CN104292300B - The epitope minimum motif peptide of tri- structural proteins of VP1, VP2 and VP4 and its application in the O-shaped strain of foot and mouth disease virus (O/BY/CHA/2010) - Google Patents
The epitope minimum motif peptide of tri- structural proteins of VP1, VP2 and VP4 and its application in the O-shaped strain of foot and mouth disease virus (O/BY/CHA/2010) Download PDFInfo
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Abstract
The invention belongs to biological medicine and technical field of biological, the epitope minimum motif peptide of tri- structural proteins of VP1, VP2 and VP4 and its application in specially a kind of O-shaped strain of foot and mouth disease virus (O/BY/CHA/2010).5 linear epitope minimum motif peptides provided by the invention can be used as researching and developing new resisting O-type foot and mouth disease virus recombinant multi-epitope peptide vaccine candidate's epi-position peptide, and its amino acid sequence is respectively SEQ.ID NO.1~SEQ.ID NO.5.The present invention also provides the candidate's epi-position of the detection antigen for the recombinant multi-epitope peptide for being used as the high specific and high sensitive for developing diagnosis foot and mouth disease virus popularity, and its amino acid sequence is as shown in SEQ.ID NO.6~SEQ.ID NO.10.
Description
Technical field
The invention belongs to biological medicine and technical field of biological, and in particular to O-shaped foot and mouth disease virus (FMDV) strain
(O/BY/CHA/2010) Structural protein VP1, VP2 and VP4 epitope minimum motif peptide, extension peptide and its application in.
Background technology
Livestock foot-and-mouth disease is that livestock contagious disease the most serious in the world today, main harm pig, ox, sheep etc. is cloven-hoofed dynamic
Aftosa is classified as first of A class infectious diseases by thing, World Organization for Animal Health.For many years, aftosa worldwide large-scale outbreak and
Prevalence, huge economic losses are caused to animal husbandry.According to immunogenicity, foot and mouth disease virus has A, O, C, SAT I, SAT II, SAT
III and Asia I totally 7 serotypes and the hypotype of more than 65.
Immunity inoculation is the main path of developing country's prevention aftosa outburst.Traditional inactivated vaccine has immunogenicity
High, the advantages that protectiveness is good, but it is possible that vaccine inactivation is not thorough or viral escape, so as to cause the outburst stream of aftosa
OK, have potential dangerous.Therefore, Many researchers turn to the research to recombinant vaccine and multivalence peptide vaccine.With regard to the latter
For recombinant multi-epitope peptide vaccine, preferable vaccine should include Linear B Cell Epitopes (hereinafter referred to as linear epitope) and T simultaneously
Cell epitope, the former induces generation antibody in B cell, and the latter can then stimulate T cell to produce cell factor, promote B cell
Secretory antibody.Therefore, the Screening and Identification of both epitopes is always the important research content in virology and vaccinology research field,
For example, just there is research report (such as Tang H, Liu X S, Fang Y Z, the et al.The of the antigenic peptide of correlation before
Epitopes of Foot and Mouth Disease[J].Asian Journal of Animal and Veterinary
Advances,2012,7(12):1261-1265；Blanco E,McCullough K,Summerfield A,et
al.Interspecies major histocompatibility complex-restricted Th cell epitope
on foot-and-mouth disease virus capsid protein VP4[J].J Virol,2000,74:4902–
4907；Wang Jialong etc..).
But although the authentication method of this respect it is hundreds and thousands of (Wu Jing and Wu Wutong .B cell protein epitopes
Progress of Research Methods Pharmaceutical Biotechnologies, 7 (4)：239-242,2000；Shen Guanxin etc. translates antibody technique experiment guide science
Publishing house, 2002；The progress life sciences of the .B such as Wang Honglin cell epitopes positioning, 21:317-319,2009), as more than
Enumerate shown in document, due to being limited by linear (non-conformation type) B cell epitope Identification method, identified in the past be all without
It is that longer 16 are poly- or longer antigenic peptide mostly that antibody identification minimum motif (is generally made up of) qualification result 3~8 residues
(antigenic peptide), rather than real epitope peptide.In addition, presented in synthetic peptide vaccine to recombinant multi-epitope peptide epidemic disease
(Shi YP, Hasnain, SE, Sacci JB, et al.Immunogenicity and in vitro under the background of seedling development
protective efficacy of a recombinant multistage Plasmodium falciparum
candidate vaccine.Proc.Natl.Acad.Sci.USA.96,1615–162,1999；He YP,Xu WX,Hong
AZ,et al.Immunogenic comparison for two different recombinant chimeric
peptides(CP12 and CP22)containing one or two copies of three linear B cell
epitopes from β-hCG subunit.J Biotechnol,151:15-21,2011), it is effectively pre- in order to develop antibody
Anti- property target virus multi-epitope peptide vaccine, the identification of target protein linear epitope and its antibody identification minimum motif just seem particularly heavy
Will.
