an additional active agent. In another embodiment, the “effective amount” avoids or substantially attenuates undesirable side effects. In certain embodiments, the “effective amount,” “sufficient amount” or “therapeutically effective amount” in the context of the present disclosure is an amount sufficient to reduce one or more of the following: a bacterial infection, neutrophil dysfunction, sepsis, trauma, immunosuppression associated with sepsis and/or trauma, organ injury associated with any of the foregoing (such as, but not limited to, ARDS, lung fibrosis, and COPD), or a symptom of any of the foregoing. Such a reduction in any of the foregoing may be by at least 5%, preferably at least 10%, at least 15%, at least 20%, at least 25%, at least 30%, at least 35%, at least 40%, at least 45%, at least 50%, at least 55%, at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, or 100%. In some embodiments, the “effective amount,” “sufficient amount” or “therapeutically effective amount” in the context of the present disclosure increases an immune response in a subject, including, but not limited to, a subject suffering from sepsis, trauma, and/or immunosuppression (including immunosuppression resulting from sepsis and/or trauma) by at least 5%, preferably at least 10%, at least 15%, at least 20%, at least 25%, at least 30%, at least 35%, at least 40%, at least 45%, at least 50%, at least 55%, at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, or 99%. In some embodiments, the “effective amount,” “sufficient amount” or “therapeutically effective amount” in the context of the present disclosure increases the survival rate of a subject suffering from sepsis, trauma, and/or immunosuppression (including immunosuppression resulting from sepsis and/or trauma) by at least 5%, preferably at least 10%, at least 15%, at least 20%, at least 25%, at least 30%, at least 35%, at least 40%, at least 45%, at least 50%, at least 55%, at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, or 100%. In each of the foregoing, when a reduction of increase is specified, such reduction of increase may be determined with respect to a subject that has not been treated with a compound of the disclosure and that is diagnosed as suffering from sepsis, trauma, and/or immunosuppression resulting from sepsis and/or trauma. The term “excipient” as used herein means a substance formulated alongside the active ingredient of a composition included for purposes such as, but not limited to, long-term stabilization, bulking up solid formulations that contain potent active ingredients in small amounts (thus often referred to as bulking agents, fillers, or diluents), or to confer a therapeutic enhancement on the active ingredient in the final dosage form, such as facilitating drug absorption, reducing viscosity, or enhancing solubility. Excipients can also be useful in the manufacturing process, to aid in the handling of the active substance concerns such as by facilitating powder flowability or non-stick properties, in addition to aiding in vitro stability such as prevention of denaturation or aggregation over the expected shelf life. Preferably, the excipient is a pharmaceutically acceptable excipient. Examples of suitable excipients are described in “Remington's Pharmaceutical Sciences” by E. W. Martin. The term “High Mobility Group Box 1 (HMGB1)” refers to the protein encoded by the human HMGB1 gene, and may also be referred to as high-mobility group protein 1 (HMG-1) and amphoterin. HMGB1 is recognized in mediating the inflammatory response by binding receptors, including TLR, TLR4, TLR9, and RAGE. The term “in need of” (such as in the phrase “in need of treatment”) refers to a judgment made by a healthcare professional that a subject requires or will benefit from administration of a compound of the disclosure. This judgment is made based on a variety of factors that are in the realm of a healthcare professional's expertise, such as, but not limited to, the knowledge that the subject is ill, or will be ill, as the result of a disease or condition that is treatable by a method or drug composition of the disclosure. The term “nicotinamide adenine dinucleotide phosphate oxidase (NADPH) oxidase 2 (NOX2)” refers to the protein encoded by the human NOX2 gene, which may also called the CYBB gene. NOX2 may also be referred to as cytochrome b(558) subunit beta or cytochrome b-245 heavy chain. NOX2 includes subunits gp91 ^phox , p22 ^phox (flavocytochrome b ₅₅₈ ), p40 ^phox , p47 ^phox , p67 ^phox and Rac2. The term “pharmaceutically acceptable” refers to a compound that is compatible with the other ingredients of a composition and not deleterious to the subject receiving the compound or composition containing the compound. In some embodiments, the term “pharmaceutically acceptable” means approved by a regulatory agency of the Federal or a state government or listed in the U.S. Pharmacopeia or other generally recognized pharmacopeia for use in animals, and more particularly in humans. The term “pharmaceutically acceptable form” is meant to include known forms of a compound that may be administered to a subject, including, but not limited to, solvates, hydrates, prodrugs, isomorphs, polymorphs, pseudomorphs, neutral forms and salt forms of a compound of the disclosure. The term “pharmaceutically acceptable salt” is intended to include salts derived from inorganic or organic acids including, for example hydrochloric, hydrobromic, sulfuric, nitric, perchloric, phosphoric, formic, acetic, lactic, maleic, fumaric, succinic, tartaric, glycolic, salicylic, citric, methanesulfonic, benzenesulfonic, benzoic, malonic, trifluoroacetic, trichloroacetic, naphthalene-2 sulfonic and other acids. Pharmaceutically acceptable salt forms may also include forms wherein the ratio of molecules comprising the salt is not 1:1. For example, the salt may comprise more than one inorganic or organic acid molecule per molecule of base, such as two hydrochloric acid molecules per molecule of compound of formula I. As another example, the salt may comprise less than one inorganic or organic acid molecule per molecule of base, such as two molecules of compound of formula I per molecule of tartaric acid. Salts may also exist as solvates or hydrates. The term “pharmaceutical composition” refers to a mixture of one or more of the compounds of the disclosure, with other components, such as, but not limited to, pharmaceutically acceptable carriers and/or excipients. The purpose of a pharmaceutical composition is to facilitate administration of a compound of disclosure. The term “protein,” “peptide,” “polypeptides” and “oligopeptides” refer to chains of amino acids (typically L-amino acids) whose alpha carbons are linked through peptide bonds formed by a condensation reaction between the carboxyl group of the alpha carbon of one amino acid and the amino group of the alpha carbon of another amino acid. Typically, the amino acids making up a protein are numbered in order, starting at the amino terminal residue and increasing in the direction toward the carboxy terminal residue of the protein. The term “analog” (such as a “peptide analog”) refers to a variant of a parent molecule, for example, a parent peptide. For example, an analog of a parent peptide can include a variant, where one or more amino acids are substituted relative to the parent peptide. An analog can also include a modification of a parent peptide, including but not limited to, non-naturally occurring amino acids, D amino acids, modified amino- and/or carboxy-terminal (N- or C-terminal) amino acids, in particular modifications of the amino group on the N-terminus and/or modification of the carboxyl group in the C-terminus, fatty acid modifications, esterification, peptidomimetics, pseudopeptide, and the like, as disclosed herein. The term “resulting from,” “results from,” or “secondary to” when referencing a disease or condition means the disease or condition is caused, at least in part, by the recited factor(s). For example, the phrase “immunosuppression results from sepsis” mean the immunosuppression is caused either partially or totally by sepsis in the subject. As another example, the phrase “bacterial infection secondary to immunosuppression” means the bacterial infection is caused either partially or totally by a state of immunosuppression in the subject. The term “solvate” as used herein means a compound of the disclosure, or a pharmaceutically acceptable salt thereof, wherein one or more molecules of a suitable solvent are incorporated in the crystal lattice. A suitable solvent is physiologically tolerable at the dosage administered. Examples of suitable solvents are ethanol, water and the like. When water is the solvent, the molecule is referred to as a “hydrate.” The terms “subject” and “patient” as used herein include all members of the animal kingdom including, but not limited to, mammals, animals (e.g., cats, dogs, horses, swine, etc.) and humans. In certain embodiments, the subject is a human. In certain embodiments, the subject is a human of the female sex. In certain embodiments, the subject is a human of the male sex. The term “tissue” as used herein refers to an organ, part of an organ, cellular structure(s), and/or group of cells in the body of a subject. Including, but not limited to, lung, an embryo, a fetus, placenta, liver, kidney, spleen, brain, testis, or uterus. The terms “treatment” or “treating” as used herein means an approach for obtaining beneficial or desired results, including clinical results. Beneficial or desired clinical results in the context of a the present disclosure include, but are not limited to, prevention or reduction of a bacterial infection, neutrophil dysfunction, sepsis, trauma, immunosuppression associated with sepsis and/or trauma, organ injury associated with any of the foregoing (such as, but not limited to, ARDS, lung fibrosis, and COPD), or a symptom of any of the foregoing, alleviation or amelioration of one or more symptoms or conditions, a diminution of extent of disease, a stabilized (i.e., not worsening) state of disease, delaying or slowing of disease progression, amelioration or palliation of the disease state and remission (whether partial or total). “Treatment” or “treating” can also mean prolonging survival as compared to expected survival if not receiving treatment. The present disclosure provides mechanistic insight into development of the neutrophil immunosuppressive phenotype, in particular via DAMP-mediated decrease of neutrophil function (such as respiratory burst). Previous studies have shown that release of oxidized HMGB1 has been linked to tissue injury and intrinsic apoptosis characterized by a robust production of reactive oxygen species (ROS) and reactive nitrogen species (RNS) by mitochondria (see D. Tang, et al., Antioxid. Redox Signal 14, 1315-1335, 2011). While HMGB1 adversely affects killing of bacteria, such decrease in NOX2 activity has been previously implicated in enhanced pro-inflammatory activation of neutrophils, and more severe organ injury (see L. C. Whitmore et al., Am. J. Physiol. Lung Cell Mol. Physiol.307, L71-82, 2014; L. C. Whitmore et al., J. Innate Immun.5, 565-80, 2013; and W. Han et al., J. Immunol. 190, 4786-4794, 2013). In particular, mice deficient in p47 ^phox or gp91 ^phox subunit developed more severe response to endotoxin-mediated ALI. A possible benefit of NOX2 activation is likely mediated by production of hydrogen peroxide (H ₂ O ₂ ). Previous findings have demonstrated the H2O2 anti-inflammatory action, including redox-dependent inhibition of the NF-KB signaling cascade in neutrophils (see J. W. Zmijewski et al., Am. J. Respir. Crit. Care Med.179, 694-704, 2009; S. Banerjee et al., J. Biol. Chem.2009; and J. W. Zmijewski et al., Am. J. Physiol. Cell Physiol. 293, C255-66, 2007). These findings indicate that preservation of NOX2 activity is not only crucial for eradication of pathogenic microbes, but also to moderate neutrophil pro-inflammatory activation and severity of lung injury. In its reduced form, HMGB1 has three cysteine thiols Cys23, Cys45, and Cys106, and all are available for oxidation. However, while HMGB1 is prone to form a disulfide bond between Cys23 and Cys45, oxidation of Cys106 has been shown to have regulatory function, e.g. promoted HMGB1 nucleus-to-cytosol translocation (see G. Hoppe et al., Exp. Cell Res. 312, 3526-3538, 2006, and H. Yang et al., Mol. Med.18, 250-259, 2012). Unlike reduced and disulfide HMGB1, HMGB1 derived from apoptotic cells has been found in an oxidized state and with limited ability to activate immune responses (see U. Andersson and K. J. Tracey Annu. Rev. Immunol. 