PATENT Ref. No. KSURF 40481WO/27214.00056 SAFE, DIVA-COMPATIBLE, SUBUNIT VACCINE FOR AFRICAN SWINE FEVER VIRUS SEQUENCE LISTING [0001] The contents of the electronic sequence listing (40481WO_sequence_listing.xml; Size: 35,000 bytes; and Date of Creation: September 29, 2022) is herein incorporated by reference in its entirety. BACKGROUND OF THE DISCLOSURE [0002] African swine fever (“ASF”) is a highly contagious and deadly viral disease affecting both domestic and feral swine of all ages. ASF is currently not a threat to human health and cannot be transmitted from pigs to humans. The ASF virus (“ASFV”) genome is a large, (175–215 nm), icosahedral, double-stranded DNA virus with a linear genome of 189 kilobases containing more than 180 genes in the Asfarviridae family and is the causative agent of ASF. The number of genes differs slightly among different isolates of the virus. ASFV has similarities to the other large DNA viruses, e.g., poxvirus, iridovirus, and mimivirus. In common with other viral hemorrhagic fevers, the main target cells for replication are those of monocyte, macrophage lineage. Entry of the virus into the host cell is receptor-mediated, but the precise mechanism of endocytosis is presently unclear. The virus causes a hemorrhagic fever with high mortality rates in domestic pigs as well as warthogs, bushpigs, and soft ticks. It persistently infects its natural hosts, which likely act as a vector, with no disease signs. ASFV is endemic to sub-Saharan Africa and exists in the wild through a cycle of infection between ticks and wild pigs, bushpigs, and warthogs. The disease was first described after European settlers brought pigs into areas endemic with ASFV, and as such, is an example of an emerging infectious disease. [0003] ASFV replicates in the cytoplasm of infected cells. It is the only virus with a double- stranded DNA genome known to be transmitted by arthropods. The virus encodes enzymes required for replication and transcription of its genome, including elements of a base excision repair system, structural proteins, and many proteins that are not essential for replication in cells, but instead have roles in virus survival and transmission in its hosts. Virus replication takes place PATENT Ref. No. KSURF 40481WO/27214.00056 in perinuclear factory areas. It is a highly orchestrated process with at least four stages of transcription—immediate-early, early, intermediate, and late. The majority of replication and assembly occurs in discrete, perinuclear regions of the cell called virus factories, and finally progeny virions are transported to the plasma membrane along microtubules where they bud out or are propelled away along actin projections to infect new cells. As the virus progresses through its lifecycle, most, if not all of the host cell's organelles are modified, adapted, or in some cases destroyed. Assembly of the icosahedral capsid occurs on modified membranes from the endoplasmic reticulum. Products from proteolytically processed polyproteins form the core shell between the internal membrane and the nucleoprotein core. An additional outer membrane is gained as particles bud from the plasma membrane. The virus encodes proteins that inhibit signalling pathways in infected macrophages and thus modulate transcriptional activation of immune response genes. In addition, the virus encodes proteins which inhibit apoptosis of infected cells to facilitate production of progeny virions. Viral membrane proteins with similarity to cellular adhesion proteins modulate interaction of virus-infected cells and extracellular virions with host components. [0004] ASF is spread by contact with infected animals’ body fluids. It can be spread in a variety of ways including through ticks that feed on infected animals, humans as they can move the virus on vehicles or clothing, and by feeding pigs uncooked garbage that contains infected pork products. The signs of ASF include high fever, decreased appetite, weakness, red, blotchy skin or skin lesions, diarrhea, vomiting, coughing and difficulty breathing. Timeliness is essential to preventing the spread of ASF as some isolates can cause death of animals as quickly as a week after infection. There is no treatment or vaccine available for this disease. The only way to stop this deadly disease is to depopulate all affected or exposed swine herds. [0005] ASF is found in countries around the world. More recently, it has spread to the Dominican Republic and Haiti. ASF has also spread through China, Mongolia and Vietnam, as well as within parts of the European Union. It has never been found in the United States [0006] Consequently, there is an urgent need to develop safe and effective vaccines to protect against infection by ASFV. What is needed are compositions that are effective at reducing the incidence of, reducing the severity of, reducing the duration of, and/or reducing the transmissibility of ASFV. PATENT Ref. No. KSURF 40481WO/27214.00056 SUMMARY OF THE DISCLOSURE [0007] The present disclosure addresses the problems inherent in the art and provides immunogenic compositions or vaccines that reduce at least one of the incidence, severity, duration, and transmissibility of ASFV. BRIEF DESCRIPTION OF THE DRAWINGS [0008] The following drawings form part of the present specification and are included to further demonstrate certain aspects of the present disclosure. The disclosure may be better understood by reference to one or more of these drawings in combination with the detailed description of specific embodiments presented herein. [0009] FIGURE 1 is a set of photographs illustrating VSV expression of recombinant proteins E/CSFV, E183L-Ub, B646L-Ub, B646L, and CP204L-Ub; [0010] Fig. 2 is a graph comparing the survival curve of vaccinated animals versus unvaccinated animals after challenge with virulent ASFV; and [0011] Fig.3 is a representation of a map of rVSV-vectored vaccine for CSF and ASF. DETAILED DESCRIPTION [0012] The following detailed description and examples set forth preferred materials and procedures used in accordance with the present disclosure. It is to be understood, however, that this description and these examples are provided by way of illustration only, and nothing therein shall be deemed to be a limitation upon the overall scope of the present disclosure. [0013] The present disclosure provides immunogenic compositions and/or vaccines against ASFV that reduce at least one of the incidence of, severity of, duration of, and/or transmission of ASFV. In some forms, the immunogenic compositions comprise at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, or more ASFV proteins. In some forms, the ASFV proteins are from a circulating strain of ASFV. In some forms, the ASFV proteins are from the Georgia 2007 strain of ASFV. In some forms, the proteins are from a combination of more than one strain of ASFV. In some forms, at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25 or more proteins included in the composition is from a circulating strain or the Georgia 2007 strain of ASFV. In some forms, at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25 or more proteins included PATENT Ref. No. KSURF 40481WO/27214.00056 in the composition is from a strain of ASFV having at least 90, 91, 92, 93, 94, 95, 96, 97, 98, 99, 99.1, 99.2, 99.3, 99.4, 99.5, 99.6, 99.7, 99.8, 99.9, or even 100% sequence identity or sequence homology with the Georgia 2007 strain of ASFV. In some forms, at least 1, 2, 3, 4, 5, 6, 7, 8, 9, or 10 proteins included in the composition is/are selected from the group consisting of B646-Ub, CP204L-Ub, E183L-Ub, B602L, CP530R, E199L, E153R, EP402R, I73R, EP364R, and any combination thereof. In some forms, the protein is encoded by a nucleotide sequence having at least 75, 80, 85, 86, 87, 88, 89, 90, 91, 92, 93, 94, 95, 96, 97, 98, 99, 99.1, 99.2, 99.3, 99.4, 99.5, 99.6, 99.7, 99.8, 99.9, or even 100% sequence identity or sequence homology with a sequence selected from the group consisting of SEQ ID Nos 2-11. [0014] In some forms, the present disclosure provides a plasmid that comprises at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, or more ASFV nucleotide sequences that encodes at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, or