It is well known that identified from target protein the invention of one section of antigenic peptide that can induce antibody tormation have novelty and
Creativeness, therefore such granted patent can be found everywhere both at home and abroad.Identify what each antibody can identify from target protein
Fine epitope peptide, also or its () is comprised in one section of published antigenic peptide sequence, and it equally has novelty and wound
The property made, because it is equally the needs of practical application, such as developing the field of the recombinant multi-epitope peptide based on epitope minimum motif peptide
Close, it is possible to which combination linear epitope peptide is (because for be adapted to such as Escherichia coli and/or the high table of eukaryotic as much as possible
Consider up to development cost, the artificial antigen peptide limited length of design, typically in 200 amino acid residues or so, wherein to be true
Multi-epitope peptide has strongly immunogenic designed by guarantor, it is necessary to while the broad spectrum activity for combining general 10~30 residues of length aids in by force
Property and cytotoxic t cell epitope peptide for sars), also can help to produce it is specific needed for effective epitope antibodies (due to Linear B Cell table
Position is made up of maximum 8 residues of minimum 3 residues, it is clear that may have N number of epitope in long antigenic peptide, it is possible to produce
N number of epitope antibodies, and it is minimum from fine epitope peptide N number of epitope number can then to be reduced to, and with sharp purpose antibody tormation, keeps away simultaneously
Exempt from other antibody tormations that may be harmful to).In a word, identify that the meaning of fine epitope peptide and application benefit are aobvious on invention target protein
And it is clear to.
It is pointed out that because aftosa to national economy, the significant impact of trade, be known as " political economy disease " it
Claim, so the research for foot and mouth disease virus vaccine is long-standing, and first successful identification epitope peptide and realize base
It is especially in the majority to study O-shaped FMDV because of the virus (ref.) of synthetic peptide vaccine.Pfaff et al. just identifies early in nineteen eighty-two
FMDV O 1K VP 1 (144-159aa) LRGDLQVLAQKVARTL be a main antibody combining site (Pfaff E,
Mussgay M,HO,Schulz GE,Schaller H.Antibodies against a preselected
peptide recognize and neutralize foot and mouth disease virus.EMBO J.1982；1
(7):869-74.)；In same year, Bittle et al. has found that FMDV is O-shaped, the VP1 (25-41aa) of Kaufbeuren strains
(200-213) be main B cell antigen epi-position (Bittle JL, Houghten RA, Alexander H, Shinnick TM,
Sutcliffe JG,Lerner RA,Rowlands DJ,Brown F.Protection against foot-and-mouth
disease by immunization with a chemically synthesized peptide predicted from
the viral nucleotide sequence.Nature.1982 Jul 1；298(5869):30-3.).But due to by
The limitation of epitope Identification method, it is difficult to carry out minimum motif identification.Due to this 3 peptide fragments between FMDV is various or in type not
With conservative, the variation of FMDV strains is very fast in addition, once new epidemic situation occurs, it is necessary to specific aim vaccine is set up again.Hereafter,
It is related to the identification of Asial I type coat protein epitopes, VP1 (1-12aa), (17-29aa), (194-211aa)；VP2
(40-50aa), VP3 (26-39aa), VP4 (30-41), but do not carry out fine Epitope Identification (Zhang ZW to it equally1,
Zhang YG,Wang YL,Pan L,Fang YZ,Jiang ST,Lü JL,Zhou P.Screening and
identification of B cell epitopes of structural proteins of foot-and-mouth
disease virus serotype Asia1.Vet Microbiol.2010 Jan6；140(1-2):25-33.).Grind above
Study carefully from while a side reflection target protein epitope scanning mapping and minimum motif identification not a duck soup, also confirm that the present invention 5
Individual O-shaped FMDV epitope fine identifies the demand of really practical application, can embody creativeness.