29, 139-162, 2011, and H. Kazama et al., Immunity 29, 21- 32, 2008). In the present disclosure peptides were designed to block the interaction of DAMPs with one or more components of NOX2. The disclosed peptides were designed based on the amino acid sequences corresponding to the three external transmembrane loops of gp91 ^phox , a representative NOX2 component. The present disclosure shows such peptides (i.e., the gp91 ^phox /NOX2 decoy strategy) can reduce the plasma-mediated, DAMP- dependent decrease of NOX2 activation and maintain and/or increase neutrophil function (such as respiratory burst). In particular, gp91 ^phox /NOX2 decoy strategy is a viable therapeutic strategy to reduce risk of bacterial infections during sepsis/trauma-induced immunosuppression. NADPH oxidase 2, gp91 ^phox , and AI peptides NOX2 is a membrane-bound enzyme that forms reactive oxygen species (ROS) via NADPH-dependent oxygen reduction. As the rapid production and release of ROS is a major mechanism by which neutrophils attack pathogens, including microbial pathogens, NOX2 inactivation reduces a host ability to respond adequately and eliminate such pathogens. NOX2 includes several subunits, including transmembrane gp91 ^phox and p22 ^phox (flavocytochrome b ₅₅₈ ), cytosolic p40 ^phox , p47 ^phox , p67 ^phox and regulatory Rac2. DAMPs affect immune responses of a host to infection and trauma after their release from damaged or dying cells. After release, DAMPs bind to pattern recognition receptors (PRRs). The PRRs are found on innate immune cells, such as macrophages, monocytes, mast cells, and dendritic cells, as well as non-immune cells, such as epithelial cells and fibroblasts. DAMP interaction with its PRR initiates a downstream signaling cascade resulting in an immune response, such as leukocyte recruitment. The DAMP High Mobility Group Box 1 (HMGB1) is implicated in regulation of innate and adaptive immunity, severity of organ injury, as well as the wound healing process, with increased plasma levels of HMGB1 corresponding to lethality in severe infections and trauma. Disulfide and oxidized forms of HMGB1 are shown herein to bind the gp91 ^phox subunit of NOX2, inhibiting NOX2 activity and leading to a decreased the neutrophil respiratory burst and impaired ability to clear pathogens. Described is a strategy for the reduction of NOX2 inhibition by DAMPs (including HMGB1), particularly in the setting of severe infection, sepsis, and trauma, through the use of anti-immunosuppression peptides (AI peptides) and a gp91 ^phox /NOX2 decoy strategy. The AI peptides are designed based on the amino acid sequence corresponding to external domains of a NOX2 component. In a particular embodiment, compounds of the disclosure are designed based on the amino acid sequence corresponding to the three external transmembrane loops of gp91 ^phox . In a further particular embodiment, n AI peptide has the sequence set forth in SEQ ID NOS: 1-3. AI peptides are configured to bind mediators of immunosuppression (such as, but not limited to, DAMPs) in plasma and other bodily fluids, including BAL. AI peptides sequester mediators of immunosuppression (such as, but not limited to, DAMPs) that can interact with and inhibit activation of NOX2. Thus, an immunosuppressive effect resulting from infection, sepsis, and/or trauma is reduced by AI peptides using the gp91 ^phox /NOX2 decoy strategy of the present disclosure. Compounds of the Disclosure The present disclosure provides for AI peptides or analogs thereof which bind mediators of immunosuppression (such as, but not limited to, DAMPs). In a particular aspect, AI peptides are designed to correspond to an external domain of a NOX2 component, such as an external transmembrane loop of gp91 ^phox . Exemplary AI peptides are provided herein, including AI peptide 1 (SEQ ID NO: 1), AI peptide 2 (SEQ ID NO: 2), and AI peptide 3 (SEQ ID NO: 3). In an alternative aspect, an AI peptide has a sequence that has 50% or greater, 60% or greater, 70% or greater, 80% or greater, 90% or greater, 95% or greater, or 99% or greater sequence identity to SEQ ID NOS: 1-3, preferably 70% or greater, 80% or greater, 90% or greater or 95% or greater sequence identity. In another alternative aspect, an AI peptide has a sequence containing 1 or more substitutions and/or one or more unnatural amino acids as compared to a peptide sequence of SEQ ID NOS: 1-3. In another alternative aspect, an AI peptide is a peptide analog of the sequence of SEQ ID NOS; 1-3. In another aspect, an AI peptide has a sequence that has 50% or greater, 60% or greater, 70% or greater, 80% or greater, 90% or greater, 95% or greater, or 99% or greater sequence identity to an external transmembrane domain of gp91 ^phox , preferably 70% or greater, 80% or greater, 90% or greater or 95% or greater sequence identity. In some embodiments, an external domain of gp91 ^phox corresponds to an external loop of the transmembrane domain of gp91 ^phox . The gp91 ^phox subunit from a mouse or human, preferably a human, is used. AI peptides corresponding to the three external transmembrane loops of gp91 ^phox are shown in Table 1. The amino acid sequence of human gp91 ^phox is provided below (SEQ ID NO: 4). The amino acid sequences corresponding to the extracellular loops 1-3 are underlined and in bold. MGNWAVNEGL SIFVILVWLG LNVFLFVWYY RVYDIPPKFF YTRKLLGSAL 60 70 80 90 100 ALARAPAACL NFNCMLILLP VCRNLLSFLR GSSACCSTRV RRQLDRNLTF 110 120 130 140 150 HKMVAWMIAL HSAIHTIAHL FNVEWCVNAR VNNSDPYSVA LSELGDRQNE 160 170 180 190 200 SYLNFARKRI KNPEGGLYLA VTLLAGITGV VITLCLILII TSSTKTIRRS 210 220 230 240 250 YFEVFWYTHH LFVIFFIGLA IHGAERIVRG QTAESLAVHN ITVCEQKISE 260 270 280 290 300 WGKIKECPIP QFAGNPPMTW KWIVGPMFLY LCERLVRFWR SQQKVVITKV 310 320 330 340 350 VTHPFKTIEL QMKKKGFKME VGQYIFVKCP KVSKLEWHPF TLTSAPEEDF 360 370 380 390 400 FSIHIRIVGD WTEGLFNACG CDKQEFQDAW KLPKIAVDGP FGTASEDVFS 410 420 430 440 450 YEVVMLVGAG IGVTPFASIL KSVWYKYCNN ATNLKLKKIY FYWLCRDTHA 460 470 480 490 500 FEWFADLLQL LESQMQERNN AGFLSYNIYL TGWDESQANH FAVHHDEEKD 510 520 530 540 550 VITGLKQKTL YGRPNWDNEF KTIASQHPNT RIGVFLCGPE ALAETLSKQS 560 570 ISNSESGPRG VHFIFNKENF The compounds of the disclosure, can be produced using various techniques known in the art. For recombinant production of compounds of the disclosure, nucleic acid encoding a compounds of the disclosure can be synthesized and inserted into one or more vectors for further cloning and/or expression in host cells. Compounds of the disclosure containing a heterologous sequence may be produced in the same manner, with the exception that the cDNA additionally encodes the heterologous amino acid sequence. In some embodiments, compounds of the disclosure having one or more amino acid substitutions, insertions or deletions are generated by site-directed mutagenesis or other methods known in the art. Such nucleic acid may be readily isolated and sequenced using conventional procedures. Expression vectors comprising a compounds of the disclosure can be transfected into the host cells or stably expressed in the host cells. Suitable host cells for cloning or expression of the compounds of the disclosure include prokaryotic or eukaryotic cells. Expression of the compounds of the disclosure can be achieved used yeast, insect, or mammalian expression systems. The expressed polypeptides can be purified using methods known in the art. For example, a compounds of the disclosure may be purified by affinity chromatography using an appropriate monoclonal antibody or using the optional sequence tag disclosed herein. The purified polypeptides can be verified by using SDS page or Western Blot analysis, as is known in the art. Polypeptide Analog The present disclosure also contemplates the use of peptide analogs of the compounds of the disclosure, including peptides of SEQ ID NOS: 1-3. In one embodiment, the peptide analog contains one or more non-naturally occurring amino acids, D amino acids, modified amino- and/or carboxy-terminal (N- or C-terminal) amino acids, in particular modifications of the amino group on the N-terminus and/or modification of the carboxyl group in the C-terminus, fatty acid modifications, and/or esterification. In another embodiment, the peptide analog has one or more substitutions, insertions and/or deletions relative to a reference amino acid sequence. For example, a compounds of the disclosure may include one or more amino acid substitutions relative to a reference amino acid or sequence. For example, a peptide analog may include a non-conservative and/or conservative amino acid substitution relative to a reference polypeptide. Conservative amino acid substitutions are those substitutions that are predicted to interfere least with the properties of the reference polypeptide. Conservative amino acid substitutions generally maintain one or more of: (a) the structure of the polypeptide backbone in the area of the substitution, for example, as a beta sheet or alpha helical conformation, (b) the charge or hydrophobicity of the molecule at the site of the substitution, and/or (c) the bulk of the side chain. Logically, a non-conservative amino acid substitution will not generally maintain one or more of: (a) the structure of the polypeptide backbone in the area of the substitution, for example, as a beta sheet or alpha helical conformation, (b) the charge or hydrophobicity of the molecule at the site of the substitution, and/or (c) the bulk of the side chain. The following Table 2 provides a list of exemplary conservative and highly conservative amino acid substitutions. For example, a conservative amino acid substitution may involve a substitution of a native amino acid residue with a nonnative residue such that there is little or no effect on the polarity, steric bulk, charge, hydrophobicity and/or hydrophilicity of the amino acid residue at that position. Conservative amino acid substitutions also encompass non-naturally occurring amino acid residues which are typically incorporated by chemical peptide synthesis rather than by synthesis in biological systems. These include peptidomimetics, and other reversed or inverted forms of amino acid moieties. It will be appreciated by those of skill in the art that polypeptide described herein may be chemically synthesized as well as produced by recombinant means. In making an amino acid substitution as described herein, the hydropathic index of an amino acid may be considered. Each amino acid has been assigned a hydropathic index on the basis of their hydrophobicity and charge characteristics. Hydropathic index values are resented by: isoleucine (+4.5); valine (+4.2); leucine (+3.8); phenylalanine (+2.8); cysteine/cystine (+2.5); methionine (+1.9); alanine (+1.8); glycine (-0.4); threonine (-0.7); serine (-0.8); tryptophan (-0.9); tyrosine (-1.3); proline (-1.6); histidine (-3.2); glutamate (- 3.5); glutamine (-3.5); aspartate (-3.5); asparagine (-3.5); lysine (-3.9); and arginine (-4.5). The importance of the hydropathic amino acid index in conferring interactive biological function on a protein is understood in the art (Kyte et al., J. Mol. Biol., 157:105- 131, 1982). It is known that certain amino acids may be substituted for other amino acids having a similar hydropathic index or score and still retain a similar biological activity. In one embodiment, making changes based upon the hydropathic index, the substitution of amino acids whose hydropathic indices are within +/- 1; in an alternate embodiment, the hydropathic indices are within +/- 0.5; in yet another alternate embodiment, the hydropathic indices are within +/- 0.25. In making an amino acid substitution as described herein, the hydrophilicity may also be considered. In certain embodiments, the greatest local average hydrophilicity of a polypeptide as governed by the hydrophilicity of its adjacent amino acids, correlates with a biological property of the protein. The following hydrophilic index values have been assigned to amino acid residues: arginine (+3.0); lysine (+3.0); aspartate (+3.0.+-.1); glutamate (+3.0.+-.1); serine (+0.3); asparagine (+0.2); glutamine (+0.2); glycine (0); threonine (-0.4); proline (-0.5.+-.1); alanine (-0.5); histidine (-0.5); cysteine (-1.0); methionine (-1.3); valine (-1.5); leucine (-1.8); isoleucine (-1.8); tyrosine (-2.3); phenylalanine (-2.5); tryptophan (-3.4). In one embodiment, in making changes based upon similar hydrophilicity values, the substitution of amino acids whose hydrophilicity values are within +/- 1; in an alternate embodiment, the hydrophilicity values are within +/- 0.5; in yet another alternate embodiment, the hydrophilicity values are within +/- 0.25. A skilled artisan will be able to determine suitable substitutions, insertions and deletions, including combinations thereof, of a polypeptide as set forth in any of SEQ ID NOS: 1-3 using techniques known in the art. For identifying suitable areas of a polypeptide that may be changed without destroying activity, one skilled in the art may target areas not believed to be important for activity. For example, when homologous polypeptides with similar activities from the same species or from other species are known, one skilled in the art may compare the amino acid sequence of a polypeptide described herein to such homologous polypeptides. With such a comparison, one can identify residues and portions of the molecules that are conserved among similar polypeptides. It will be appreciated that changes in areas of a polypeptide described herein that are not conserved relative to such homologous polypeptide would be less likely to adversely affect the biological activity and/or structure of a polypeptide described herein. One skilled in the art would also know that, even in relatively conserved regions, one may substitute chemically similar amino acids for the naturally occurring residues while retaining activity (for example, conservative amino acid substitutions). Therefore, even areas that may be important for biological activity or for structure may be subject to such amino acid substitutions without destroying the biological activity or without adversely affecting the polypeptide structure. With regard to deletions, a peptide analog may be generated by deleting one or more amino acids from the amino-terminal portion and/or the carboxy-terminal portion of the amino acid sequence. The deletions, insertions, and substitutions can be selected, as would be known to one of ordinary skill in the art, to generate a desired peptide analog. For example, conservative amino acid substitutions and/or substitution of amino acids with similar hydrophilic and/or hydropathic index values is expected to be tolerated in a conserved region and a polypeptide activity may be conserved with such substitutions. In certain embodiments, the peptide analog is a mimetic or a pseudopeptide. The term “mimetic” refers to and encompass chemicals containing chemical moieties that mimic the function of a parent molecule, such as for example a peptide. For example, if a peptide contains two charged chemical moieties having functional activity, a mimetic places two charged chemical moieties in a spatial orientation and constrained structure so that the charged chemical function is maintained in three-dimensional space. Thus, a mimetic orients functional groups of a peptide or analog of the invention such that the functional activity of a peptide or analog is retained. Mimetics or peptidomimetics can include chemically modified peptides, peptide-like molecules containing non-naturally occurring amino acids, peptoids and the like, and have the functional activity of the peptide or analog upon which the peptidomimetic is derived (see, for example, Burger's Medicinal Chemistry and Drug Discovery 5th ed., vols. 1 to 3 (ed. M. E. Wolff; Wiley Interscience 1995)). Methods for identifying a peptidomimetic are well known in the art and include, for example, the screening of databases that contain libraries of potential peptidomimetics (Allen et al., Acta Crystallogr. Section B, 35:2331 (1979)) or using molecular modeling (Rusinko et al., J. Chem. Inf. Comput. Sci. 29:251 (1989)). Mimetics or peptidomimetics can provide desirable properties such as greater stability, for example, when administered to a subject, such as during passage through the digestive tract and, therefore, can be useful for oral administration. A variety of mimetics or peptidomimetics are known in the art including, but not limited to, peptide-like molecules which contain a constrained amino acid, a non-peptide component that mimics peptide secondary structure, or an amide bond isostere. A mimetic or peptidomimetic that contains a constrained, non-naturally occurring amino acid can include, without limitation, an α-methylated amino acid; α,α-dialkylglycine or α- aminocycloalkane carboxylic acid; an ^N α- ^C α-cyclized amino acid; an ^N α-methylated amino acid; a β- or γ-amino cycloalkane carboxylic acid; an α-, β-unsaturated amino acid; β-,β- dimethyl or β-methyl amino acid; a β-substituted-2,3-methano amino acid; an N--Cδ or ^C α- ^C δ cyclized amino acid; a substituted proline or another amino acid mimetic. A mimetic or peptidomimetic which mimics peptide secondary structure can contain, without limitation, a nonpeptidic β-turn mimic; .