more ASFV proteins. In some forms, the ASFV nucleotide sequences are from a circulating strain of ASFV. In some forms, the ASFV nucleotide sequences are from the Georgia 2007 strain of ASFV. In some forms, the nucleotide sequences are from a combination of more than one strain of ASFV. In some forms, at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25 or more nucleotide sequences included in the plasmid is from a circulating strain or the Georgia 2007 strain of ASFV. In some forms, at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25 or more nucleotide sequences included in the plasmid is from a strain of ASFV having at least 90, 91, 92, 93, 94, 95, 96, 97, 98, 99, 99.1, 99.2, 99.3, 99.4, 99.5, 99.6, 99.7, 99.8, 99.9, or even 100% sequence identity or sequence homology with the Georgia 2007 strain of ASFV. In some forms, at least 1, 2, 3, 4, 5, 6, 7, 8, 9, or 10 nucleotide sequences included in the plasmid encode for a protein selected from the group consisting of B646-Ub, CP204L-Ub, E183L-Ub, B602L, CP530R, E199L, E153R, EP402R, I73R, EP364R, and any combination thereof. In some forms, the nucleotide sequence included in the plasmid has at least 75, 80, 85, 86, 87, 88, 89, 90, 91, 92, 93, 94, 95, 96, 97, 98, 99, 99.1, 99.2, 99.3, 99.4, 99.5, 99.6, 99.7, 99.8, 99.9, or even 100% sequence identity or sequence homology with a sequence selected from the group consisting of SEQ ID Nos 2-11. In some forms, the plasmid includes at least one fragment from classical swine fever virus (CSFV). In some forms, the fragment from CSFV encodes for an envelope protein. In some forms, the CSFV envelope protein is encoded by a nucleotide sequence having at least 75, 80, 85, 86, 87, 88, 89, 90, 91, 92, PATENT Ref. No. KSURF 40481WO/27214.00056 93, 94, 95, 96, 97, 98, 99, 99.1, 99.2, 99.3, 99.4, 99.5, 99.6, 99.7, 99.8, 99.9, or even 100% sequence identity or sequence homology with SEQ ID No.1. In some forms, the CSFV fragment replaces a glycoprotein in the plasmid. In some forms, the glycoprotein is replaced using restriction enzymes. In some forms, the restriction enzymes are selected from the group consisting of Mlul, Avrll, and any combination thereof. In some forms, the plasmid is a vesicular stomatitis virus (VSV) plasmid. In some forms, the VSV plasmid includes a nucleotide sequence having at least 75, 80, 85, 86, 87, 88, 89, 90, 91, 92, 93, 94, 95, 96, 97, 98, 99, 99.1, 99.2, 99.3, 99.4, 99.5, 99.6, 99.7, 99.8, 99.9, or even 100% sequence identity or sequence homology with SEQ ID No. 12. In some forms, the plasmid is organized as depicted in Fig. 3. In some forms, the desired proteins are expressed using the Orf poxvirus. [0015] The present disclosure further provides methods for reducing the incidence, severity, duration, transmissibility, or any combination thereof of infection with or by ASFV in an animal in need thereof. In some forms, the animal is selected from the group consisting of pigs and/or swine. In some forms, the swine include domestic pigs, feral pigs, warthogs, bushpigs, and any combination thereof. In some forms, the method includes the step of administering an immunogenic composition or vaccine that comprises at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, or more ASFV proteins. In some forms, the ASFV proteins are from a circulating strain of ASFV. In some forms, the ASFV proteins are from the Georgia 2007 strain of ASFV. In some forms, the proteins are from a combination of more than one strain of ASFV. In some forms, at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25 or more proteins included in the composition is from a circulating strain or the Georgia 2007 strain of ASFV. In some forms, at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25 or more proteins included in the composition is from a strain of ASFV having at least 90, 91, 92, 93, 94, 95, 96, 97, 98, 99, 99.1, 99.2, 99.3, 99.4, 99.5, 99.6, 99.7, 99.8, 99.9, or even 100% sequence identity or sequence homology with the Georgia 2007 strain of ASFV. In some forms, at least 1, 2, 3, 4, 5, 6, 7, 8, 9, or 10 proteins included in the immunogenic composition is/are selected from the group consisting of B646-Ub, CP204L-Ub, E183L-Ub, B602L, CP530R, E199L, E153R, EP402R, I73R, EP364R, and any combination thereof. In some forms, the protein is encoded by a nucleotide sequence having at least 75, 80, 85, 86, 87, 88, 89, 90, 91, 92, 93, 94, 95, 96, 97, 98, 99, 99.1, 99.2, 99.3, 99.4, 99.5, 99.6, 99.7, 99.8, 99.9, or even 100% sequence identity or sequence homology with a sequence PATENT Ref. No. KSURF 40481WO/27214.00056 selected from the group consisting of SEQ ID Nos 2-11. In some forms, the immunogenic composition or vaccine is administered 1, 2, 3, 4, 5, or more times. In some forms, successive administrations of the immunogenic composition are at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, or more days apart. In some forms, the incidence of ASFV infection is reduced by 10, 20, 30, 40, 50, 60, 70, 80, 90, 95, or even 100% in an animal or group of animals receiving an administration of the immunogenic composition or vaccine in comparison to an animal or group of animals that has not received at least one administration of the immunogenic composition or vaccine. In some forms, the severity of ASFV infection is reduced by 10, 20, 30, 40, 50, 60, 70, 80, 90, 95, or even 100% in an animal or group of animals receiving an administration of the immunogenic composition or vaccine in comparison to an animal or group of animals that has not received at least one administration of the immunogenic composition or vaccine. In some forms, severity is determined by the number of signs of ASFV infection exhibited by an animal or group of animals. In some forms, the signs of ASFV infection are selected from the group consisting of high fever, decreased appetite, weakness, red, blotchy skin or skin lesions, diarrhea, vomiting, coughing, difficulty breathing, death and any combination thereof. In some forms, severity is determined is determined by a comparison of at least one of the signs of ASFV infection using a scale that compares the extent of at least one of the signs of ASFV infection with a standard of severity for that sign. For example, if an animal exhibited a normal temperature, the scale would indicate that temperatures farther from the normal temperature were more severe than temperatures closer to the normal temperature. In some forms, the duration of infection by ASFV is reduced by 10, 20, 30, 40, 50, 60, 70, 80, 90, 95, or even 100% in an animal or group of animals receiving an administration of the immunogenic composition or vaccine in comparison to an animal or group of animals that has not received at least one administration of the immunogenic composition or vaccine. In some forms, the transmissibility of ASFV is reduced by 10, 20, 30, 40, 50, 60, 70, 80, 90, 95, or even 100% in an animal or group of animals receiving an administration of the immunogenic composition or vaccine in comparison to an animal or group of animals that has not received at least one administration of the immunogenic composition or vaccine. [0016] In some forms, the method present disclosure provides a plasmid that comprises at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, or more ASFV nucleotide sequences that encodes at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, PATENT Ref. No. KSURF 40481WO/27214.00056 17, 18, 19, 20, 21, 22, 23, 24, 25, or more ASFV proteins. In some forms, the ASFV nucleotide sequences are from a circulating strain of ASFV. In some forms, the ASFV nucleotide sequences are from the Georgia 2007 strain of ASFV. In some forms, the nucleotide sequences are from a combination of more than one strain of ASFV. In some forms, at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25 or more nucleotide sequences included in the plasmid is from a circulating strain or the Georgia 2007 strain of ASFV. In some forms, at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25 or more nucleotide sequences included in the plasmid is from a strain of ASFV having at least 90, 91, 92, 93, 94, 95, 96, 97, 98, 99, 99.1, 99.2, 99.3, 99.4, 99.5, 99.6, 99.7, 99.8, 99.9, or even 100% sequence