The content of the invention
It is an object of the invention to provide 3 structure eggs in foot and mouth disease virus (FMDV) O-shaped strain (O/BY/CHA/2010)
White fine epitope peptide, and the extension peptide (8 peptide) of these epitope minimum motif peptides or it is longer than the anti-of the small peptide (8 peptide)
It is former；Also provide the minimum motif peptide, minimum motif peptide extension small peptide (8 peptide) or be longer than the small peptide (8 peptide) antigen should
With.
Present disclosure is more specifically described as follows.
In order to realize that the present invention provides the fine epitope peptide of foot and mouth disease virus (FMDV) O-shaped 3 structural proteins of strain
Purpose, we utilize the O-shaped standard serums of the anti-FMDV of cavy, the O-shaped poison of FMDV of pop by improveing biosynthesis peptide method
Strain O/BY/CHA/2010 3 structural proteins have carried out linear epitope scanning mapping research.In covering VP1, VP2 and VP4 tri-
In the overlapping 18 poly- peptide of structural proteins full length sequence, identification can standard serum generation immunoblotting reaction O-shaped with the anti-FMDV of cavy
Antigenic peptide；Overlapping 8 peptide sequence is further designed for antigenic peptide, determines that it is fine anti-by immunoblotting reaction
Former epitope and amino acid sequence.Test result indicates that：By improveing biosynthesis peptide method and the O-shaped standard serums of the anti-FMDV of cavy
Effectively identify the fine antigen table of 3 structural proteins contained by the O-shaped strain of foot and mouth disease virus (O/BY/CHA/2010)
Position peptide.
The present invention provides tri- structural proteins of VP1, VP2 and VP4 in the O-shaped strain of foot and mouth disease virus (O/BY/CHA/2010)
Epitope minimum motif peptide, it is identified with the O-shaped standard serums of the anti-FMDV of cavy, shares 5 epitopes, its amino acid sequence difference
For：Shown in SEQ.ID NO.1, SEQ.ID NO.2, SEQ.ID NO.3, SEQ.ID NO.4 and SEQ.ID NO.5.
Wherein, the amino acid sequence of the minimum epitope motifs peptide of VP1 structural proteins is SEQ.ID NO.1 and SEQ.ID
Shown in NO.2, FMDV is designated as successively:VP1142-147、FMDV:VP1204-208；The amino of the minimum epitope motifs peptide of VP2 structural proteins
Acid sequence is shown in SEQ.ID NO.3 and SEQ.ID NO.4, is designated as FMDV successively:VP28-13、FMDV:VP214-18；VP4 structures
The amino acid sequence of the minimum epitope motifs peptide of albumen is shown in SEQ.ID NO.5, is designated as FMDV:VP422-27。
The present invention also provides the extension small peptide of above-mentioned 5 minimum epitope motifs peptides, and its amino acid sequence is followed successively by SEQ.ID
Shown in No.6~SEQ.ID No.10, when chemical synthesis or amalgamation and expression albumen in use, extension residue moiety can additions and deletions or
Substitute.
The present invention also provides described minimum epitope motifs peptide in recombinant multi-epitope peptide vaccine preparation, medicine or prepares detection
Application in terms of antibody.
The extension small peptide that the present invention also provides epitope minimum motif peptide is preparing aftosa epidemiological diagnosis alone or in combination
Serum identification epitope tag marker application.
The fine epitope peptide of the O-shaped strain of above-mentioned foot and mouth disease virus (O/BY/CHA/2010) structural proteins, at other
There is also weight that is, as structure for FMDV (O-shaped, A types, Asial I types, c-type, SAT I, SAT II, SAT III) popular strain
Group multi-epitope peptide vaccine is also effective to its alloytype mouth disease virus strain.
Brief description of the drawings
Fig. 1 is the SDS-PAGE analysis results of VP1 21 18 peptide amalgamation and expressions；Figure 1A：Swimming lane 1：BL21 (DE3) empty bacterium
The total protein of expression, swimming lane 2：The truncation GST188 albumen of pXXGST-1 plasmid expressions, swimming lane 3~14：The covered structure of expression
18 poly- peptide P1~P12 fusion proteins of overlapped 10 residues of albumen VP1 overall lengths, swimming lane 15：Molecular weight of albumen Marker；
Figure 1B：Swimming lane 1：The total protein of BL21 (DE3) empty bacterium expression, swimming lane 2：The truncation GST188 albumen of pXXGST-1 plasmid expressions,
Swimming lane 3~11：The poly- peptide P13~P21 fusion proteins of VP1 structural proteins 18 of expression, swimming lane 12：Molecular weight of albumen Marker.Mesh
Band be located at position corresponding at 25kDa, truncate GST188 carrier proteins and be slightly less than restructuring destination protein.In 1B figures swimming lane 5
Purpose band is also 18 poly- peptides, and possible amino acid composition and primary structure difference cause mobility relatively low.