γ-turn mimic; or mimic of helical structure, each of which is well known in the art. As non-limiting examples, a peptidomimetic also can be a peptide-like molecule which contains an amide bond isostere such as a retro-inverso modification; reduced amide bond; methylenethioether or methylene-sulfoxide bond; methylene ether bond; ethylene bond; thioamide bond; trans-olefin or fluoroolefin bond; 1,5-disubstituted tetrazole ring; ketomethylene or fluoroketomethylene bond or another amide isostere. One skilled in the art understands that these and other mimetics or peptidomimetics of a peptide or analog of the invention can be used. The invention also provides pseudopeptide derivatives of peptides or analogs of the invention. Pseudopeptides are known in the art as peptides in which a peptide bond (amide bond) in a peptide is modified to an amide bond surrogate (see, for example, Cudic and Stawikowski, Mini-Rev Organic Chem. 4:268-280 (2007); Anderson, in Neuropeptide Protocols, Brent and Carvell, eds. 73:49-60 (1996)). Exemplary amide bond surrogates include, but are not limited to, peptidosulfonamides, phosphonopeptides, depsides and depsipeptides, oliogureas, azapeptides and peptoids (see Cudic and Stawikowski, supra, 2007) as well as as methylene amino, thioether and hydroxyethylene derivatives, and the like (Anderson, supra, 1996). The peptides or analogs of the invention can be produced using methods well known to those skilled in the art, including chemical synthesis of the peptides or analogs using well known methods of peptide synthesis, as described herein. Thus, when the peptides or analogs include one or more non-standard amino acids, it is more likely that they will be produced by a chemical synthetic method. In addition to using chemical synthesis of peptides or analogs, the peptides or analogs can be produced by expression from encoding nucleic acids. This is particularly useful for peptides or analogs that include only naturally occurring amino acids. In such a case, a nucleic acid encoding the peptide sequence can be prepared using well known methods (see Sambrook et al., Molecular Cloning: A Laboratory Manual, Third Ed., Cold Spring Harbor Laboratory, New York (2001); Ausubel et al., Current Protocols in Molecular Biology, John Wiley and Sons, Baltimore, Md. (1999)). Generally such a nucleic acid will be expressed recombinantly in a suitable host organism such as a bacterium, yeast, mammalian or insect cell, and the like. Production in bacteria can be particularly useful for large scale production of a peptide or analog of the invention. The peptide can be expressed in the organism and purified using well known purification techniques. Methods of Treatment and Use The compounds of the disclosure are useful for a variety of purposes. The compounds of the disclosure may be used in therapeutic methods as described herein, including methods for treating bacterial infection, neutrophil dysfunction, sepsis, trauma, immunosuppression associated with sepsis and/or trauma, organ injury associated with any of the foregoing (such as, but not limited to, ARDS, lung fibrosis, and COPD), or a symptom of any of the foregoing. In a first aspect, the present disclosure provides a method for treating a bacterial infection in a subject, the method comprising administering a compound of the disclosure, either alone or as a part of a pharmaceutical composition, to the subject. In one embodiment of this aspect, the infection is a bacterial infection. In another aspect of this embodiment, the present disclosure provides for a method of treating a bacterial infection in a subject with immunosuppression, including immunosuppression caused by sepsis and/or trauma. Such an infection, whether bacterial or of other origin, may lead to sepsis infection leads to sepsis. In another embodiment of this aspect, the infection, whether bacterial or of other origin, occurs secondary to immunosuppression, such as, but not limited to, immunosuppression caused by sepsis and/or trauma. Bacterial infections can be caused any bacterial organism; in one aspect, the bacterial infection is caused by an organism selected from the following: Pseudomonas aeruginosa, Pseudomonas fluorescens, Pseudomonas acidovorans, Pseudomonas alcaligenes, Pseudomonas putida, Stenotrophomonas maltophilia, Burkholderia cepacia, Aeromonas hydrophilia, Escherichia coli, Citrobacter freundii, Salmonella typhimurium, Salmonella typhi, Salmonella paratyphi, Salmonella enteritidis, Shigella dysenteriae, Shigella flexneri, Shigella sonnei, Enterobacter cloacae, Enterobacter aerogenes, Klebsiella pneumoniae, Klebsiella oxvtoca, Serratia marcescens, Francisella tularensis, Morganella morganii, Proteus mirabilis, Proteus vulgaris, Providencia alcalifaciens, Providencia rettgeri, Providencia stuartii, Acinetobacter baumannii, Acinetobacter calcoaceticus, Acinetobacter haemolyticus, Yersinia enterocolitica, Yersinia pestis, Yersinia pseudotuberculosis, Yersinia intermedia, Bordetella pertussis, Bordetella parapertussis, Bordetella bronchiseptica, Haemophilus influenzae, Haemophilus parainfluenzae, Haemophilus haemolyticus, Haemophilus parahaemolyticus, Haemophilus ducreyi, Pasteiirella multocida, Pasteiirella haemolytica, Branhamella catarrhalis, Helicobacter pylori, Campylobacter fetus, Campylobacter jejuni, Campylobacter coli, Borrelia burgdorferi, Vibrio cholerae, Vibrio parahaemolyticus, Legionella pneumophila, Listeria monocytogenes, Neisseria gonorrheal, Neisseria meningitidis, Kingella kingae, Moraxella, Peptococcus niger, Gardnerella vaginalis, Bacteroides fragilis, Bacteroides distasonis, Bacteroides caccae, Bacteroides vulgatiis, Bacteroides ovaliis, Bacteroides thetaiotaomicron, Bacteroides uniformis, Bacteroides eggerthii, Bacteroides splanchnicus, Clostridium difficile, Mycobacterium tuberculosis, Mycobacterium avium, Mycobacterium intracelliilare, Mycobacterium leprae, Corynebacterium diphtheriae, Corynebacterium ulcerans, Streptococcus pneumoniae, Streptococcus agalactiae, Streptococcus pyogenes, Enterococcus faecalis, Enterococcus faecium, Staphylococcus aureus, Staphylococcus epidermidis, Staphylococcus saprophytics, Staphylococcus intermedins, Staphylococcus hyicus subsp. hyicus, Staphylococcus haemolyticus, Staphylococcus hominis, or Staphylococcus saccharolyticus. In a particular embodiment of this aspect, the bacterial infection is caused by Pseudomonas aeruginosa. In a second aspect, the present disclosure provides a method for treating sepsis in a subject, the method comprising administering a compound of the disclosure, either alone or as a part of a pharmaceutical composition, to the subject. In one embodiment of this aspect, the sepsis is the result of a bacterial infection. In another embodiment of this aspect, the bacterial infection is caused by a bacteria listed in the first aspect. In another embodiment of this aspect, the method decreases sepsis-induced mortality and/or morbidity. In another embodiment of this aspect, the method decreases immunosuppression related to sepsis. In a third aspect, the present disclosure provides a method for treating trauma or blood loss resulting from trauma in a subject, the method comprising administering a compound of the disclosure, either alone or as a part of a pharmaceutical composition, to the subject. In one embodiment of this aspect, the method decreases trauma-induced mortality and/or morbidity. In another embodiment of this aspect, the method decreases immunosuppression resulting from trauma and/or blood loss related to trauma. In a fourth aspect, the present disclosure provides a method for treating immunosuppression in a subject, the method comprising administering a compound of the disclosure, either alone or as a part of a pharmaceutical composition, to the subject. The immunosuppression may be caused by a dysregulation of the innate immune response, such as, but not limited to, inhibition of one or more functions of a neutrophil. Specifically, the respiratory burst may be inhibited in a cell involved in the innate immune response, such as but not limited to a neutrophil. In one embodiment of this aspect, the immunosuppression results from a bacterial infection or sepsis. Such a bacterial infection or sepsis may be caused by a bacteria listed in the first aspect. In another embodiment of this aspect, the immunosuppression results from trauma or blood loss associated with trauma. The immunosuppression regardless of cause may be characterized by an increased expression and/or concentration of a DAMP in the subject, such as, but not limited to, HMGB1 protein, including its disulfide and oxidized forms (i.e., GSS-HMGB1). Such increased expression and/or concentration of a DAMP may occur in the circulation of a subject (the blood) or in a specific organ of the subject (such as the lung and other organs described herein in the fifth aspect). As a result of the administration, mortality and/or morbidity resulting from immunosuppression is decreased. In a fifth aspect, the present disclosure provides a method of treating organ injury or dysfunction in a subject, the method comprising administering a compound of the disclosure, either alone or as a part of a pharmaceutical composition, to the subject. The organ injury or dysfunction may be caused by dysregulation of the innate immune response or immunosuppression, including immunosuppression resulting from infection, sepsis, and/or trauma. In particular, the organ injury or dysfunction may be caused by inhibition of the respiratory burst in a cell involved in the innate immune response, such as but not limited to a neutrophil. Organ dysfunction or injury includes multiple organ dysfunction syndrome (MODS). Injured organs include, but are not limited to the spleen, liver, retroperitoneum, small bowel, kidneys, bladder, colorectum, diaphragm, heart, brain, lungs, and pancreas. In one embodiment of this aspect, the organ injury is lung injury. Therefore, in a specific embodiment of the fifth aspect the present disclosure provides a method of treating lung injury in a subject, the method comprising administering a compound of the disclosure, either alone or as a part of a pharmaceutical composition, to the subject. In one embodiment of this aspect, the lung injury contributes to the development of a lung condition selected from the group consisting of ARDS, lung fibrosis, idiopathic pulmonary fibrosis (IPF), and COPD. The lung injury may be caused by a bacteria listed in the first aspect. The lung injury may be caused by dysregulation of the innate immune response or immunosuppression, including immunosuppression resulting from infection, sepsis, and/or trauma. In particular, the lung injury may be caused by inhibition of the respiratory burst in a cell involved in the innate immune response, such as but not limited to a neutrophil, and/or the production of inflammatory mediators by a cell involved in the innate immune response, such as, but not limited to, a neutrophil and/or by the production of pro-inflammatory mediators produced by a cell involved in the innate immune response. In a sixth aspect, the present disclosure provides a method of treating a disease or condition associated immunosuppression, including, but not limited to, trauma-induced immunosuppression or sepsis-induced immunosuppression, the method comprising administering a compound of the disclosure, either alone or as a part of a pharmaceutical composition, to the subject. The disease or condition associated with immunosuppression may be an infection, including a bacterial infection, or organ dysfunction, such as, but not limited to lung dysfunction. In certain embodiments, the bacterial infection is caused by a bacterium listed in the first aspect. In certain embodiments, the organ dysfunction is ARDS, lung fibrosis, IPF, or COPD. In certain embodiments of this aspect, the immunosuppression may be caused by dysregulation of the innate immune response. In certain embodiments of this aspect, the immunosuppression is caused by inhibition of NOX2 activity, including inhibition of NOX2 activity mediated by binding of a DAMP to a component of NOX2 (such as, but not limited to, gp91 ^phox ). In particular, the immunosuppression may be caused by inhibition of the respiratory burst in a cell involved in the innate immune response, such as but not limited to a neutrophil, and/or the production of inflammatory mediators by a cell involved in the innate immune response, such as, but not limited to, a neutrophil, and/or by the production of pro-inflammatory mediators produced by a cell involved in the innate immune response. In a seventh aspect, the present disclosure provides a method of increasing NOX2 activity in a subject or preventing a decrease in NOX2 activity in a subject, the method comprising administering a compound of the disclosure, either alone or as a part of a pharmaceutical composition, to the subject. In one embodiment of this aspect, the subject is suffering from an infection, sepsis, and/or trauma. In another aspect of this