identity or sequence homology with the Georgia 2007 strain of ASFV. In some forms, at least 1, 2, 3, 4, 5, 6, 7, 8, 9, or 10 nucleotide sequences included in the plasmid encode for a protein selected from the group consisting of B646-Ub, CP204L-Ub, E183L-Ub, B602L, CP530R, E199L, E153R, EP402R, I73R, EP364R, and any combination thereof. In some forms, the nucleotide sequence included in the plasmid has at least 75, 80, 85, 86, 87, 88, 89, 90, 91, 92, 93, 94, 95, 96, 97, 98, 99, 99.1, 99.2, 99.3, 99.4, 99.5, 99.6, 99.7, 99.8, 99.9, or even 100% sequence identity or sequence homology with a sequence selected from the group consisting of SEQ ID Nos 2-11. In some forms, the plasmid includes at least one fragment from classical swine fever virus (CSFV). In some forms, the fragment from CSFV encodes for an envelope protein. In some forms, the CSFV envelope protein is encoded by a nucleotide sequence having at least 75, 80, 85, 86, 87, 88, 89, 90, 91, 92, 93, 94, 95, 96, 97, 98, 99, 99.1, 99.2, 99.3, 99.4, 99.5, 99.6, 99.7, 99.8, 99.9, or even 100% sequence identity or sequence homology with SEQ ID No.1. In some forms, the CSFV fragment replaces a glycoprotein in the plasmid. In some forms, the glycoprotein is replaced using restriction enzymes. In some forms, the restriction enzymes are selected from the group consisting of Mlul, Avrll, and any combination thereof. In some forms, the plasmid is a vesicular stomatitis virus (VSV) plasmid. In some forms, the VSV plasmid includes a nucleotide sequence having at least 75, 80, 85, 86, 87, 88, 89, 90, 91, 92, 93, 94, 95, 96, 97, 98, 99, 99.1, 99.2, 99.3, 99.4, 99.5, 99.6, 99.7, 99.8, 99.9, or even 100% sequence identity or sequence homology with SEQ ID No. 12. In some forms, the plasmid is organized as depicted in Fig. 3. In some forms, the desired proteins are expressed using the Orf poxvirus. [0017] The present disclosure further provides methods for reducing the incidence, severity, duration, transmissibility, or any combination thereof of infection with or by ASFV in an PATENT Ref. No. KSURF 40481WO/27214.00056 animal in need thereof. In some forms, the animal is selected from the group consisting of pigs and/or swine. In some forms, the swine include domestic pigs, feral pigs, warthogs, bushpigs, and any combination thereof. In some forms, the method includes the step of administering an immunogenic composition or vaccine that comprises a plasmid having at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, or more nucleotide sequences that encode ASFV proteins. In some forms, the ASFV nucleotide sequences are from a circulating strain of ASFV. In some forms, the ASFV nucleotide sequences are from the Georgia 2007 strain of ASFV. In some forms, the nucleotide sequences are from a combination of more than one strain of ASFV. In some forms, at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25 or more nucleotide sequences included in the composition is from a circulating strain or the Georgia 2007 strain of ASFV. In some forms, at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25 or more nucleotide sequences included in the plasmid is/are from a strain of ASFV having at least 90, 91, 92, 93, 94, 95, 96, 97, 98, 99, 99.1, 99.2, 99.3, 99.4, 99.5, 99.6, 99.7, 99.8, 99.9, or even 100% sequence identity or sequence homology with the Georgia 2007 strain of ASFV. In some forms, at least 1, 2, 3, 4, 5, 6, 7, 8, 9, or 10 nucleotide sequences included in the immunogenic composition encode for a protein that is/are selected from the group consisting of B646-Ub, CP204L-Ub, E183L-Ub, B602L, CP530R, E199L, E153R, EP402R, I73R, EP364R, and any combination thereof. In some forms, the plasmid includes at least one nucleotide sequence having at least 75, 80, 85, 86, 87, 88, 89, 90, 91, 92, 93, 94, 95, 96, 97, 98, 99, 99.1, 99.2, 99.3, 99.4, 99.5, 99.6, 99.7, 99.8, 99.9, or even 100% sequence identity or sequence homology with a sequence selected from the group consisting of SEQ ID Nos 2-11. In some forms, the immunogenic composition or vaccine is administered 1, 2, 3, 4, 5, or more times. In some forms, successive administrations of the immunogenic composition are at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, or more days apart. In some forms, the incidence of ASFV infection is reduced by 10, 20, 30, 40, 50, 60, 70, 80, 90, 95, or even 100% in an animal or group of animals receiving an administration of the immunogenic composition or vaccine in comparison to an animal or group of animals that has not received at least one administration of the immunogenic composition or vaccine. In some forms, the severity of ASFV infection is reduced by 10, 20, 30, 40, 50, 60, 70, 80, 90, 95, or even 100% in an animal or group of animals receiving an administration of the immunogenic composition or vaccine in comparison to an animal or group of animals that has not received at PATENT Ref. No. KSURF 40481WO/27214.00056 least one administration of the immunogenic composition or vaccine. In some forms, severity is determined by the number of signs of ASFV infection exhibited by an animal or group of animals. In some forms, the signs of ASFV infection are selected from the group consisting of high fever, decreased appetite, weakness, red, blotchy skin or skin lesions, diarrhea, vomiting, coughing, difficulty breathing, death and any combination thereof. In some forms, severity is determined is determined by a comparison of at least one of the signs of ASFV infection using a scale that compares the extent of at least one of the signs of ASFV infection with a standard of severity for that sign. For example, if an animal exhibited a normal temperature, the scale would indicate that temperatures farther from the normal temperature were more severe than temperatures closer to the normal temperature. In some forms, the duration of infection by ASFV is reduced by 10, 20, 30, 40, 50, 60, 70, 80, 90, 95, or even 100% in an animal or group of animals receiving an administration of the immunogenic composition or vaccine in comparison to an animal or group of animals that has not received at least one administration of the immunogenic composition or vaccine. In some forms, the transmissibility of ASFV is reduced by 10, 20, 30, 40, 50, 60, 70, 80, 90, 95, or even 100% in an animal or group of animals receiving an administration of the immunogenic composition or vaccine in comparison to an animal or group of animals that has not received at least one administration of the immunogenic composition or vaccine. [0018] “Sequence Identity” as it is known in the art refers to a relationship between two or more polypeptide sequences or two or more polynucleotide sequences, namely a reference sequence and a given sequence to be compared with the reference sequence. Sequence identity is determined by comparing the given sequence to the reference sequence after the sequences have been optimally aligned to produce the highest degree of sequence similarity, as determined by the match between strings of such sequences. Upon such alignment, sequence identity is ascertained on a position-by-position basis, e.g., the sequences are “identical” at a particular position if at that position, the nucleotides or amino acid residues are identical. The total number of such position identities is then divided by the total number of nucleotides or residues in the reference sequence to give % sequence identity. Sequence identity can be readily calculated by known methods, including but not limited to, those described in Computational Molecular Biology, Lesk, A. N., ed., Oxford University Press, New York (1988), Biocomputing: Informatics and Genome Projects, Smith, D.W., ed., Academic Press, New York (1993); Computer Analysis of Sequence Data, Part I, Griffin, A.M., and Griffin, H. G., eds., Humana Press, New Jersey (1994); Sequence Analysis PATENT Ref. No. KSURF 40481WO/27214.00056 in Molecular Biology, von Heinge, G., Academic Press (1987); Sequence Analysis Primer, Gribskov, M. and Devereux, J., eds., M. Stockton Press, New York (1991); and Carillo, H., and Lipman, D., SIAM J. Applied Math., 48: 1073 (1988), the teachings of which are incorporated herein by reference. Preferred methods to determine the sequence