Fig. 2 is SDS-PAGE points of the 18 poly- peptide fusion proteins for expressing VP2 26 overlapped 10 residues of structural proteins
Analyse result；Fig. 2A swimming lanes 1：The truncation GST188 albumen of pXXGST-1 plasmid expressions, swimming lane 2~14：The VP2 structural proteins of expression
18 poly- peptide P1~P13 fusion proteins, swimming lane 15：Molecular weight of albumen Marker；Fig. 2 B：Swimming lane 1：PXXGST-1 plasmid expressions
GST188 albumen, swimming lane 2~14：The poly- peptide P14~P26 fusion proteins of VP2 structural proteins 18 of expression, swimming lane 15：Protein molecular
Measure Marker.Purpose band is located at position more on the lower side at 25kDa, truncates GST188 carrier proteins and is slightly less than restructuring purpose egg
In vain.
Fig. 3 is the SDS-PAGE analysis results for expressing VP4 10 18 poly- peptide fusion proteins of structural proteins：Swimming lane 1：
The GST188 albumen of pXXGST-1 plasmid expressions, swimming lane 2~11：18 poly- peptide P1~P10 fusion proteins of VP4 structural proteins are expressed,
Swimming lane 12：Molecular weight of albumen Marker.Purpose band is located at position more on the lower side at 25kDa, truncates GST188 carrier proteins
It is slightly less than restructuring destination protein.
The western blotting qualification of 3 structural proteins of Fig. 4 FMDV O/BY/CHA/2010 strains, 18 poly- peptide；Fig. 4 A：Swimming lane 1
Compareed for BL21 (DE3) empty bacteriums total protein, swimming lane 2 is that pXXGST-1 expresses GST188 protein controls, and swimming lane 3~11 is followed successively by
The poly- peptide P13~P21 fusion proteins of VP1 structural proteins 18, swimming lane 12 are molecular weight of albumen Marker；Fig. 4 B：Swimming lane 1 is
PXXGST-1 plasmid expression GST188 protein controls, swimming lane 2~14 are followed successively by VP2 structural proteins P1~P13, and swimming lane 15 is albumen
Molecular weight Marker；Fig. 4 C：Swimming lane 1 is GST188 protein controls, and swimming lane 2~11 is followed successively by VP4 structural proteins P1~P10 fusions
Albumen, swimming lane 12 are molecular weight of albumen Marker.
Fig. 5 VP1 141aa-160aa 8 peptides clone structure and expression note：1 is that pXXGST-1 is compareed, and 2~14 are followed successively by
8 peptides are recombinated, 15 be Marker.Purpose band protein band obvious between 25kDa~15kDa, truncate GST188
Carrier protein is slightly less than restructuring destination protein.
Fig. 6 VP1-14 8 peptides clone structure and expression；Wherein：1 is that pXXGST-1 is compareed, and 2~11 are followed successively by VP1-14-
1~VP1-14-10,12 be Marker.
Fig. 7 VP1-20 8 peptides clone structure and expression；Wherein：1 is that pXXGST-1 is compareed, and 2~12 are followed successively by VP1-20-
1~VP1-20-11,13 be Marker.
Fig. 8 VP1-21 8 peptides clone structure and expression；Wherein：1 is that pXXGST-1 is compareed, and 2~7 are followed successively by VP1-21-1
~VP1-21-6,8 be Marker.
Fig. 9 VP2-1 8 peptides clone structure and expression；Wherein：1~11 is followed successively by VP2-1-1~VP2-1-11, and 12 are
Marker。
Figure 10 VP2-2 8 peptides clone structure and expression；Wherein：1 is that pXXGST-1 is compareed, and 2~9 are followed successively by VP2-2-1
~VP2-2-8,10 be Marker.
Figure 11 VP4-3 8 peptides clone structure and expression；Wherein：1 is that BL21 (DE3) empty bacterium compares, and 2 be pXXGST-1 pairs
According to 3~13 are followed successively by VP4-3-1~VP4-3-11, and 14 be Marker.
Figure 12 VP1 141-160 8 peptide western blotting qualifications；Wherein：1 is that pXXGST-1 is compareed, and 2~14 are followed successively by
VP1-N~VP1-Z, 15 be Marker.