embodiment, the subject is suffering from immunosuppression resulting from infection, sepsis and/or trauma. The infection or sepsis may be caused by a bacteria listed in the first aspect. In particular, the effect on NOX2 activity occurs in the a bodily fluid of the subject, such as the blood, blood plasma or BAL. Preferably, the effect on NOX2 activity occurs in an organ of the subject, such as the lung. In an eight aspect, the present disclosure provides a method of increasing an activity of a cell involved in the innate immune response in a subject or preventing a decrease in an activity of a cell involved in the innate immune response in a subject, the method comprising administering a compound of the disclosure, either alone or as a part of a pharmaceutical composition, to the subject. In one embodiment of this aspect, the subject is suffering from an infection, sepsis, and/or trauma. In another aspect of this embodiment, the subject is suffering from immunosuppression resulting from infection, sepsis and/or trauma. The infection or sepsis may be caused by a bacteria listed in the first aspect. The cell involved in the innate immune response may be a neutrophil and the activity of the neutrophil may be the respiratory burst. In a ninth aspect, the present disclosure provides a method of inhibiting a DAMP- mediated decrease in NOX2 activity in a subject, the method comprising administering a compound of the disclosure, either alone or as a part of a pharmaceutical composition, to the subject. In one embodiment of this aspect, the subject is suffering from an infection, sepsis, and/or trauma. In another aspect of this embodiment, the subject is suffering from immunosuppression resulting from infection, sepsis and/or trauma. The infection or sepsis may be caused by a bacteria listed in the first aspect. The DAMP may be HMGB1 protein, specifically HMGB1 protein in a disulfide form or an oxidized form (i.e., GSS-HMGB1). In a tenth aspect, the present disclosure provides a method of inhibiting binding of a DAMP to a component of NOX2 in a subject, the method comprising administering a compound of the disclosure, either alone or as a part of a pharmaceutical composition, to the subject. In one embodiment of this aspect, the subject is suffering from an infection, sepsis, and/or trauma. In another aspect of this embodiment, the subject is suffering from immunosuppression resulting from infection, sepsis and/or trauma. The infection or sepsis may be caused by a bacteria listed in the first aspect. The DAMP may be HMGB1 protein, specifically HMGB1 protein in a disulfide form or an oxidized form (i.e., GSS-HMGB1) and the component of NOX2 may be gp91 ^phox . In one embodiment of this aspect, the inhibition of binding results in an increase in NOX2 activity, such as, but not limited to, the respiratory burst. In another embodiment of this aspect, the inhibition of binding results in an increase in NOX2 activity, such as, but not limited to, the respiratory burst, in cell involved in the innate immune response, such as. But not limited to, a neutrophil. In an eleventh aspect, the present disclosure provides a method of reducing or preventing sepsis-induced mortality and morbidity in a subject, preventing or reducing inactivation of NOX2 in a subject, preventing or reducing inactivation of NOX2 in circulation and/or other bodily fluids of a subject, or decreasing the severity of conditions associated with neutrophil pro-inflammatory activation, including fibrosis, IPF, ARDS, and COPD, each of the foregoing in a clinical setting of infection, sepsis, or trauma or immunosuppression resulting from infection, sepsis, or trauma, the method comprising administering a compound of the disclosure, either alone or as a part of a pharmaceutical composition, to the subject. The methods of the first to eleventh aspects may further comprise first determining if a subject is in need of treatment. The methods of the first to eleventh aspects may further comprise first determining if a subject has an infection or sepsis. The methods of the first to eleventh aspects may further comprise first determining if a subject is immunosuppressed. In any of the methods of the first to eleventh aspects, the methods may be used for prophylactic treatment. In any of the methods of the first to eleventh aspects, the methods may be used for prophylactic treatment for subjects at risk of infection, sepsis, or organ dysfunction related to infection and/or sepsis/trauma-induced immunosuppression. When a condition in a subject is first detected, such as infection or sepsis for example, the methods of the first to eleventh aspects optionally include carrying out the tests to determine the presence or absence of the condition, such as for example, determining the identity or identities of bacteria that are causing an infection, the location of infection, and other laboratory based tests, such as a complete blood count, white blood cell count, C-reactive protein levels, and procalcitonin tests. Samples for testing include patient bodily fluids, such as blood, blood plasma, blood serum, aerosols (such as from a cough or a sneeze), mucous, cerebrospinal fluid, urine, saliva, tears, sputum, amniotic fluid, breast milk, semen, seminal fluid, vaginal secretions, and sweat. Samples for testing further include skin samples, such as those collected using a dry swab of a skin location, a moist swab of a mucosal surface, or a skin biopsy. Testing of bacteria include methods known in the art, such as bacterial culture, Gram staining, coagulase testing, catalase testing, polymerase chain reaction (PCR), and enzyme-linked immunosorbent assay (ELISA). Risk of infection is determined, in some instances, by the presence of bacteria, a concentration of bacteria, or bacteria above or below a threshold value. In any of the methods of the first to eleventh aspects, the compound of the disclosure (ant AI peptide) binds a mediator of immunosuppression in a bodily fluid of the subject. In certain embodiments, the mediator of immunosuppression is a DAMP, such as but not limited to, HMGB1, including disulfide linked forms and oxidized forms thereof (GSS- HMGB1). In any of the methods of the first to eleventh aspects, a pharmaceutical composition and/or medicaments comprising a compound of the disclosure may be used. In any of the methods of the first to eleventh aspects, the methods include administering to the subject an amount of a disclosed compound produced by methods of the present disclosure. In any of the methods of the first to eleventh aspects, administration may be undertaken by any route, including, but not limited to, intravenously, intraperitoneally, parenterally, intramuscularly, orally, rectally, intranasally (nose drops), by inhalation via the pulmonary system, topically, or transdermally. In any of the methods of the first to eleventh aspects, the compound of the disclosure may be administered in a pharmaceutically acceptable form. In any of the methods of the first to eleventh aspects, the methods may administration of an additional active agent known to be beneficial for a specific disease or condition, such as for example, administration of an antibiotic for an infection. Such additional active agent may increase the effectiveness of the administration of a compound of the disclosure. Additional active agents described herein or pharmaceutically acceptable forms thereof can be administered together in a single composition with a compound of the disclosure, or in separate compositions in any order, including simultaneous administration, as well as temporally spaced on the order of minutes, days, or weeks apart. In any of the methods of the first to eleventh aspects, the methods include a single administration of a compound of the disclosure or multiple administrations of a compound of the disclosure, optionally with additional active agents which may be administered as a single administration or multiple administrations. Administration of a compound of the disclosure and an additional active agent can be undertaken using the same or different routes of administration as described herein. In any of the methods of the first to eleventh aspects, the subject is a mammal. In any of the methods of the first to eleventh aspects, the subject is a human. In any of the methods of the first to eleventh aspects, the administering step comprises administering an effective amount of a compound of the disclosure, or a composition, such as a pharmaceutical composition, comprising a compound of the disclosure and a pharmaceutically acceptable carrier, to a subject. In any of the methods of the first to eleventh aspects, the compound of the disclosure is selected from the AI peptides set forth in any of SEQ ID NOS: 1-3 or an analog thereof. In any of the methods of the first to eleventh aspects, the compound of the disclosure is the AI peptide set forth in SEQ ID NO 3 or an analog thereof. In any of the methods of the first to eleventh aspects, the methods comprise administering one or more of the AI peptides set forth in SEQ ID NOS: 1-3 or an analog thereof, or a single AI peptide set forth in SEQ ID NOS: 1-3 or an analog thereof. In any of the methods of the first to eleventh aspects, the methods comprise administering one or more of the AI peptides set forth in SEQ ID NOS: 1-2 or an analog thereof, or SEQ ID NOS: 1 or 3, or an analog thereof. In any of the methods of the first to eleventh aspects, the methods comprise administering the AI peptides set forth in SEQ ID NO: 1 or an analog thereof, the AI peptides set forth in SEQ ID NO: 2 or an analog thereof, or the AI peptides set forth in SEQ ID NO: 3 or an analog thereof. In any of the methods of the first to eleventh aspects, the compound of the disclosure, including the AI peptides of SEQ ID NOS: 1-3 or analogs thereof, may be administered in a pharmaceutically acceptable form. Suitable pharmaceutically acceptable forms include, but are not limited to, salts, solvates, and hydrates. The present disclosure further provides methods of identifying mediators of infection-, sepsis- and trauma-mediated immunosuppression. The compounds of the disclosure and methods provide significant advantages over the prior art. Previous therapeutic interventions for infection-, sepsis- and trauma-mediated immunosuppression are generally limited to antibiotics and resuscitation strategies. The compounds of the disclosure provide an additional or alternative therapy that preserves neutrophil respiratory burst, the method involved in the eradication of pathogenic microbes. Moreover, neutrophil NOX2 activation and release of H2O2 have anti-inflammatory effects. Thus, AI peptides are capable of decreasing the severity of conditions associated with neutrophil pro-inflammatory activation, such as COPD, ARDS, and IPF. Dosage and Administration In accordance with the methods of the present disclosure, the compounds of the disclosure are administered to the subject (or are contacted with cells of the subject) in an effective amount. In certain embodiments, the effective amount of a compound of the disclosure is that which is effective, for example, to treat an infection, neutrophil dysfunction, sepsis, trauma, immunosuppression associated with sepsis and/or trauma, organ injury associated with any of the foregoing (such as, but not limited to, ARDS, lung fibrosis, IPF, and COPD), or a symptom of any of the foregoing. In certain embodiments, the effective amount of a compound of the disclosure enhances or otherwise improves the prophylactic or therapeutic effect(s) of another therapy, such as treatment with an additional active agent. In certain embodiments, the effective amount of a compound of the disclosure is that which reduces or eliminates the bacteria associated with a secondary bacterial infection after sepsis and/or trauma-induced immunosuppression. In certain embodiments, the effective amount of a compound of the disclosure is that which improves survival from an infection, neutrophil dysfunction, sepsis, trauma, immunosuppression associated with sepsis and/or trauma, or organ injury associated with any of the foregoing (such as, but not limited to, ARDS, lung fibrosis, IPF, and COPD). In certain embodiments, the effective amount of a compound of the disclosure ranges from about 0.1 mg/kg/day to about 50 mg/kg/day. In certain embodiments, the effective amount ranges from about 0.1 mg/kg/day to about 40 mg/kg/day. In certain embodiments, the effective amount ranges from about 0.1 mg/kg/day to about 30 mg/kg/day. In certain embodiments, the effective amount ranges from about 0.1 mg/kg/day to about 20 mg/kg/day. In certain embodiments, the effective amount ranges from about 0.1 mg/kg/day to about 10 mg/kg/day. In certain embodiments, the effective amount ranges from about 0.1 mg/kg/day to about 8 mg/kg/day. In certain embodiments, the effective amount ranges from about 0.1 mg/kg/day to about 6 mg/kg/day. In certain embodiments, the effective amount ranges from about 0.1 mg/kg/day to about 4 mg/kg/day. In certain embodiments, the effective amount ranges from about 0.1 mg/kg/day to about 3 mg/kg/day. In certain embodiments, the effective amount ranges from about 0.1 mg/kg/day to about 2 mg/kg/day. In certain embodiments, the effective amount ranges from about 0.1 mg/kg/day to about 1 mg/kg/day. In certain embodiments, the effective amount ranges from about 0.1 mg/kg/day to about 0.8 mg/kg/day. In certain embodiments, the effective amount ranges from about 0.1 mg/kg/day to about 0.6 mg/kg/day. In certain embodiments, the effective amount ranges from about 0.1 mg/kg/day to about 0.4 mg/kg/day. In certain embodiment, the effective amounts per day described above are administered according to a course of treatment and may be administered in a single dose or in more than 1 dose per day. Preferably, the effective amounts per day described above are administered according to a course of treatment and administered in one dose (q.d.) or two doses each day (b.i.d.), wherein the amount of the compound of the disclosure in each dose need not be the same. In certain embodiments, each dose is administered according to a course of treatment. As used herein, the term “dose” refers to an amount of a compound of the disclosure administered at a given time point according to a