identity are designed to give the largest match between the sequences tested. Methods to determine sequence identity are codified in publicly available computer programs which determine sequence identity between given sequences. Examples of such programs include, but are not limited to, the GCG program package (Devereux, J., et al., Nucleic Acids Research, 12(1):387 (1984)), BLASTP, BLASTN and FASTA (Altschul, S. F. et al., J. Molec. Biol., 215:403-410 (1990). The BLASTX program is publicly available from NCBI and other sources (BLAST Manual, Altschul, S. et al., NCVI NLM NIH Bethesda, MD 20894, Altschul, S. F. et al., J. Molec. Biol., 215:403-410 (1990), the teachings of which are incorporated herein by reference). These programs optimally align sequences using default gap weights in order to produce the highest level of sequence identity between the given and reference sequences. As an illustration, by a polynucleotide having a nucleotide sequence having at least, for example, 85%, preferably 90%, even more preferably 95% “sequence identity” to a reference nucleotide sequence, it is intended that the nucleotide sequence of the given polynucleotide is identical to the reference sequence except that the given polynucleotide sequence may include up to 15, preferably up to 10, even more preferably up to 5 point mutations per each 100 nucleotides of the reference nucleotide sequence. In other words, in a polynucleotide having a nucleotide sequence having at least 85%, preferably 90%, even more preferably 95% identity relative to the reference nucleotide sequence, up to 15%, preferably 10%, even more preferably 5% of the nucleotides in the reference sequence may be deleted or substituted with another nucleotide, or a number of nucleotides up to 15%, preferably 10%, even more preferably 5% of the total nucleotides in the reference sequence may be inserted into the reference sequence. These mutations of the reference sequence may occur at the 5’ or 3’ terminal positions of the reference nucleotide sequence or anywhere between those terminal positions, interspersed either individually among nucleotides in the reference sequence or in one or more contiguous groups within the reference sequence. Analogously, by a polypeptide having a given amino acid sequence having at least, for example, 85%, preferably 90%, even more preferably 95% sequence identity to a reference amino acid sequence, it is intended that the given amino acid sequence of the polypeptide is identical to the reference sequence except that the given polypeptide sequence may PATENT Ref. No. KSURF 40481WO/27214.00056 include up to 15, preferably up to 10, even more preferably up to 5 amino acid alterations per each 100 amino acids of the reference amino acid sequence. In other words, to obtain a given polypeptide sequence having at least 85%, preferably 90%, even more preferably 95% sequence identity with a reference amino acid sequence, up to 15%, preferably up to 10%, even more preferably up to 5% of the amino acid residues in the reference sequence may be deleted or substituted with another amino acid, or a number of amino acids up to 15%, preferably up to 10%, even more preferably up to 5% of the total number of amino acid residues in the reference sequence may be inserted into the reference sequence. These alterations of the reference sequence may occur at the amino or the carboxy terminal positions of the reference amino acid sequence or anywhere between those terminal positions, interspersed either individually among residues in the reference sequence or in the one or more contiguous groups within the reference sequence. Preferably, residue positions which are not identical differ by conservative amino acid substitutions. However, conservative substitutions are not included as a match when determining sequence identity. [0019] “Sequence homology”, as used herein, refers to a method of determining the relatedness of two sequences. To determine sequence homology, two or more sequences are optimally aligned, and gaps are introduced if necessary. However, in contrast to “sequence identity”, conservative amino acid substitutions are counted as a match when determining sequence homology. In other words, to obtain a polypeptide or polynucleotide having 95% sequence homology with a reference sequence, 85%, preferably 90%, even more preferably 95% of the amino acid residues or nucleotides in the reference sequence must match or comprise a conservative substitution with another amino acid or nucleotide, or a number of amino acids or nucleotides up to 15%, preferably up to 10%, even more preferably up to 5% of the total amino acid residues or nucleotides, not including conservative substitutions, in the reference sequence may be inserted into the reference sequence. Preferably the homologous sequence comprises at least a stretch of 50, even more preferably 100, even more preferably 250, even more preferably 500 nucleotides. [0020] A “conservative substitution” refers to the substitution of an amino acid residue or nucleotide with another amino acid residue or nucleotide having similar characteristics or PATENT Ref. No. KSURF 40481WO/27214.00056 properties including size, hydrophobicity, etc., such that the overall functionality does not change significantly. [0021] It will be found that the immunogenic compositions comprising any of the disclosed vaccine candidates as provided herewith are very effective in reducing the severity of or incidence of clinical signs associated with ASFV up to and including the prevention of such signs. Further, such immunogenic compositions reduce the transmissibility of ASFV. Advantageously, immunogenic compositions of this disclosure are also effective as treatments after an animal has been exposed to or contracted ASFV. [0022] The immunogenic compositions described herein can further include one or more other immunomodulatory agents such as, e. g., interleukins, interferons, or other cytokines. The immunogenic compositions can also include Gentamicin and Merthiolate. In another preferred embodiment, the present disclosure contemplates vaccine compositions comprising from about 1ug/ml to about 60 µg/ml of antibiotics, and more preferably less than about 30 µg/ml of antibiotics. [0023] The terms “immunogenic protein”, “immunogenic polypeptide” or “immunogenic amino acid sequence” as used herein refer to any amino acid sequence which elicits an immune response in a host against a pathogen comprising said immunogenic protein, immunogenic polypeptide or immunogenic amino acid sequence. An “immunogenic protein”, “immunogenic polypeptide” or “immunogenic amino acid sequence” as used herein, includes the full-length sequence of any proteins, analogs thereof, or immunogenic fragments thereof. By “immunogenic fragment” is meant a fragment of a protein which includes one or more epitopes and thus elicits the immunological response against the relevant pathogen. Such fragments can be identified using any number of epitope mapping techniques, well known in the art. See, e.g., Epitope Mapping Protocols in Methods in Molecular Biology, Vol.66 (Glenn E. Morris, Ed., 1996) Humana Press, Totowa, New Jersey. For example, linear epitopes may be determined by e.g., concurrently synthesizing large numbers of peptides on solid supports, the peptides corresponding to portions of the protein molecule, and reacting the peptides with antibodies while the peptides are still attached to the supports. Such techniques are known in the art and described in, e.g., U.S. Patent No. 4,708,871; Geysen et al. (1984) Proc. Natl. Acad. Sci. USA 81:3998-4002; Geysen et al. (1986) Molec. Immunol.23:709-715. Similarly, conformational epitopes are readily identified by PATENT Ref. No. KSURF 40481WO/27214.00056 determining spatial conformation of amino acids such as by, e.g., x-ray crystallography and 2- dimensional nuclear magnetic resonance. See, e.g., Epitope Mapping Protocols, supra. Synthetic antigens are also included within the definition, for example, polyepitopes, flanking epitopes, and other recombinant or synthetically derived antigens. See, e.g., Bergmann et al. (1993) Eur. J. Immunol. 23:2777-2781; Bergmann et al. (1996), J. Immunol. 