Figure 13 VP1-14, VP1-20, VP1-21 8 peptide western blotting qualifications；Wherein：Figure 13 A：1 is pXXGST-1 pairs
According to 2~11 are followed successively by VP1-14-1~VP1-14-10, and 12 be Marker；Figure 13 B：1 is that pXXGST-1 is compareed, and 2~12 successively
It is Marker for VP1-20-1~VP1-20-11,13；Figure 13 C：1 be pXXGST-1 compare, 2~6 be followed successively by VP1-21-2~
VP1-21-6,7 be Marker.
Figure 14 VP2-1 and VP2-2 8 peptide western blotting qualifications；Wherein：Figure 14 A：1 be pXXGST-1 compare, 2~12 according to
Secondary is VP2-1-1~VP2-1-11, and 13 be Marker；Figure 14 B：1 be pXXGST-1 compare, 2~9 be followed successively by VP2-2-1~
VP2-2-8,10 be Marker.
Figure 15 VP4-3 8 peptide western blotting qualifications；Wherein：1 be pXXGST-1 compare, 2~13 be followed successively by VP4-3-1~
VP4-3-11,14 be Marker.
Embodiment
The present invention can be described further by following Examples.Illustrative example is not intended to limit model involved in the present invention
Enclose, the scope has been sufficiently clarified in description before.The experimental method of unreceipted actual conditions in the following example,
The third edition " the molecule gram of the translations such as Huang Peitang is write according to normal condition and [U.S.] J. Pehanorm Brookers and D.W. Russells
It is grand：Laboratory manual " (Science Press, 2002) and [U.S.] E. breathe out Lip river and D. Lay grace writes " the antibody skill of the translations such as Shen Guanxin
The step of described in art experiment guide " (Science Press, 2002), or carried out according to the condition of production and sales business suggestion.
Embodiment 1
The present embodiment is the identification of FMDV O/BY/CHA/20104 structural proteins fine epitope of O-shaped strain：
(1) the poly- peptide coding DNA fragment design of target protein series 18/8
Gene according to the O-shaped strain O/BY/CHA/2010 of FMDV tri- structural proteins of VP1, VP2, VP4 in GenBank
Sequence (GenBank accession number JN998085.1), after carrying out e. coli codon optimization to it, design three albumen bases of covering
Because of 18/8 poly- peptide coding DNA fragment of the overlapped 10 aa residues of full length sequence, and at its both ends respectively plus BamH I and
TAA-Sal I cohesive end sequences, the positive minus strand fragment of each small peptide coding DNA of chemical synthesis.Complete 18 poly- pepscan of the first round
After mapping, reactivity peptide fragment is designed to 8 poly- peptides of overlapped 7 residues of series, while the epitope for finding before
The serial 8 poly- peptides of VP1 (21-40) and VP1 (141-160) designs, carry out the second wheel antibody identification meter position minimum motif identification.
(2) structure of series structure of small peptide fusion protein expression plasmid, screening and identification
By molecular cloning method, the 18/8 of synthesis poly- peptide positive and negative chain encoding DNA fragmentation is annealed two-by-two, then passed through
They are connected overnight by DNA ligase with the carrier pXXGST-1 through BamH I and Sal I double digestions respectively, and next day will connect and produce
Thing Transformed E .coliBL21 (DE3) competence bacterial strain, it is coated on the LB flat boards for adding Amp.Choose single bacterium colony be inoculated in 3mL added with
In Amp LB fluid nutrient mediums, 220r/min, after 30 DEG C are shaken 16~18h of bacterium, bacterium solution is transferred to new 3mL in 2% ratio and added
Have in Amp LB fluid nutrient mediums, continue 220r/min, 30 DEG C of culture 4h, until cell density OD600Light absorption value reaches 0.6,
Then in 42 DEG C of induced expression 5h；Take 1mL bacterium solutions that thalline is collected by centrifugation, add 50 μ L ddH2After O suspension thallines, 50 are added
μ L 2 × loading Buffer is mixed, and 5min is placed in boiling water, 14000r/min centrifugation 10min, takes 10 μ L of supernatant to carry out SDS-
PAGE electrophoresis (15% separation gel), negative control are with vehicle Control pXXGST-1 transformed bacterias.Fig. 1-Fig. 3 is the SDS- of 18 peptides
PAGE results；Fig. 5-Figure 11 is 8 peptides clone structure and expression.