course of treatment. For example, if a course of treatment for a compound of the disclosure is b.i.d (2 times/administrations per day) for 7 days, the two administrations on each of days 1-7 would each comprise administering a dose of a compound of the disclosure (for 2 doses each day). In certain embodiments, a dose is administered q.d. (1 time/administration per day) according to a course of treatment. In certain embodiments, a dose is administered b.i.d. according to a course of treatment. In certain embodiments, a dose is administered t.i.d. (three times/administrations per day) according to a course of treatment. When 2 or more doses are administered on a given day according to a course of treatment, each dose administered according to the course of treatment may contain the same amount of a compound of the disclosure or one or more of doses administered according to the course of treatment may contain a greater or lesser amount of a compound of the disclosure as compared to another dose administered according to the course of treatment. For example, if a course of treatment for a compound of the disclosure is b.i.d for 7 days, the first dose administered on day 1 may contain a first amount (i.e., 2 mg/kg) and the second dose administered on day 1 may contain a second amount (i.e., 0.5 mg/kg). As another example, if a course of treatment for a compound of the disclosure is b.i.d for 7 days, the first dose administered on day 1 may contain a first amount (i.e., 2 mg/kg), the second dose administered on day 1 may contain a second amount (i.e., 0.5 mg/kg), the two doses administered on each of days 2-4 may contain the second amount, and the two doses administered on each of days 5-7 may contain a third amount (i.e., 1 mg/kg). A dose may be further divided into a sub-dose. Any given dose may be delivered in a single unit dose form or more than one unit dose form. For example, a dose when given by IV administration may be provided as a single IV infusion (i.e., a single 5 mg/kg IV infusion) or as two or more IV infusions administered one after the other (i.e., two 2.5 mg/kg IV infusions). Further, a sub-dose might be, for example, a number of discrete loosely spaced administrations, such as multiple inhalations from an insufflator, by application of a plurality of drops into the eye, or multiple tablets for oral administration. In certain embodiments, only one dose of a compound of the disclosure is administered during a course of treatment and no further doses are administered. Therefore, in the methods described herein the methods may comprise the administration of a single dose of an effective amount of a compound of the disclosure during the entire course of treatment. When a single dose is administered during the entire course of treatment, the course of treatment may be less than 4 weeks, such as 1 week, 2 weeks or three weeks. In certain embodiments, the single dose contain an effective amount of a compound of the disclosure. In certain embodiments, more than one dose of a compound of the disclosure is administered during a course of treatment. Therefore, in the methods described herein, the methods may comprise the administration of multiple doses during the course of treatment. In certain embodiments, the course of treatment may range from 2 days to 1 month, from 2 days to 3 weeks, from 2 days to 2 weeks, or from 2 days to 1 week. In certain embodiments, the course of treatment may range from 2 days to 6 days, from 2 days to 5 days, from 2 days to 4 days, or from 2 days to 3 days. In certain embodiments, a dose is delivered at least 1 time per day (i.e., 1 to 3 times) during the course of treatment. In certain embodiments, a dose is not administered every day during the course of treatment (for example, a dose is be administered at least 1 timer per day every other day, every third day, or every week during the course of treatment). Furthermore, the amount of a compound of the disclosure in each dose need not be the same as discussed above. In certain embodiments, of the foregoing, one or more doses, preferably all of the doses, contain an effective amount of a compound of the disclosure. In a preferred embodiment, a course of treatment may comprise administering at least one dose as a loading dose and at least one dose as a maintenance dose, wherein the loading dose contains a greater amount of a compound of the disclosure as compared to the maintenance dose (such as, but not limited to, 2 to 10 times higher). In one aspect of this embodiment, the loading dose is administered initially, either for a single administration or more than one administration, followed by administration of one or more maintenance doses through the remaining course of treatment. For example, for a course of treatment that is b.i.d. for 7 days, a loading dose of 5 mg/kg may be administered as the first dose on day 1 of the course of treatment, followed by maintenance doses of 2 mg/kg for the remainder of the course of treatment. As a further example, for a course of treatment that is b.i.d. for 7 days, a loading dose of 5 mg/kg may be administered as the first dose on day 1 of the course of treatment, followed by maintenance doses of 2 mg/kg as the second dose on day 1 and each dose on days 2-4, followed by maintenance doses of 1 mg/kg for the remainder of the course of treatment. Furthermore, a loading dose may be given as a dose that is not the first dose administered during a course of treatment. For example, a loading dose may be administered as the first dose on day 1 and as a dose one additional day (for example, day 4). For example, for a course of treatment that is b.i.d. for 7 days, a loading dose of 5 mg/kg may be administered as the first dose on day 1 of the course of treatment, followed by maintenance doses of 2 mg/kg as the second dose on day 1 and each dose on days 2-3, followed by a loading dose of 5 mg/kg as the first dose on day 4, followed by maintenance doses of 2 mg/kg for the remainder of the course of treatment. When more than one loading dose is administered during a course of treatment, the loading dose may be the same (i.e., 5 mg/kg) or different (i.e., 10 mg/kg for the first loading dose and 5 mg/kg for each other loading dose). Pharmaceutical compositions are provided that comprise an amount, preferably an effective amount, of a compound of the disclosure. In one embodiment, such pharmaceutical compositions contain an effective amount of a compound of the present disclosure. In a particular embodiment, the compound of the disclosure is a polypeptide have a sequence as set forth in any of SEQ ID NOS: 1-3 or an analog thereof. In a particular embodiment, the compound of the disclosure is at least one polypeptide having a sequence as set forth in SEQ ID NOS: 1-3 or an analog thereof. In addition, other active agents may be included in such pharmaceutical compositions. Additional active agents to be included may be selected based on the disease or condition to be treated. The pharmaceutical compositions disclosed may comprise one or more compound of the disclosure, alone or in combination with additional active agents, in combination with a pharmaceutically acceptable carrier and/or excipient. Such pharmaceutical compositions may be used in the manufacture of a medicament for use in the methods described herein. The compounds of the disclosure are useful in both free form and in the pharmaceutically acceptable forms, such as pharmaceutically acceptable salts. The pharmaceutically acceptable carriers and/or excipients are well-known to those who are skilled in the art. The choice of carrier and/or excipient will be determined in part by the particular compound(s), as well as by the particular method used to administer the compound composition. Accordingly, there is a wide variety of suitable formulations of the pharmaceutical composition of the present invention. The following methods and excipients are merely exemplary and are in no way limiting. Suitable carriers and excipients include solvents such as water, alcohol, and propylene glycol, solid absorbants and diluents, surface active agents, suspending agent, tableting binders, lubricants, flavors, and coloring agents. The pharmaceutically acceptable carriers can include polymers and polymer matrices. Examples of acceptable pharmaceutical carriers include carboxymethyl cellulose, crystalline cellulose, glycerin, gum arabic, lactose, magnesium stearate, methyl cellulose, powders, saline, sodium alginate, sucrose, starch, talc and water, among others. Typically, the pharmaceutically acceptable carrier is chemically inert to the active agents in the composition and has no detrimental side effects or toxicity under the conditions of use. Surfactants such as, for example, detergents, are also suitable for use in the formulations. Specific examples of surfactants include polyvinylpyrrolidone, polyvinyl alcohols, copolymers of vinyl acetate and of vinylpyrrolidone, polyethylene glycols, benzyl alcohol, mannitol, glycerol, sorbitol or polyoxyethylenated esters of sorbitan; lecithin or sodium carboxymethylcellulose; or acrylic derivatives, such as methacrylates and others, anionic surfactants, such as alkaline stearates, in particular sodium, potassium or ammonium stearate; calcium stearate or triethanolamine stearate; alkyl sulfates, in particular sodium lauryl sufate and sodium cetyl sulfate; sodium dodecylbenzenesulphonate or sodium dioctyl sulphosuccinate; or fatty acids, in particular those derived from coconut oil, cationic surfactants, such as water-soluble quaternary ammonium salts of formula N+R'R''R'''R''''Y- , in which the R radicals are identical or different optionally hydroxylated hydrocarbon radicals and Y- is an anion of a strong acid, such as halide, sulfate and sulfonate anions; cetyltrimethylammonium bromide is one of the cationic surfactants which can be used, amine salts of formula N+R'R''R''', in which the R radicals are identical or different optionally hydroxylated hydrocarbon radicals; octadecylamine hydrochloride is one of the cationic surfactants which can be used, non-ionic surfactants, such as optionally polyoxyethylenated esters of sorbitan, in particular Polysorbate 80, or polyoxyethylenated alkyl ethers; polyethylene glycol stearate, polyoxyethylenated derivatives of castor oil, polyglycerol esters, polyoxyethylenated fatty alcohols, polyoxyethylenated fatty acids or copolymers of ethylene oxide and of propylene oxide, amphoteric surfactants, such as substituted lauryl compounds of betaine. The compounds of the disclosure and pharmaceutical compositions containing such compounds as described in the instant disclosure can be administered by any conventional method available for use in conjunction with pharmaceuticals, either as individual therapeutic agents or in combination with additional therapeutic agents. In one embodiment, the compounds of the disclosure are administered in therapeutically effective amount, whether alone or as a part of a pharmaceutical composition. The therapeutically effective amount and the dosage administered will, of course, vary depending upon known factors, such as the pharmacodynamic characteristics of the particular agent and its mode and route of administration, the age, health and weight of the recipient; the severity and stage of the disease state or condition; the kind of concurrent treatment; the frequency of treatment; and the effect desired. The total amount of the compound administered will also be determined by the route, timing and frequency of administration as well as the existence, nature, and extent of any adverse side effects that might accompany the administration of the compound and the desired physiological effect. It will be appreciated by one skilled in the art that various conditions or disease states, in particular chronic conditions or disease states, may require prolonged treatment involving multiple administrations. In these pharmaceutical compositions, the compound(s) of the present disclosure will ordinarily be present in an amount of about 0.5-95% weight based on the total weight of the composition. Multiple dosage forms may be administered as part of a single treatment. The active agent can be administered enterally in solid dosage forms, such as capsules, tablets, and powders, or in liquid dosage forms, such as milk, elixirs, syrups and suspensions. It can also be administered parenterally, in sterile liquid dosage forms. The compound(s) of the present disclosure can also be administered intranasally (nose drops) or by inhalation via the pulmonary system, such as by propellant based metered dose inhalers or dry powders inhalation devices. Other dosage forms include topical administration, such as administration transdermally, via patch mechanism or ointment. Formulations suitable for enteral or oral administration may be liquid solutions, such as a therapeutically effective amount of the compound(s) dissolved in diluents, such as milk, water, saline, buffered solutions, infant formula, other suitable carriers, or combinations thereof. Formulations suitable for enteral or oral administration of the compounds of the disclosure are known in the art as exemplified by: Shaji, et al., Indian J Pharm Sci. 2008 May-Jun; 70(3): 269–277; Bruno, et al., Ther Deliv.2013 Nov; 4(11): 1443–1467; Ibrahim, et al., DARU Journal of Pharmaceutical Sciences, 2020, 28, 403–416. The compound(s) can then be mixed to the diluent just prior to administration. In an alternate embodiment, formulations suitable for enteral or oral administration may be capsules, sachets, tablets, lozenges, and troches. In each embodiment, the formulation may contain a predetermined amount of the compound(s) of the present disclosure, as solids or granules, powders, suspensions and suitable emulsions. Liquid formulations may include diluents, such as water and alcohols, for example, ethanol, benzyl alcohol, propylene glycol, glycerin, and the polyethylene alcohols, either with or without the addition of a pharmaceutically acceptable surfactant, suspending agent, or emulsifying agent. Capsule forms can be of the ordinary hard- or soft-shelled gelatin type containing, for example, surfactants, lubricants, and inert fillers, such as lactose, sucrose, calcium phosphate, and corn starch. Tablet forms can include one or more of