157:3242-3249; Suhrbier, A. (1997), Immunol. and Cell Biol.75:402-408; Gardner et al., (1998) 12th World AIDS Conference, Geneva, Switzerland, June 28-July 3, 1998. [0024] In the present description, the terms polypeptide, peptide and protein are interchangeable. [0025] Additionally, any composition or vaccine candidate of the disclosure can include one or more pharmaceutical-acceptable or veterinary-acceptable carriers. As used herein, “a pharmaceutical-acceptable carrier” or “veterinary-acceptable carrier” includes any and all solvents, dispersion media, coatings, stabilizing agents, diluents, preservatives, antibacterial and antifungal agents, isotonic agents, adsorption delaying agents, and the like. In some forms, the pharmaceutical or veterinary acceptable carrier is selected from the group consisting of a solvent, a dispersion media, a coating, a stabilizing agent, a preservative, an antimicrobial agent, an antifungal agent, an isotonic agent, and an adsorption delaying agent, and any combination thereof. [0026] It is understood that the immunogenic compositions described herein can be administered to any animal susceptible to ASFV infection including all swine. [0027] An “immunogenic or immunological composition” refers to a composition of matter that comprises at least one antigen which elicits an immunological response in the host of a cellular and/ or antibody-mediated immune response to the composition or vaccine of interest. Usually, an “immunological response” includes but is not limited to one or more of the following effects: the production or activation of antibodies, B cells, helper T cells, suppressor T cells, and/or cytotoxic T cells and/or ^ ^ T cells, directed specifically to an antigen or antigens included in the composition or vaccine of interest. Preferably, the host will display either a therapeutic or protective immunological response such that resistance to new infection will be enhanced and/or the clinical severity of the disease reduced. Such protection will be demonstrated by either a reduction in the severity or prevalence of, up to and including a lack of symptoms normally displayed by an infected host, a quicker recovery time and/or a lowered viral titer in the infected host. PATENT Ref. No. KSURF 40481WO/27214.00056 [0028] “Adjuvants” as used herein, can include aluminum hydroxide and aluminum phosphate, saponins e.g., Quil A, QS-21 (Cambridge Biotech Inc., Cambridge MA), GPI-0100 (Galenica Pharmaceuticals, Inc., Birmingham, AL), water-in-oil emulsion, oil-in-water emulsion, water-in-oil-in-water emulsion. The emulsion can be based in particular on light liquid paraffin oil (European Pharmacopea type); isoprenoid oil such as squalane or squalene oil resulting from theoligomerization of alkenes, in particular of isobutene or decene; esters of acids or of alcohols containing a linear alkyl group, more particularly plant oils, ethyl oleate, propylene glycol di- (caprylate/caprate), glyceryl tri-(caprylate/caprate) or propylene glycol dioleate; esters of branched fatty acids or alcohols, in particular isostearic acid esters. The oil is used in combination with emulsifiers to form the emulsion. The emulsifiers are preferably nonionic surfactants, in particular esters of sorbitan, of mannide (e.g. anhydromannitol oleate), of glycol, of polyglycerol, of propylene glycol and of oleic, isostearic, ricinoleic or hydroxystearic acid, which are optionally ethoxylated, and polyoxypropylene-polyoxyethylene copolymer blocks, in particular the Pluronic products, especially L121. See Hunter et al., The Theory and Practical Application of Adjuvants (Ed.Stewart-Tull, D. E. S.). JohnWiley and Sons, NY, pp51-94 (1995) and Todd et al., Vaccine 15:564-570 (1997). [0029] For example, it is possible to use the SPT emulsion described on page 147 of “Vaccine Design, The Subunit and Adjuvant Approach” edited by M. Powell and M. Newman, Plenum Press, 1995, and the emulsion MF59 described on page 183 of this same book. [0030] A further instance of an adjuvant is a compound chosen from the polymers of acrylic or methacrylic acid and the copolymers of maleic anhydride and alkenyl derivative. Advantageous adjuvant compounds are the polymers of acrylic or methacrylic acid which are cross-linked, especially with polyalkenyl ethers of sugars or polyalcohols. These compounds are known by the term carbomer (Phameuropa Vol.8, No.2, June 1996). Persons skilled in the art can also refer to U. S. Patent No. 2,909,462 which describes such acrylic polymers cross-linked with a polyhydroxylated compound having at least 3 hydroxyl groups, preferably not more than 8, the hydrogen atoms of at least three hydroxyls being replaced by unsaturated aliphatic radicals having at least 2 carbon atoms. The preferred radicals are those containing from 2 to 4 carbon atoms, e.g. vinyls, allyls and other ethylenically unsaturated groups. The unsaturated radicals may themselves contain other substituents, such as methyl. The products sold under the name Carbopol; (BF PATENT Ref. No. KSURF 40481WO/27214.00056 Goodrich, Ohio, USA) are particularly appropriate. They are cross-linked with an allyl sucrose or with allyl pentaerythritol. Among then, there may be mentioned Carbopol 974P, 934P and 971P. Among the copolymers of maleic anhydride and alkenyl derivative, the copolymers EMA (Monsanto) which are copolymers of maleic anhydride and ethylene. The dissolution of these polymers in water leads to an acid solution that will be neutralized, preferably to physiological pH, in order to give the adjuvant solution into which the immunogenic, immunological or vaccine composition itself will be incorporated. [0031] Further suitable adjuvants include, but are not limited to, the RIBI adjuvant system (Ribi Inc.), Block co-polymer (CytRx, Atlanta GA), SAF-M (Chiron, Emeryville CA), monophosphoryl lipid A, Avridine lipid-amine adjuvant, heat-labile enterotoxin from E. coli (recombinant or otherwise), cholera toxin, IMS 1314 or muramyl dipeptide among many others. [0032] Preferably, the adjuvant is added in an amount of about 100 µg to about 10 mg per dose. Even more preferably, the adjuvant is added in an amount of about 100 µg to about 10 mg per dose. Even more preferably, the adjuvant is added in an amount of about 500 µg to about 5 mg per dose. Even more preferably, the adjuvant is added in an amount of about 750 µg to about 2.5 mg per dose. Most preferably, the adjuvant is added in an amount of about 1 mg per dose. [0033] In preferred forms the recombinant viral vector or plasmid containing ASFV DNA and expressing the desired proteins disclosed above, including SEQ ID NOS 2-11 is generated by transfecting a transfer vector that has had at least one ASFV gene cloned therein into a viral vector. In some preferred forms, only the portion of the transfer vector that contains the desired ASFV DNA is transfected into the viral vector. [0034] The term “transfected into a viral vector” means, and is used as a synonym for “introducing” or “cloning” a heterologous DNA into a viral vector, such as for example into a baculovirus vector. A “transfer vector” means a DNA molecule, that includes at least one origin of replication, the heterologous gene, in the present case of ASFV, DNA sequences which allow the cloning of said heterologous gene into the viral vector will be included. Preferably the sequences which allow cloning of the heterologous gene into the viral vector are flanking the heterologous gene. Even more preferably, those flanking sequences are at least homologous in parts with sequences of the viral vector. The sequence homology then allows recombination of PATENT Ref. No. KSURF 40481WO/27214.00056 both molecules, the viral vector, and the transfer vector to generate a recombinant viral vector containing the heterologous gene. [0035] In more preferred forms, the methods of the present disclosure will begin with the isolation of ASFV DNA and especially sequences that code for SEQ ID NOS 2-11. Any ASFV gene, such as variants of SEQ ID NOS.2-11, can be used for purposes of the present disclosure. In some forms, the ASFV DNA is preferably amplified using PCR methods. The resulting DNA is then cloned into the transfer vector. [0036] Thus, in one aspect of the present