Take small peptide fusion protein to be more than the recombinant clone bacterium progress DNA sequencing that carrier protein compares 1~2kDa, verify eachization
Learn the correctness of synthesis small peptide coding fragment sequence.
(3) western blotting qualification of 18/8 poly- peptide of antigen reactivity
Serial 18/8 poly- peptide clone bacterium correct to DNA sequencing carries out thermal induction expression, collects total bacterial protein and directly enters
Capable western blotting qualification, i.e. electrophoresis is terminated into each induction bacterium total protein electrotransfer on rear PAGE gel to aperture 0.2
μm cellulose acetate film on, with 5% skim milk (being prepared with PBST) close 2h；Add the O-shaped standard blood of the anti-FMDV of cavy
(being diluted with 5% skim milk by its potency) is incubated 1h clearly；Washed 3 times, 5min/ times with PBST；Add horseradish peroxidating
The rabbit Anti-cavy IgG (being diluted with 5% skim milk by its potency) of thing enzyme mark is incubated 1h；Washed 3 times with cleaning solution,
5min/ times；Experimental result is detected with exposure instrument and (uses ECL substrate luminescence reagents box).Fig. 4 is the Western blotting of 18 poly- peptides
Qualification result；Figure 12-Figure 15 is the western blotting qualification result of 8 peptides clone.
(4) determination of antigen epitope minimum motif
The 8 poly- peptide of reactivity screened is as shown in table 1,
The 18 poly- peptides and the determination of 8 poly- peptides and fine epitope that the immunoblotting reaction of table 1 screens
Fine epitope VP1 142-147 (PNVRGD), VP1204-208 are determined according to their consensus sequence
(KIVAP), VP2 8-13 (TLLEDR), VP2 14-18 (ILTTR), VP4 22-27 (INNYYM).
Claims (2)
1. the epitope minimum motif peptide of VP4 structural proteins, its amino in a kind of foot and mouth disease virus O type strains O/BY/CHA/2010
Acid sequence is SEQ.ID NO.5.
2. the minimum epitope of VP4 structural proteins in the O-shaped strain O/BY/CHA/2010 of foot and mouth disease virus as claimed in claim 1
Motif peptide, the application in terms of recombinant multi-epitope peptide vaccine preparation, medicine or preparation detection antibody.
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| CN104873967A (en) * | 2015-04-30 | 2015-09-02 | 中国农业科学院特产研究所 | O type foot and mouth disease virus-like particle vaccine as well as preparation method and application thereof |
| CN106749646B (en) * | 2016-12-22 | 2020-12-22 | 中国农业科学院哈尔滨兽医研究所 | Foot-and-mouth disease virus serotype shared epitope recognized by monoclonal antibody 3D9 and application thereof |
| CN107253979B (en) * | 2017-05-17 | 2020-09-29 | 中国农业科学院哈尔滨兽医研究所 | Foot-and-mouth disease virus serotype shared epitope recognized by monoclonal antibody 10B10 and application thereof |
| CN108931644B (en) * | 2018-07-19 | 2021-09-10 | 河南省农业科学院 | Foot-and-mouth disease virus immune antibody evaluation and infection and immune differential diagnosis dual test strip |
| CN108761093B (en) * | 2018-07-19 | 2020-12-25 | 河南百奥生物工程有限公司 | Test strip for evaluating foot-and-mouth disease virus antibody |
| CN117304277B (en) * | 2023-09-26 | 2024-03-08 | 中国农业科学院兰州兽医研究所 | O-type foot-and-mouth disease virus VP4 protein T cell epitope polypeptide and application thereof |
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| CN101643720A (en) * | 2009-07-31 | 2010-02-10 | 中国农业科学院哈尔滨兽医研究所 | Antiviral serotype shared monoclonal antibody of foot-and-mouth disease and distinguished epitope thereof |
| CN103183728A (en) * | 2013-03-25 | 2013-07-03 | 中国牧工商(集团)总公司 | Polypeptide used for preparing O type peptide vaccine of cattle foot-and-mouth disease and preparation methods and applications thereof |
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| CN101643720A (en) * | 2009-07-31 | 2010-02-10 | 中国农业科学院哈尔滨兽医研究所 | Antiviral serotype shared monoclonal antibody of foot-and-mouth disease and distinguished epitope thereof |
| CN103183728A (en) * | 2013-03-25 | 2013-07-03 | 中国牧工商(集团)总公司 | Polypeptide used for preparing O type peptide vaccine of cattle foot-and-mouth disease and preparation methods and applications thereof |
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