the following: lactose, sucrose, mannitol, corn starch, potato starch, alginic acid, microcrystalline cellulose, acacia, gelatin, guar gum, colloidal silicon dioxide, croscarmellose sodium, talc, magnesium stearate, calcium stearate, zinc stearate, stearic acid, and other excipients, colorants, diluents, buffering agents, disintegrating agents, moistening agents, preservatives, flavoring agents, and pharmacologically compatible carriers. Lozenge forms can comprise the active ingredient in a flavor, usually sucrose and acacia or tragacanth, as well as pastilles comprising the active ingredient in an inert base, such as gelatin and glycerin, or sucrose and acadia, emulsions, and gels containing, in addition to the active ingredient, such carriers as are known in the art. Formulations suitable for parenteral administration include aqueous and non- aqueous, isotonic sterile injection solutions, which can contain anti-oxidants, buffers, bacteriostats, and solutes that render the formulation isotonic with the blood of the patient, and aqueous and non-aqueous sterile suspensions that can include suspending agents, solubilizers, thickening agents, stabilizers, and preservatives. The compound(s) can be administered in a physiologically acceptable diluent in a pharmaceutically acceptable carrier, such as a sterile liquid or mixture of liquids, including water, saline, aqueous dextrose and related sugar solutions, an alcohol, such as ethanol, isopropanol, or hexadecyl alcohol, glycols, such as propylene glycol or polyethylene glycol such as poly(ethyleneglycol) 400, glycerol ketals, such as 2,2-dimethyl-1,3-dioxolane-4-methanol, ethers, an oil, a fatty acid, a fatty acid ester or glyceride, or an acetylated fatty acid glyceride with or without the addition of a pharmaceutically acceptable surfactant, such as a soap or a detergent, suspending agent, such as pectin, carbomers, methylcellulose, hydroxypropylmethylcellulose, or carboxymethylcellulose, or emulsifying agents and other pharmaceutical adjuvants. Oils, which can be used in parenteral formulations include petroleum, animal, vegetable, or synthetic oils. Specific examples of oils include peanut, soybean, sesame, cottonseed, corn, olive, petrolatum, and mineral. Suitable fatty acids for use in parenteral formulations include oleic acid, stearic acid, and isostearic acid. Ethyl oleate and isopropyl myristate are examples of suitable fatty acid esters. Suitable soaps for use in parenteral formulations include fatty alkali metal, ammonium, and triethanolamine salts, and suitable detergents include (a) cationic detergents such as, for example, dimethyldialkylammonium halides, and alkylpyridinium halides, (b) anionic detergents such as, for example, alkyl, aryl, and olefin sulfonates, alkyl, olefin, ether, and monoglyceride sulfates, and sulfosuccinates, (c) nonionic detergents such as, for example, fatty amine oxides, fatty acid alkanolamides, and polyoxyethylene polypropylene copolymers, (d) amphoteric detergents such as, for example, alkyl .beta.-aminopropionates, and 2-alkylimidazoline quaternary ammonium salts, and (e) mixtures thereof. The parenteral formulations typically contain from about 0.5% to about 50% by weight of the compound(s) in solution. Suitable preservatives and buffers can be used in such formulations. In order to minimize or eliminate irritation at the site of injection, such compositions may contain one or more nonionic surfactants having a hydrophile-lipophile balance (HLB) of from about 12 to about 17. The quantity of surfactant in such formulations ranges from about 5% to about 15% by weight. Suitable surfactants include polyethylene sorbitan fatty acid esters, such as sorbitan monooleate and the high molecular weight adducts of ethylene oxide with a hydrophobic base, formed by the condensation of propylene oxide with propylene glycol. The compound(s) of the present disclosure can be formulated into aerosol formulations to be administered via nasal or pulmonary inhalation. These aerosol formulations can be placed into pressurized acceptable propellants, such as dichlorodifluoromethane, propane, and nitrogen. Such aerosol formulations may be administered by metered dose inhalers. They also may be formulated as pharmaceuticals for non-pressured preparations, such as in a nebulizer or an atomizer. The compound(s) of the present disclosure, alone or in combination with other suitable components, may be administered in an aqueous solution as a nasal or pulmonary spray and may be dispensed in spray form by a variety of methods known to those skilled in the art. Systems for dispensing liquids as a nasal spray are disclosed in U.S. Pat. No. 4,511,069. The formulations may be presented in multi-dose containers, for example in the sealed dispensing system disclosed in U.S. Pat. No.4,511,069. Additional aerosol delivery forms may include, e.g., compressed air-, jet-, ultrasonic-, and piezoelectric nebulizers, which deliver the active agent dissolved or suspended in a pharmaceutical solvent, e.g., water, ethanol, or a mixture thereof. Nasal and pulmonary solutions of the present invention typically comprise the drug or drug to be delivered, optionally formulated with a surface-active agent, such as a nonionic surfactant (e.g., polysorbate-80), and one or more buffers. In some embodiments of the present invention, the nasal spray solution further comprises a propellant. The pH of the nasal spray solution is optionally between about pH 3.0 and 6.0, preferably 4.5.+-.0.5. Suitable buffers for use within these compositions are as described above or as otherwise known in the art. Other components may be added to enhance or maintain chemical stability, including preservatives, surfactants, dispersants, or gases. Suitable preservatives include, but are not limited to, phenol, methyl paraben, paraben, m-cresol, thiomersal, chlorobutanol, benzylalkonimum chloride, and the like. Suitable surfactants include, but are not limited to, oleic acid, sorbitan trioleate, polysorbates, lecithin, phosphatidyl cholines, and various long chain diglycerides and phospholipids. Suitable dispersants include, but are not limited to, ethylenediaminetetraacetic acid, and the like. Suitable gases include, but are not limited to, nitrogen, helium, chlorofluorocarbons (CFCs), hydrofluorocarbons (HFCs), carbon dioxide, air, and the like. Within alternate embodiments, nasal and pulmonary formulations are administered as dry powder formulations comprising the active agent in a dry, usually lyophilized, form of an appropriate particle size, or within an appropriate particle size range, for intranasal delivery. Minimum particle size appropriate for deposition within the nasal or pulmonary passages is often about 0.5 µm. mass median equivalent aerodynamic diameter (MMEAD), commonly about 1 µm MMEAD, and more typically about 2 µm MMEAD. Maximum particle size appropriate for deposition within the nasal passages is often about 10 µm MMEAD, commonly about 8 µm MMEAD, and more typically about 4 µm MMEAD. Intranasally and pulmonaryly respirable powders within these size ranges can be produced by a variety of conventional techniques, such as jet milling, spray drying, solvent precipitation, supercritical fluid condensation, and the like. These dry powders of appropriate MMEAD can be administered to a patient via a conventional dry powder inhaler (DPI), which relies on the patient's breath, upon pulmonary or nasal inhalation, to disperse the power into an aerosolized amount. Alternatively, the dry powder may be administered via air-assisted devices that use an external power source to disperse the powder into an aerosolized amount, e.g., a piston pump. To formulate compositions for nasal or pulmonary delivery, the active agent can be combined with various pharmaceutically acceptable additives, as well as a base or carrier for dispersion of the active agent(s). Desired additives include, but are not limited to, pH control agents, such as arginine, sodium hydroxide, glycine, hydrochloric acid, citric acid, etc. In addition, local anesthetics (e.g., benzyl alcohol), isotonizing agents (e.g., sodium chloride, mannitol, sorbitol), adsorption inhibitors (e.g., Tween 80), solubility enhancing agents (e.g., cyclodextrins and derivatives thereof), stabilizers (e.g., serum albumin), and reducing agents (e.g., glutathione) can be included. When the composition for nasal or pulmonary delivery is a liquid, the tonicity of the formulation, as measured with reference to the tonicity of 0.9% (w/v) physiological saline solution taken as unity, is typically adjusted to a value at which no substantial, irreversible tissue damage will be induced in the nasal mucosa at the site of administration. Generally, the tonicity of the solution is adjusted to a value of about 1/3 to 3, more typically 1/2 to 2, and most often 3/4 to 1.7. The compound(s) of the present disclosure may be dispersed in a base or vehicle, which may comprise a hydrophilic compound having a capacity to disperse the active agent and any desired additives. The base may be selected from a wide range of suitable carriers, including but not limited to, copolymers of polycarboxylic acids or salts thereof, carboxylic anhydrides (e.g., maleic anhydride) with other monomers (e.g., methyl (meth)acrylate, acrylic acid, etc.), hydrophilic vinyl polymers such as polyvinyl acetate, polyvinyl alcohol, polyvinylpyrrolidone, cellulose derivatives such as hydroxymethylcellulose, hydroxypropylcellulose, etc., and natural polymers such as chitosan, collagen, sodium alginate, gelatin, hyaluronic acid, and nontoxic metal salts thereof. Often, a biodegradable polymer is selected as a base or carrier, for example, polylactic acid, poly(lactic acid- glycolic acid) copolymer, polyhydroxybutyric acid, poly(hydroxybutyric acid-glycolic acid) copolymer and mixtures thereof. Alternatively or additionally, synthetic fatty acid esters such as polyglycerin fatty acid esters, sucrose fatty acid esters, etc. can be employed as carriers. Hydrophilic polymers and other carriers can be used alone or in combination, and enhanced structural integrity can be imparted to the carrier by partial crystallization, ionic bonding, crosslinking and the like. The carrier can be provided in a variety of forms, including, fluid or viscous solutions, gels, pastes, powders, microspheres and films for direct application to the nasal mucosa. The use of a selected carrier in this context may result in promotion of absorption of the active agent. The compounds of the disclosure may alternatively contain as pharmaceutically acceptable carriers substances as required to approximate physiological conditions, such as pH adjusting and buffering agents, tonicity adjusting agents, wetting agents and the like, for example, sodium acetate, sodium lactate, sodium chloride, potassium chloride, calcium chloride, sorbitan monolaurate, triethanolamine oleate, etc. For solid compositions, conventional nontoxic pharmaceutically acceptable carriers can be used which include, for example, pharmaceutical grades of mannitol, lactose, starch, magnesium stearate, sodium saccharin, talcum, magnesium carbonate, and the like. Compositions of the present disclosure can also be formulated as a solution, microemulsion, or other ordered structure suitable for high concentration of active ingredients. The carrier can be a solvent or dispersion medium containing, for example, water, ethanol, polyol (for example, glycerol, propylene glycol, and liquid polyethylene glycol, and the like), and suitable mixtures thereof. Proper fluidity for solutions can be maintained, for example, by the use of a coating such as lecithin, by the maintenance of a desired particle size in the case of dispersible formulations, and by the use of surfactants. In certain embodiments, compound(s) and compositions of the present disclosure are administered in a time-release formulation, for example in a composition which includes a slow release polymer. Such compositions can be prepared with carriers that will protect against rapid release, for example a controlled release vehicle such as a polymer, microencapsulated delivery system or bioadhesive gel. Prolonged delivery, in various compositions of the invention can be brought about by including in the composition agents that delay absorption, for example, aluminum monosterate hydrogels and gelatin. When controlled release formulations is desired, controlled release binders suitable for use in accordance with the invention include any biocompatible controlled-release material which is inert to the active agent and which is capable of incorporating the biologically active agent. Numerous such materials are known in the art. Formulations suitable for topical administration include creams, emulsions, and gels containing, in addition to the active ingredient, such carriers as are known in the art. The compounds of the disclosure and compositions of the present disclosure can be presented in unit-dose or multi-dose sealed containers, such as ampules and vials, and can be stored in a freeze-dried (lyophilized) condition requiring only the addition of the sterile liquid excipient, for example, water, for injections, immediately prior to use. Suitable unit doses, i.e., therapeutically effective amounts, may be determined during clinical trials designed appropriately for each of the conditions for which administration of a chosen compound is indicated and will, of course, vary depending on the desired clinical endpoint. Extemporaneous injection solutions and suspensions can be prepared from sterile powders, granules, and tablets. The requirements for effective pharmaceutically acceptable carriers for injectable compositions are well known to those of ordinary skill in the art. See Pharmaceutics and Pharmacy Practice, J.B. Lippincott Co., Philadelphia, Pa., Banker and Chalmers, Eds., 238-250 (1982) and ASHP Handbook on Injectable Drugs, Toissel, 4 ^th ed., 622-630 (1986). Additionally, formulations suitable for rectal administration may be presented as suppositories by mixing with a variety of bases such as emulsifying bases or water-soluble bases. Formulations suitable for vaginal administration may be presented as pessaries, tampons, creams, gels, pastes, foams, or spray formulas containing, in addition to the active ingredient, such carriers