disclosure, a method for constructing a recombinant viral vector containing ASFV DNA is provided. This method generally comprises the steps of: 1) cloning at least one recombinant ASFV gene into a transfer vector; and 2) transfecting the portion of the transfer vector containing the recombinant ASFV gene into a viral vector, to generate the recombinant viral vector. [0037] In another aspect of the present disclosure, a method for preparing a composition, preferably an immunogenic composition, such as a vaccine, for invoking an immune response against ASFV is provided. Generally, this method includes the steps of transfecting a construct into a virus, wherein the construct comprises 1) recombinant DNA from a gene of ASFV, 2) infecting cells in growth media with the transfected virus, 3) causing the virus to express the recombinant ASFV protein, 4) recovering the expressed recombinant ASFV protein, 5) and preparing the composition by combining the recovered protein with a suitable adjuvant and/or other pharmaceutically acceptable carrier. In some preferred forms, the composition also includes at least a portion of the viral vector expressing said ASFV protein, and/or a portion of the cell culture supernate. In some forms, the ASFV protein is encoded by a DNA sequence disclosed herein. In some forms, the ASFV protein is encoded by a sequence selected from the group consisting of SEQ ID NOS.2-11. [0038] In another aspect of the present disclosure, a method for preparing an immunogenic composition, such as a vaccine, for invoking an immune response against ASFV comprises the steps of 1) expressing and recovering ASFV protein, and in preferred forms, 2) admixing the recovered protein with a suitable adjuvant. Preferably, the expressing step 1) includes steps for the preparation and recovery of ASFV protein. Another optional step for this method includes cloning the amplified ASFV DNA into a first vector, excising the ASFV DNA from this first vector, and PATENT Ref. No. KSURF 40481WO/27214.00056 using this excised ASFV DNA for cloning into the transfer vector. Preferably, the recovery step of this method also includes the step of separating the media from the cells and cell debris. This can be done in any conventional manner, with one preferred manner comprising filtering the cells, cell debris, and growth media through a filter having pores ranging in size from about 0.45 µM to about 1.0 µM. Finally, for this aspect, it is preferred to include a virus inactivation step prior to combining the recovered recombinant ASFV protein in a composition. When an inactivation step is included, it is also preferred to include a neutralization step, as described above. [0039] The methods of the present disclosure can also comprise the addition of any stabilizing agent, such as for example saccharides, trehalose, mannitol, saccharose and the like, to increase and/or maintain product shelf-life and/or to enhance stability. [0040] According to a further aspect, ASFV protein, such as one or more encoded by SEA ID NOS 2-11 is provided in the immunological composition at an antigen inclusion level effective for inducing the desired immune response, namely reducing the incidence of or lessening the severity of clinical signs resulting from ASFV infection, or reducing the transmissibility of ASFV. In some preferred forms, the ASFV protein inclusion level is at least 0.2 µg antigen/ml of the final immunogenic composition (µg/ml), more preferably from about 0.2 to about 2000 µg/ml. [0041] Those of skill in the art will understand that the composition herein may incorporate known injectable, physiologically acceptable, sterile solutions. For preparing a ready-to-use solution for parenteral injection or infusion, aqueous isotonic solutions, such as e.g. saline or corresponding plasma protein solutions are readily available. In addition, the immunogenic and vaccine compositions of the present disclosure can include diluents, isotonic agents, stabilizers, or adjuvants. Diluents can include water, saline, dextrose, ethanol, glycerol, and the like. Isotonic agents can include sodium chloride, dextrose, mannitol, sorbitol, and lactose, among others. Stabilizers include albumin and alkali salts of ethylendiamintetracetic acid, among others. Suitable adjuvants, are those described above. [0042] According to a further aspect, the immunogenic composition of the present disclosure further comprises a pharmaceutical acceptable salt, preferably a phosphate salt in physiologically acceptable concentrations. Preferably, the pH of said immunogenic composition is adjusted to a physiological pH, meaning between about 6.5 and 7.5. PATENT Ref. No. KSURF 40481WO/27214.00056 [0043] The immunogenic compositions described herein can further include one or more other immunomodulatory agents such as, e. g., interleukins, interferons, or other cytokines. The immunogenic compositions can also include Gentamicin and Merthiolate. In another preferred embodiment, the present disclosure contemplates vaccine compositions comprising from about 1ug/ml to about 60 µg/ml of antibiotics, and more preferably less than about 30 µg/ml of antibiotics. [0044] Another aspect of the present disclosure relates to a kit. Generally, the kit includes a container comprising at least one dose of the immunogenic composition of ASFV protein as provided herewith, wherein one dose comprises at least 2 µg ASFV protein. Said container can comprise from 1 to 250 doses of the immunogenic composition. In some preferred forms, the container contains 1, 10, 25, 50, 100, 150, 200, or 250 doses of the immunogenic composition of ASFV protein. Preferably, each of the containers comprising more than one dose of the immunogenic composition of ASFV protein further comprises an anti-microbiological active agent. Those agents are for example, antibiotics including Gentamicin and Merthiolate and the like. Thus, one aspect of the present disclosure relates to a container that comprises from 1 to 250 doses of the immunogenic composition of ASFV protein, wherein one dose comprises at least 2 µg ASFV protein, and Gentamicin and/or Merthiolate, preferably from about 1 µg/ml to about 60 µg/ml of antibiotics, and more preferably less than about 30 µg/ml. In preferred forms, the kit also includes an instruction manual, including the information for the intramuscular application of at least one dose of the immunogenic composition of ASFV protein into animals, to lessen the incidence and/or severity of clinical symptoms associated with ASFV infection. Moreover, according to a further aspect, said instruction manual comprises the information of a second or further administration(s) of at least one dose of the immunogenic composition of ASFV protein, wherein the second administration or any further administration is at least 14 days beyond the initial or any former administration. In some preferred forms, said instruction manual also includes the information, to administer an immune stimulant. Preferably, said immune stimulant shall be given at least twice. Preferably, at least 3, more preferably at least 5, and even more preferably at least 7 days are between the first and the second or any further administration of the immune stimulant. Preferably, the immune stimulant is given at least 10 days, preferably 15, even more preferably 20, and still even more preferably at least 22 days beyond the initial administration of the immunogenic composition of ASFV protein. It is understood that any immune stimulant PATENT Ref. No. KSURF 40481WO/27214.00056 known to a person skilled in the art can also be used. “Immune stimulant” as used herein, means any agent or composition that can trigger a general immune response, preferably without initiating or increasing a specific immune response, for example the immune response against a specific pathogen. It is further instructed to administer the immune stimulant in a suitable dose. The kit may also comprise a second container, including at least one dose of the immune stimulant. [0045] A further aspect of the present disclosure relates to the kit as described above, comprising the immunogenic composition of ASFV protein as provided herewith and the instruction manual, wherein the