as are known in the art to be appropriate. One skilled in the art will appreciate that suitable methods of administering a compound of the present invention to an patient are available, and, although more than one route can be used to administer a particular compound, a particular route can provide a more immediate and more effective reaction than another route. Additional Therapeutic Agents In addition, the compositions or methods described herein may further comprise one or more additional active agents in combination with a compound of the disclosure. Indeed, it is a further aspect of the disclosure to provide methods for enhancing prior art therapies and/or pharmaceutical compositions by co-administering a compound of the disclosure with an additional active agent. In co-administration procedures, the additional agents may be administered concurrently or sequentially. In one embodiment, the compound of the disclosure is administered prior to an additional active agent(s). The pharmaceutical formulations and modes of administration may be any of those described above. In addition, the one or more co-administered additional agents may each be administered using different modes or different formulations. The additional agent or agents to be co-administered depends on the type of condition being treated. For example, in some embodiments, the additional agent is an antibiotic, pain reliever (e.g., NSAID) or anti-viral agent. Non-limiting examples of antibiotics include penicillins (e.g., natural penicillins, penicillinase-resistant penicillins, antipseudomonal penicillins, aminopenicillins), tetracyclines, macrolides (e.g., erythromycin), lincosamides (e.g., clindamycin), streptogramins (e.g., Synercid), aminoglycosides, and sulfonamides. Non-limiting examples of such anti-viral agents include, but are not limited to, neuraminidase inhibitors, viral polymerase inhibitors, viral end cap snatchers, water soluble metal salts, including zinc metal salts, and lectins. In addition, “anti-viral agents” include other compounds familiar to one of skill in the art including, for example, various polymers such as naphthalene sulfonates and other sulfated or sulfonated polymers (McCormack S et al., Lancet, 2010 Oct.16; 376(9749):1329-37). Kits The present disclosure also provides a kit for use in the methods described herein, the kit comprising a compound of the disclosure, or a pharmaceutically acceptable form thereof, and at least one of the following: (i) at least one other therapeutic agent; (ii) packaging material; (iii) instructions for administering the compound of the disclosure, or pharmaceutically acceptable form thereof and the other therapeutic agent or agents to a subject to treat a subject. In one embodiment, the present disclosure provides a kit comprising a polypeptide as set forth in any of SEQ ID NOS: 1-3 or an analog thereof, or a pharmaceutically acceptable form of the foregoing, and at least one of the following: (i) at least one other therapeutic agent; (ii) packaging material; (iii) instructions for administering the compound of the disclosure, or pharmaceutically acceptable form thereof and the other therapeutic agent or agents to a subject to treat a subject. In one embodiment, the present disclosure provides a kit comprising more than one of the polypeptides set forth in SEQ ID NOS: 1-3 or an analog thereof, or a pharmaceutically acceptable form of the foregoing, and at least one of the following: (i) at least one other therapeutic agent; (ii) packaging material; (iii) instructions for administering the compound of the disclosure, or pharmaceutically acceptable form thereof and the other therapeutic agent or agents to a subject to treat a subject. In one embodiment, the present disclosure provides a kit comprising the polypeptide as set forth in SEQ ID NO: 1 or an analog thereof, or a pharmaceutically acceptable form of the foregoing, and the polypeptide as set forth in SEQ ID NO: 3 or an analog thereof, or a pharmaceutically acceptable form of the foregoing, and at least one of the following: (i) at least one other therapeutic agent; (ii) packaging material; (iii) instructions for administering the compound of the disclosure, or pharmaceutically acceptable form thereof and the other therapeutic agent or agents to a subject to treat a subject. In one embodiment, the present disclosure provides a kit comprising the polypeptide as set forth in SEQ ID NO: 3 or an analog thereof, or a pharmaceutically acceptable form of the foregoing, and at least one of the following: (i) at least one other therapeutic agent; (ii) packaging material; (iii) instructions for administering the compound of the disclosure, or pharmaceutically acceptable form thereof and the other therapeutic agent or agents to a subject to treat a subject. In one embodiment of the kits disclosed, the subject is a human. In another embodiment of the kits disclosed, the compound of the disclosure has a polypeptide sequence including, but not limited to all or any of the sequences set forth in any of SEQ ID NOS: 1-3. EXAMPLES Materials and Methods Trauma patients for the following studies were admitted to the University of Alabama at Birmingham from January to December 2018. This study was approved by the University of Alabama at Birmingham Institutional Review Board. Inclusion criteria were blunt or penetrating trauma, Level I activation and systolic blood pressure of <90mmHg, respiratory compromise or placement of an advanced airway or a Glasgow Coma Score of <9. Patients were excluded if they were <19 years old, consent was denied, not returned or not obtainable due to no family available for consenting. Patients were also excluded if they had a bleeding diathesis or were known to take anti-coagulant medications, had known liver disease, were pregnant, were incarcerated, or expired within 1 hour of admission. A blood sample (10 ml) was drawn after admission to the Emergency Department, but before fluid resuscitation. Whole blood was collected via a central line in acid citrate dextrose (ACD) vacutainers. Plasma was collected, separated and stored for up to 24 hours at 4 °C. Next, plasma was frozen in liquid nitrogen, and for long-term storage kept at −80 °C. Blood samples (10 ml) were also collected from healthy volunteers. For mice studies, all experiments were conducted in accordance with approved protocols by the University of Alabama at Birmingham Institutional Animal Care and Use Committee. Male C57BL/6 mice were purchased from The Jackson Laboratory (Bar Harbor, ME). Mice 10 to 12 weeks of age were used for experiments. Mice were given food and water ad libitum and kept on a 12-hours light-dark cycle. For a mouse model for sepsis-induced immunosuppression, cecal ligation and puncture (CLP) was performed in 10- to 12- week-old male C57BL/6 mice as described before (see D. Rittirsch et al., Nat. Protoc.4, 31-36, 2009). Briefly, the cecum was ligated for about 20-30% from a distal site of cecum (about 500 mm from the tip of cecum). A through-and-through puncture was performed with a 21-gauge needle and then a drop of feces was extruded to the peritoneal cavity. Saline (0.9%; 500 μl) was then applied into the peritoneal cavity and the abdominal wall incision was closed in two layers. The control group of mice (sham) underwent surgery without CLP. For P. aeruginosa-induced pneumonia, mice were anesthetized with isoflurane and then suspended by their upper incisors on a 60° incline board. The tongue was gently extended and Pseudomonas aeruginosa strain K (PAK; 2.5 × 10 ⁷ /mouse) suspension in PBS (50 μl) or PBS alone (control; 50 μl) was deposited into the pharynx, followed by bacterial aspiration into the lungs, similar to the method that was described previously (see J. Zmijewski et al., Am. J. Respir. Crit. Care Med. 178, 168-179, 2008). Lung homogenates were prepared 4 hours after PAK instillation and serial dilutions used to determine bacterial counts. Bacterial colonies were grown on agar plates and colony forming units (CFUs) were counted the following day. In selected experiments, mice were subjected to HMGB1 (25 µg/mouse; i.t.), which was administered about 30 minutes prior to PAK instillation (2.5 × 10 ⁷ /mouse) for about 4 hours. For mouse models for peritonitis, peritonitis was induced in mice (subjected to intraperitoneal injection of E. coli (2 × 10 ⁸ ). Selected or combined AI peptides (2.5 µg/mouse; i.p.) were administered about 2 hours after injection of bacteria. Mice viability was recorded during the 96 hours post E. coli injection. The reagents and antibodies used included: Hanks’ Balanced Salt Solution (HBSS), RPMI-1640, LPS, Antimycin A, Tunicamycin, Phorbol-12-myristate 13-acetate (PMA), and cytochrome c, purchased from Sigma-Aldrich (St. Louis, MO). Fetal Bovine Serum (FBS) was purchased from R&D Systems (Minneapolis, MN). F-12K medium, Alexa Flour 594 NHS ester, and Apex Alexa Flour 488 Antibody labeling Kit, 3,3’,5,5’- tetramethylbenzidine (TMB), Neutra-Avidin Agarose, Glutathione Ethyl Ester Biotin Amide (BioGEE), Streptavidin-HRP, Protein A/G Agarose, Zeba Spin desalting columns, and dextran were purchased from Thermo Fisher Scientific (Waltham, MA). Antibodies to HMGB1 were from Abcam (Cambridge, MA). Anti-gp91 ^phox , β-actin and Horse Radish Peroxidase (HRP)-conjugated antibodies were from Santa Cruz Biotechnology (Santa Cruz, CA). Antibodies to 6xHis-HRP, Anti-HMGB1-Alexa594, Ultra-LEAF purified Mouse IgG2b, k isotype control antibody and Ultra-Leaf purified anti-HMGB1 neutralizing antibody were obtained from BioLegend (San Diego CA). HMGB1 and 6xHis-HMGB1 recombinant proteins were obtained from GENWAY Biotech Inc. (San Diego, CA), whereas reduced and disulfide HMGB1 recombinant proteins were purchased from Tecan US, Inc. (Morrisville, NC). Mounting emulsion containing 4′,6-diamidino-2-phenylindole (DAPI) was from Vector Laboratories (Burlingame, CA) and Hoechst dye from Life Technologies (Grand Island, NY). Superoxide Dismutase Assay Kit was obtained from Cayman Chemical (Ann Arbor, MI). In neutrophil respiratory burst studies, PMA-dependent activation of NOX2 was carried out using cytochrome c reduction assay, as described previously (see J. M. Tadie et al., Am. J. Physiol. Cell Physiol.302, C249-256, 2012). Briefly, human neutrophils (blood neutrophils or HL-60 neutrophil cell line; 8 × 10 ⁵ ) suspended in phenol free RPMI-1640 media (serum free; 200 μl) were incubated in a humidified incubator for 30 min, at 37 ^◦ C (5% CO ₂ ). Next, healthy donor (HD) or trauma/hemorrhage (T/H) plasma (500 μg/ml) was added to the neutrophil culture for an additional 30 min. Respiratory burst was measured after inclusion of Cytochrome C (160 μM) and PMA (16 μM). Cytochrome C reduction was recorded at Abs 550 nm for 10–15 min, using an Evolution 201 UV–visible spectrophotometer (Thermo Fisher Scientific, Waltham, MA). To determine the effect of anti-immunosuppression (Ai)-Peptides, plasma samples (500 μg/ml) were prepared in serum free media (RPMI-1640) and incubated with AI peptides (0 or 2.5 μg/ml) for 30 min, followed by inclusion of neutrophils. The impact of HMGB1 (recombinant) on NOX2 activity was evaluated using mouse peritoneal (mature) isolated from 2 to 3 mice/per experiment. Peritoneal neutrophils (8 × 10 ⁵ cells/sample) were incubated with HMGB1 (0 or 1 μg/ml) for 20 min at 37 ^◦ C, followed by stimulation with PMA (16 μM) and recording the NOX2 activity rates using cytochrome C reduction assay. Linear rates were used to calculate NOX2 activity. For fluorescent labeling of HMGB1 and anti-gp91 ^phox IgG, fluorescent HMGB1 (HMGB1-FL) and anti-gp91 ^phox IgG (anti-gp91 ^phox FL) were generated using Apex Antibody/Protein Labeling Kit from Thermo Fisher Scientific (Waltham, MA) and used according to the manufacturer’s protocol. Anti-gp91 ^phox IgG (goat) were obtained from Invitrogen (# PA5-19010). Neutrophil polymorphonuclear granulocytes (PMNs) were isolated from healthy donors using whole blood separation technique with Dextran 500 and a standard density gradient separation, as previously described (see H. Oh et al., J Vis. Exp. (17):745, 2008). This method provided samples of ˃95% neutrophils with ˃95% viability. Human neutrophils (HL-60) were obtained from ATCC. Cells were cultured in RPMI-1640 media supplemented with 8% heat-inactivated FBS. Cells differentiated into the neutrophil phenotype by inclusion of DMSO (1.3%) into RPMI-1640 (8% FBS) media for 3-5 days. For peritoneal macrophage and bone marrow neutrophil isolation and culture, mouse peritoneal neutrophils and macrophages were isolated as previously described (see D. W. Park et al., Am. J. Physiol. Lung Cell Mol. Physiol. 307, L735-745, 2014). Macrophages were elicited in 10- to 12- week-old mice by intraperitoneal application of Brewer thioglycollate (Sigma-Aldrich, B2551). Mouse bone marrow neutrophils were collected using negative selection column purification, as described previously (see Z. Liu et al., Mol. Med.21:937–950, 2015). Cells were cultured in RPMI-1640 media supplemented with FBS (8%). For alveolar epithelial cell culture studies, L2 alveolar epithelial cells (ATCC) were cultured using F-12K media supplemented with 8% FBS. In selected experiments, cells were incubated with Tunicamycin for 16 hours followed by fluorescence microscope analysis of HMGB1 subcellular localization. TNF-α ELISA was used to measure cytokine levels in culture media, as described previously (see D. W. Park et al., Am. J. Physiol. Lung Cell Mol. Physiol.307, L735-745, 2014). The levels of TNF-α was determined according to manufacturer’s instruction (R&D Systems, Minneapolis, MN). For binding of AI peptides with recombinant HMGB1 studies, high-binding enzyme immunoassay/RIA plates (Costar) were coated with HMGB1 recombinant (1 µg/ml PBS) for 16 hours at 4 ^o C. Next, wells were incubated with BSA (1%) for 2 hours, washed and followed by inclusion of Bio-AI peptide 1 or 3 (peptides tagged with biotin; 1 µg/ml) for an additional 4 hours at room temperature. The amounts of AI peptides bound to HMGB1 were detected using Streptavidin-HRP and TMB as a substrate. Samples were measured at OD 450 nm using a microplate reader POLARstar Optima (BMG Labtech). Western blot analysis was performed as described previously (see S. Rangarajan, et al., Nat. Med.24:1121–1127, 2018). Each experiment was carried out three of more times, including neutrophil and macrophage populations obtained from separate groups of mice. Reduced HMGB1 was generated using HGMB1 recombinant [Tris-HCl pH 7.6 (50 mM)] that was incubated with DTT (20 mM) for 60 minutes, at 37°C. DTT was removed using a buffer exchange system (Zeba Spin desalting columns). S-glutathionylation of HMGB1 (GSS-Cys106) was conducted by incubation of HMGB1 (disulfide; 10 µg) recombinant protein with BioGEE (0.5 mM) or GSH (0.5 mM), and H ₂ O ₂ (50 μM) for 30 minutes, at room temperature. Oxidized HMGB1 was purified using a buffer exchange system (Zeba Spin desalting columns). To confirm BioGEE-HMGB1 adduct formation, samples were prepared in non-reducing or reducing SDS loading buffer followed by Western blot analysis with Avidin-HRP and anti-HMGB1 antibody. For detection of GSS-protein adduct formations in vivo, peritoneal macrophage (6 x 10 ⁶ ) suspended in RPMI-1640 medium (400 μl) were incubated with or without BioGEE (0.5 mM) for 2 hours. Cells were washed and treated with Antimycin A (0 or 10 μM) for 5 hours. The amounts of BioGSS-protein adducts in cell lysates and culture media were determined using non-reducing SDS-PAGE and Western blot analysis with Avidin-HRP. Bio-GSS-HMGB1 in culture media (3.5 ml) or macrophage lysates (500 µg/ml) were measured after subsequent Streptavidin-agarose pull-down assay, reducing SDS-PAGE and Western Blot analysis with anti-HMGB1 IgG. For macrophage and AECs fluorescent imaging, macrophages and AECs were prepared on rounded coverslips and imaged as described previously (see S. Rangarajan, et al., Nat. Med. 24:1121–1127, 2018). For peritoneal neutrophils imaging, peritoneal neutrophils (10 ⁶ /ml HBSS buffer) in centrifuge tubes were incubated with HMBG1-FL (1 µg) for 10 minutes, followed by inclusion of anti-gp-91 ^phox -FL IgG (100 ng) and Hoechst 33342 (5 µM) for an additional 10 minutes, at 37 ^o C. After wash with PBS, cells were placed in glass bottom containers (Nunc Lab-Tek system, Sigma-Aldrich, MO) and images of live cells were acquired using a BZ-X710 All-in-One fluorescence microscope (Keyence Corporation of America, Itasca, IL, USA). For immunoprecipitation assay for HMGB1 and gp91 ^phox studies, cell lysates in RIPA buffer were prepared from control and neutrophils incubated with 6xHis-HMGB1 (oxidized form) recombinant protein for 20 minutes. Immunoprecipitation was conducted using anti-gp91 ^phox IgG (5 μg/ml) for 16 hours, at 4°C. Next, protein-A/G agarose was included for an additional 2 hours, at 4°C. Agarose was washed with PBS and proteins released after incubation with 2x loading buffer for 10 minutes, at 95°C. The amount of HMGB1 associated with gp91 ^phox was then determined using Western Blot analysis with antibodies against 6xHis-tag or HMGB1. Gp91 decoy peptides were designed to NOX2 transmembrane subunit gp91 ^phox and synthetized by Sigma-Aldrich (St. Louis, MO). In selected experiments, peptides (0 or 2.5 μg/ml) were incubated with plasma (500 μg/ml) for 30 minutes. Next, neutrophils were incubated with plasma for additional 15 minutes, followed by cytochrome c reduction assay. Flow cytometry was conducted as follows: neutrophils (3 x 10 ⁶ ) were incubated with oxidized or reduced HMGB1-FL (1 μg/ml) in PBS for the indicated time (see figure descriptions), at room temperature. Forward and side-scatter gating followed by detection of HMGB1 binding; at least 10,000 events were collected using the BD LSR II Flow Cytometer (Becton/Dickinson, NJ, USA). Data analysis was conducted with FlowJo analytical software, version 10 (Tree Star). For neutrophil-dependent bacterial killing studies, neutrophils (2.5 × 10 ⁵ ) in serum free media (RPMI-1640) were pre-incubated with HD or T/H plasma (500 μg/ml) for 30 min at 37 ^◦ C (5% CO ₂ ). Bacterial killing was initiated by inclusion of ampicillin-resistant E. coli (DH5α; ampicillin resistant; 5 × 10 ⁵ ) with 2:1 bacteria/neutrophil ratio (500 μl total volume), and samples were incubated for an additional 90 min, similar to a previously described method (see D.W. Park et al., Mol. Med. 19, 387–398, 2013). Next, 20 μl of cell/bacterial suspension was incubated with 480 μl Triton X-100 (0.1%) for 10 min to lyse neutrophils. Serial dilutions in PBS were plated on Luria-Bertani agar with ampicillin and incubated overnight at 37 ^◦ C. CFUs were counted the following day. In selected experiments, T/H plasma (500 μg/ml) was pre-treated with AI peptides (0 or 2.5 μg each/ml) for 30 min prior to inclusion of neutrophils. For statistical analysis, multigroup comparisons were performed using one-way ANOVA with Tukey’s post hoc test. Values were normally distributed. Statistical significance was determined by the Student’s t-test for comparisons between two groups. A value of p < 0.05 was considered significant. Analyses were performed on SPSS version 16.0, IBM (Armonk, NY) for Windows, Microsoft Corp. (Redmond, WA). Example 1- HMGB1 in lungs of post-septic mice decreased immune capacity to eradicate P. aeruginosa-induced pneumonia A potential contribution of Damage Associated Molecular Patterns (DAMPs) proteins to sepsis-induced immunosuppression was determined in a mouse model of polymicrobial intra-abdominal infection (FIG.1A). The immunosuppressive phenotype was evidenced by a significant decrease of P. aeruginosa strain K (PAK) killing in lungs of mice seven days after CLP (see “Sepsis” mice, FIG.1B). While reduced bacteria killing resulted from chronic infection and injury inflicted by CLP, immunosuppression has not developed after acute peritonitis induced, i.e. intraperitoneal injection of cecal slurry (CS). Sepsis- immunosuppressed mice were found to have significant amounts of HMGB1 accumulation in bronchoalveolar lavages (BALs) (FIGS.1C and 1D). To test if High Mobility Group Box 1 (HMGB1) affects the onset of immunosuppression, unaltered mice were subjected intratracheal injection of HMGB1 or vehicle (PBS) followed by exposure to lethal amounts of PAK (2 x 10 ⁷ /mouse i.t.). Intratracheal injection of HMGB1 reduced the ability of the host to kill PAK, as indicated by increased CFUs from lung homogenates (FIGS. 1E and 1F). Additional, ex vivo results confirmed that, direct incubation of neutrophils with HMGB1 (disulfide) decreased the rate of nicotin-amide adenine dinucleotide phosphate oxidase (NADPH) oxidase (NOX) 2 activity after stimulation with PMA (FIG.1G). These results suggest that DAMPs, in particular HMGB1 accumulation in lungs of post-sepsis mice is linked to development of the immunosuppressive phenotype. Example 2 - Apoptosis promotes DAMPs-dependent release and inhibition of neutrophil respiratory burst Severe infections and trauma are characterized by release of DAMPs from injured and dying cells, conditions frequently associated with development of ALI (see N. Robinson et al., Redox biology 26, 101239, 2019). Confocal microscopy indicates that apoptosis, induced by Tunicamycin-related endoplasmic reticulum (ER) stress in AECs or in Antimycin A (mitochondrial ETC complex III inhibitor) treated macrophage, led to HMGB1 translocation from the nucleus to the cytosol (FIGS.2A and 2B). This translocation is follow by HMGB1 release into the culture media (FIGS. 2A and 2B). Next, potential impact of dying cells on neutrophil NOX2 activation was tested (FIG. 2C). Incubation of neutrophils with lysates from dying, but not viable cells, effectively decreased NOX2 activation by PMA (FIGS.2D and 2F). Of note, a partial protection of NOX2 activation was found after pre-incubation of apoptotic lysates with HMGB1 neutralizing antibodies, compared to control IgG (FIGS.2E and 2F). These results indicate that apoptosis of alveolar epithelial or immune cells, both relevant issues in severe infection and trauma (see M. M. Khan et al., Shock 44, 294-304, 2015), can release DAMPs and adversely affect neutrophil respiratory burst. Example 3 - Oxidized HMGB1 inhibits neutrophil respiratory burst Intrinsic apoptosis or ER stress is associated with generation of mitochondrial ROS (see M. J. Parsons and D. R. Green, Essays in Biochemistry 47, 99-114, 2010). HMGB1 redox status can be affected by three cysteine thiols that are available for oxidative modifications in completely reduced HMGB1 (FIG. 3A). Oxidation of HMGB1 preferentially forms a disulfide bond between Cys23 and Cys45 within BOXA domain. The remaining Cysteine (Cys ₁₀₆ ) undergoes oxidation in BOXB domain; this oxidation has been shown to diminished HMGB1 retention in the nucleus (see G. Hoppe et al., Exp. Cell Res. 312, 3526-3538, 2006). In apoptotic cells, ROS induces protein s-glutathionylation, as indicated by Western blot analysis of Bio-GSS-protein adduct formations in apoptotic macrophages, and culture media (FIG. 3B). Further analysis showed that apoptotic macrophages generate and release s-glutathionylated HMGB1 (FIG. 3C). HMGB1 recombinant (disulfide) can be also s-glutathionylated in vitro (FIG.3D). It has been previously shown that HMGB1 decreased neutrophil NOX2 activation ex vivo (see J. M. Tadie et al., Am. J. Physiol. Cell Physiol.302, C249-256, 2012), however, it is not known if NOX2 inhibition depends on HMGB1 oxidative status. First, it was confirmed that disulfide, but not reduced or oxidized, HMGB1 stimulated (although modestly) TNF-α production (FIG.3E). Next, it was found that oxidized, but not reduced, HMGB1 effectively diminished PMA-induced neutrophil respiratory burst (FIGS. 3F and 3G). These findings suggest that release of oxidized proteins, including HMGB1, induce the neutrophil immunosuppression-like phenotype through NOX2 inactivation. Example 4 - HMGB1 binds to gp91 ^phox subunit of NOX2 Given the ability of HMGB1 to decrease neutrophil respiratory burst, a possible interaction between GSS-HMGB1 and gp91 ^phox was tested. In this experiment, neutrophils were incubated with oxidized 6xHis-HMGB1 recombinant protein followed by co- immunoprecipitation with anti-gp91 ^phox IgG. Western blot analysis indicates that recombinant HMGB1 is associated with gp91 ^phox (FIG.4A). Similar results were obtained after pull down of gp91 ^phox and Western blot analysis for endogenous HMGB1 (FIG.4B). HMGB1 and gp91 ^phox interaction was also determined on the surface membrane of viable neutrophils. Fluorescent HMGB1 (GSS-HMGB1-FL) and florescent-conjugated gp91 ^phox antibody were generated, as described in the Materials and Methods above, and confirmed using non-reducing PAGE and Western blot analysis (FIG. 4C). It was established that oxidized HMGB1-FL is rapidly binding to the neutrophil surface membrane; flow cytometry analysis shows time dependent binding HMGB1-FL (FIG. 4D). Representative images revealed a substantial overlap in fluorescence patterns between HMGB1 and gp91 ^phox , i.e. co-localization is evidenced by appearance of yellow fluorescence (FIG.4E). Of note, patterns of HMGB1 fluorescence show gp91-independent binding sites; this is consistent with the ability of HMGB1 to bind other receptors. Given the results of co- immunoprecipitation and imaging, oxidized HMGB1 appears to interact with the NOX2 gp91 ^phox subunit. Example 5 - Gp91 ^phox decoys prevent NOX2 inactivation by plasma of trauma- immunosuppressed patients Next, examination was undertaken to determine if gp91 ^phox decoy strategy prevents inhibitory effects of plasma that was obtained from individuals that survived shock/trauma, but developed secondary lung infections. Plasmas from immunosuppressed patients have significant inhibitory effects on PMA-dependent activation of neutrophil respiratory burst, as compared to healthy controls (FIG.5A). It was found that pre-incubation with gp91 ^phox decoy decreased plasma inhibitory effects on neutrophil NOX2 inactivation (FIG. 5B). These findings suggest that gp91 ^phox decoy strategy is a suitable approach to antagonize mediators of neutrophil immunosuppression (FIG.5C). Example 6 - Gp91 ^phox decoy peptides disrupt inhibitory action of trauma/hemorrhage (T/H) plasma on neutrophil respiratory burst Three external loops of gp91 ^phox were used to design NOX2 decoy anti- immunosuppression (Ai)-Peptides (FIGS.6A and 6B). These peptides have relatively high amino acid homology between human and mice. AI peptides were evaluated against T/H plasma inhibitory action on the neutrophil respiratory burst (FIG. 6C). Pre-incubation of T/H plasma with AI peptide 1, 3 or simultaneous inclusion of AI peptides 1–3 was found to effectively preserve neutrophil respiratory burst as compared to neutrophils that were treated with T/H plasma alone (FIG.6D). In this setting, Peptide 2 had substantially no effect. While use of peptide 1 or 3 alone were partially protected against T/H plasma, combined peptides showed a synergistic impact. The ability of AI peptides 1 and 3 to prevent T/H plasma inhibitory action was consistent with improved bacterial killing by neutrophils ex vivo. Notably, while T/H plasma decreased neutrophil capacity to eradicate E. coli, this effect was diminished after incubation of plasma with AI peptide 1, 3 or combined AI peptides (FIG. 6E). Mechanistic studies revealed that HMGB1 is directly binding to AI peptide 3, but not AI peptide 1, as evidenced by an ELISA assay that utilized biotinylated AI peptides (FIG.6F). This finding suggests that HMGB1 directly interacts with the third external loop of gp-91 ^phox subunit. These results indicate that NOX2 inhibition is partially dependent on HMGB1, as AI peptide 1 or 3 alone provided incomplete protection against T/H plasma, and HMGB1 is exclusively binding to AI peptide 3. This finding suggests that other molecules can be involved in inhibition of NOX2 by T/H plasma. Finally, AI peptides were tested to determine if they are able to improve mice viability in a murine model of intraperitoneal infections, i.e. E. coli -induced lethal peritonitis. Injection of E. coli (2 × 10 ⁸ /mouse; i.p.) resulted in rapid accumulation of HMGB1 in the peritoneal cavity, and all mice died within 48 h (FIGS. 6G and 6H). Importantly, delayed administration of AI peptides, i.e.2 h after E. coli injection, resulted in improved survival. Collectively, these findings suggest that AI peptides have therapeutic potential to improve survival from infections, likely via disruption of the neutrophil immunosuppressive phenotype induced by HMGB1.