instruction manual further includes the information to administer the ASFV immunogenic composition together, or around the same time as, with an immunogenic composition that comprises an additional antigen effective for reducing the severity of or incidence of clinical signs related to another mammalian pathogen. Preferably, the manual contains the information of when the ASFV protein containing composition and the immunogenic composition that comprises an additional antigen are administered. [0046] A further aspect, relates to the use of any of the compositions provided herewith as a medicament, preferably as a veterinary medicament, even more preferably as a vaccine. Moreover, the present disclosure also relates to the use of any of the compositions described herein, for the preparation of a medicament for lessening the severity of clinical symptoms associated with ASFV infection. Preferably, the medicament is for the prevention of a ASFV infection in an animal susceptible to infection with ASFV. [0047] A further aspect relates to a method for (1) the prevention of an infection, or re- infection with ASFV or (2) the reduction in incidence or severity of or elimination of clinical symptoms caused by ASFV in a subject, comprising administering any of the immunogenic compositions provided herewith to a subject in need thereof. It is understood that the reduction is in comparison to a subject that has not received an administration of a composition of the present disclosure. Preferably, the reduction is at least 10, 20, 30, 40, 50, 60, 70, 80, 90, 95, or even 100% in comparison to an animal that has not received an administration or dose of a composition described herein. It is understood that this percentage of reduction can be in terms of the number of symptoms, incidence of symptoms, or severity of symptoms. Further, this can apply to individual animals or groups of animals. Preferably, one dose or two doses of the immunogenic composition is/are administered, wherein one dose preferably comprises at least about 2 µg ASFV PATENT Ref. No. KSURF 40481WO/27214.00056 protein. A further aspect relates to the method of treatment as described above, wherein a second application of the immunogenic composition is administered. Preferably, the second administration is done with the same immunogenic composition, preferably having the same amount of ASFV protein. Preferably, the second administration is done at least 14 days beyond the initial administration, even more preferably at least 4 weeks beyond the initial administration. In preferred forms, the method is effective after just a single dose of the immunogenic composition and does not require a second or subsequent administration in order to confer the protective benefits upon the subject. [0048] According to a further aspect, the present disclosure provides a multivalent combination vaccine which includes an immunological agent effective for reducing the incidence of or lessening the severity of ASFV infection, and at least one immunological active component against another disease-causing organism in mammals. In some forms, the DNA encoding ASFV protein and the at least one immunological active component are integrated into, or transfected into a vector for administration thereof or for expressing the desired immunogenic components of ASFV and the at least one immunological active component. [0049] An “immunological active component” as used herein means a component that induces or stimulates the immune response in an animal to which said component is administered. According to a preferred embodiment, said immune response is directed to said component or to a microorganism comprising said component. According to a further preferred embodiment, the immunological active component is an attenuated microorganism, including modified live virus (MLV), a killed-microorganism or at least an immunological active part of a microorganism. [0050] “Immunological active part of a microorganism” as used herein means a protein-, sugar-, and or glycoprotein containing fraction of a microorganism that comprises at least one antigen that induces or stimulates the immune response in an animal to which said component is administered. According to a preferred embodiment, said immune response is directed to said immunological active part of a microorganism or to a microorganism comprising said immunological active part. [0051] Also included within the scope of the present disclosure are biologically functional plasmids, viral vectors and the like that contain the new recombinant nucleic acid molecules described herein, suitable host cells transfected by the vectors comprising the molecular DNA PATENT Ref. No. KSURF 40481WO/27214.00056 clones and the immunogenic polypeptide expression products. Some particularly preferred immunogenic proteins will be encoded by SEQ ID NOS. 2-11. The biologically active variants thereof are further encompassed by the disclosure. One of ordinary skill in the art would know how to modify, substitute, delete, etc., amino acid(s) from the polypeptide sequence and produce biologically active variants that retain the same, or substantially the same, activity as the parent sequence without undue effort. [0052] To produce the immunogenic polypeptide products of this disclosure, the process may include the following steps: growing, under suitable nutrient conditions, prokaryotic or eukaryotic host cells transfected with the new recombinant nucleic acid molecules described herein in a manner allowing expression of said polypeptide products, and isolating the desired polypeptide products of the expression of said nucleic acid molecules by standard methods known in the art. It is contemplated that the immunogenic proteins may be prepared by other techniques such as, for example, biochemical synthesis and the like. [0053] The polypeptides according to the disclosure can likewise be prepared by techniques which are conventional in the field of the synthesis of peptides. This synthesis can be carried out in homogeneous solution or in solid phase. For example, reference can be made to the technique of synthesis in homogeneous solution described by Houben-Weyl in 1974. This method of synthesis consists in successively condensing, two by two, the successive amino acids in the order required, or in condensing amino acids and fragments formed previously and already containing several amino acids in the appropriate order, or alternatively several fragments previously prepared in this way, it being understood that it will be necessary to protect beforehand all the reactive functions carried by these amino acids or fragments, with the exception of amine functions of one and carboxyls of the other or vice-versa, which must normally be involved in the formation of peptide bonds, especially after activation of the carboxyl function, according to the methods well known in the synthesis of peptides. According to another preferred technique of the disclosure, recourse will be made to the technique described by Merrifield. To make a peptide chain according to the Merrifield procedure, recourse is made to a very porous polymeric resin, on which is immobilized the first C-terminal amino acid of the chain. This amino acid is immobilized on a resin through its carboxyl group and its amine function is protected. The amino acids which are going to form the peptide chain are thus immobilized, one after the other, on the amino group, PATENT Ref. No. KSURF 40481WO/27214.00056 which is deprotected beforehand each time, of the portion of the peptide chain already formed, and which is attached to the resin. When the whole of the desired peptide chain has been formed, the protective groups of the different amino acids forming the peptide chain are eliminated and the peptide is detached from the resin with the aid of an acid. [0054] It is understood that “prevention” as used in the present disclosure, includes the complete prevention of infection by a ASFV, but also encompasses a reduction in the severity of or incidence of clinical signs associated with or caused by ASFV infection. Such prevention is also referred to herein as a protective effect. [0055] The disclosure likewise concerns the use of a composition according to the disclosure, for the preparation of a medicament intended for the prevention or the treatment of infection by a ASFV. [0056] These compounds can be administered by the systemic route, in particular by the intravenous route, by the intramuscular, intradermal or subcutaneous route, or by the oral route. In a more preferred manner, the vaccine composition comprising polypeptides according to the disclosure will be administered by the intramuscular route, through the food or by nebulization several times, staggered over time. [0057] Their administration modes, dosages and optimum pharmaceutical forms can be determined according to the criteria generally taken into account in the establishment of a treatment adapted to an animal such as, for example, the age or the weight, the seriousness of its general condition, the tolerance to the treatment and the secondary effects noted. Preferably, the vaccine of the present disclosure is administered in an amount that is protective or provides a protective effect against ASFV infection. [0058] For example, in the case of a vaccine according to the present disclosure comprising a polypeptide encoded by a nucleotide sequence of the genome of ASFV, or a homologue or fragment thereof, the polypeptide will be administered one time or several times, spread out over time, directly or by means of a transformed cell capable of expressing the polypeptide, in an amount of about 0.1 to 10 µg per kilogram weight of the animal, preferably about 0.2 to about 5 µg/kg, more preferably about 0.5 to about 2 µg/kg for a dose. PATENT Ref. No. KSURF 40481WO/27214.00056 [0059] Desirably, the vaccine is administered to an animal not yet exposed to the ASF virus. When administered as a liquid, the present vaccine may be prepared in the form of an aqueous solution, syrup, an elixir, a tincture and the like. Such formulations are known in the art and are typically prepared by dissolution of the antigen and other typical additives in the appropriate carrier or solvent systems. Suitable carriers or solvents include, but are not limited to, water, saline, ethanol, ethylene glycol, glycerol, etc. Typical additives are, for example, certified dyes, flavors, sweeteners and antimicrobial preservatives such as thimerosal (sodium ethylmercurithiosalicylate). Such solutions may be stabilized, for example, by addition of partially hydrolyzed gelatin, sorbitol or cell culture medium, and may be buffered by conventional methods using reagents known in the art, such as sodium hydrogen phosphate, sodium dihydrogen phosphate, potassium hydrogen phosphate, potassium dihydrogen phosphate, a mixture thereof, and the like. [0060] Liquid formulations also may include suspensions and emulsions that contain suspending or emulsifying agents in combination with other standard co-formulants. These types of liquid formulations may be prepared by conventional methods. Suspensions, for example, may be prepared using a colloid mill. Emulsions, for example, may be prepared using a homogenizer. [0061] Parenteral formulations, designed for injection into body fluid systems, require proper isotonicity and pH buffering to the corresponding levels of body fluids. Isotonicity can be appropriately adjusted with sodium chloride and other salts as needed. Suitable solvents, such as ethanol or propylene glycol, can be used to increase the solubility of the ingredients in the formulation and the stability of the liquid preparation. Further additives that can be employed in the present vaccine include, but are not limited to, dextrose, conventional antioxidants and conventional chelating agents such as ethylenediamine tetraacetic acid (EDTA). Parenteral dosage forms must also be sterilized prior to use. [0062] The composition according to the disclosure may be applied intradermally, intratracheally, or intravaginally. The composition preferably may be applied intramuscularly or intranasally. In an animal body, it can prove advantageous to apply the pharmaceutical compositions as described above via an intravenous injection or by direct injection into target tissues. For systemic application, the intravenous, intravascular, intramuscular, intranasal, intraarterial, intraperitoneal, oral, or intrathecal routes are preferred. A more local application can PATENT Ref. No. KSURF 40481WO/27214.00056 be effected subcutaneously, intradermally, intracutaneously, intracardially, intralobally, intramedullarly, intrapulmonarily or directly in or near the tissue to be treated (connective-, bone- , muscle-, nerve-, epithelial tissue). Depending on the desired duration and effectiveness of the treatment, the compositions according to the disclosure may be administered once or several times, also intermittently, for instance on a daily basis for several days, weeks or months, and in different dosages. EXAMPLE 1 [0063] Materials and Methods [0064] Cell lines: Baby hamster kidney cells (BHK-21, ATCC CCL-10) and African green monkey kidney clone E6 cells (Vero E6, ATCC, CRL-1586) were grown in Dulbecco’s Modified Eagle’s Medium (DMEM) supplemented with 10% fetal bovine serum (FBS), MEM nonessential amino acids (NEAA), 1% antibiotic-antimycotic (100X), all from Thermo Fisher Scientific ^TM . Cells were cultured at 37°C, 5% CO2 with 95% humidity. [0065] Sequences of vectors and genes: A Full-length rVSV plasmid and four recombinant VSV accessory plasmids encoding for VSV-N, VSV-P, VSV-L, and VSV-G proteins were obtained from Kerafast (Boston, MA). The gene of envelope protein from Classical Swine Fever Virus (CSFV) and 10 genes from ASFV Georgia 2007 strain were from the Diego Laboratory and their sequences are listed below. These sequences included the sequence encoding CSFV envelope (1896bp) (SEQ ID NO. 1), the sequence encoding B646-Ub (2190bp) (SEQ ID NO. 2), the sequence encoding CP204L-Ub (834bp) (SEQ ID NO. 3), the sequence encoding E183L-Ub (804bp) (SEQ ID NO.4), the sequence encoding B602L (1617bp) (SEQ ID NO.5), the sequence encoding CP530R (1617bp) (SEQ ID NO. 6), the sequence encoding E199L (624bp) (SEQ ID NO.7), the sequence encoding E153R (501bp) (SEQ ID NO.8), the sequence encoding EP402R (1107bp) (SEQ ID NO.9), the sequence encoding I73R (243bp) (SEQ ID NO.10), the sequence encoding EP364R (1134bp) (SEQ ID NO. 11), and the sequence of pAK-VSV-ΔG (11793pb) (SEQ ID NO.12). [0066] Plasmid construction: The pAK-VSV-E-ASFV-Antigen(Ag) expression plasmids were constructed using the subcloning method. The fragment encoding the glycoprotein of VSV was replaced by the fragment encoding the envelope of CSFV using MluI and AvrII restriction PATENT Ref. No. KSURF 40481WO/27214.00056 enzymes (NEB). Then, the sequences encoding ASFV antigens (Ag) were inserted into a spot between the N and P fragments using PacI and AscI restriction enzymes. [0067] Recovery of rVSV-ΔG/E-Ag: BHK-21 cells were infected with Vaccinia virus (vTF7-5, from Dr. Tom Fuerst and Dr. Bernard Moss at NIH AIDS) for 1h, followed by co- transfection of five plasmids: the full length rVSV-ΔG/E-Ag and VSV accessory plasmids encoding for the N, P, L, and G proteins. All of them were under T7 promoter control. The medium from transfected cells was harvested at 48h post transfection. It was clarified by centrifugation at 14, 000 X g for 5 min and filtered through 0.22µm syringe filters. The virus titers (TCID ₅₀ ) were monitored by checking cytopathic effect (CPE) on Vero E6 cells in the presence of 1-β-D- arabinofuranosylcytosine (25 µg/ml). The high titer of the recovered virus was obtained by passing 13 times in Vero E6 cells after the subunit expression of ASFV was verified by IFA. EXAMPLE 2 [0068] Pigs (4-week old) were vaccinated 3 times i.m. with 10 ⁶ TCID50 of each antigen subunit, i.e. a total of 1x10 ⁷ TCID ₅₀ per pig per vaccination round. [0069] First vaccination was with recombinant Orf virus; booster vaccination was given 3 weeks later with recombinant VSVs; and a third vaccination was performed with the initial Orf virus cocktail. [0070] Two weeks after the third immunization, all pigs were challenged with 25 HAUs of the virulent ASFV Armenia 2007 strain. The animals were observed for 15 days post challenge. Results are shown in the figures. [0071]