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口蹄疫病毒A/WH/09株结构蛋白P1基因的克隆及其B细胞抗原表位的预测 被引量:5

Cloning,sequencing and prediction of B cell epitope of structural protein P1 gene of foot-and-mouth disease virus strain A/WH/09
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摘要 对口蹄疫病毒(FMDV)A/WH/09株P1结构蛋白基因进行了扩增、克隆及序列测定。结果显示,FMDV A/WH/09株P1基因长2 208bp,包含完整的开放阅读框,编码736个氨基酸,其中VP1长636bp,编码212个氨基酸;VP2长654bp,编码218个氨基酸;VP3长663bp,编码221个氨基酸;VP4长255bp,编码85个氨基酸。采用DNAStar Protean软件对P1蛋白的二级结构、可塑性、亲水性、表面可及性及抗原指数等参数进行了综合分析,并预测其B细胞的抗原表位分布。结果表明,VP1、VP2和VP3上均有多个区域为B细胞抗原优势表位,VP4上也有少量潜在的B细胞抗原表位。与已鉴定的B细胞抗原表位相比,本试验所用方法预测的结果有较高的准确度,是一种较为先进的表位研究方法。 A P1 gene was amplified from foot-and-mouth disease virus strain A/WH/09 and cloned,and then sequenced.In result,the P1 gene was 2 208 bp in length that encodes a polypeptide of 736 amino acids,including complete open reading frame.VP1,VP2,VP3 and VP4 gene of the P1 gene are 636,654,663 and 255 bp in size and coded for 212,218,221 and 85 amino acids,respectively.The secondary structure,flexibility,hydrophilicity,accessibility and antigenicity of P1 were analyzed using DNAStar Protean software,and the B cell epitopes were predicted.The results showed that there were several domains in VP1,VP2 and VP3 which belonged to predominant B cell epitopes and a few of B cell epitopes were in VP4.Comparing with the epitopes that have been published,the results predicted by this method had high reliability and this method was a more advanced epitope research approach.
出处 《中国兽医科学》 CAS CSCD 北大核心 2011年第3期221-228,共8页 Chinese Veterinary Science
基金 国家"十二五"高技术研究发展计划(863)项目(2011AA10A211)
关键词 口蹄疫病毒 结构蛋白P1 测序 B细胞抗原表位 foot-and-mouth disease virus structural protein P1 sequencing B cell epitope
作者简介 娄慧(1985-),女,吉林临江人,硕士。 通讯作者,E—mail:yongguang.zhang@163.com
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参考文献14

  • 1HOPP T P,WOODS K R. Prediction of protein antigenic deter-minants from amino acid sequences[J]. Proc Natl Acad Sci USA, 1981,78(6) : 3824-3828.
  • 2KYTE J, DOOLITTLE R F. A simple method for displaying hydropathic character of a protein[J]. J Mol Biol, 1982,157 (1) :105-132.
  • 3TSCHE H. Modern Methods in Protein and Nucleic Acid Research[M]. New York:Walter de Gruger Berlin, 1990.
  • 4WELLING G W,WEIJER W J,VAN DER ZEE R,et al. Prediction of sequential antigenic regions in proteins[J]. FEBS Lett, 1985,188(2):215-218.
  • 5KARPLUS P A,SCHULTZ G E. Prediction of chain flexibility in proteins[J]. Naturwissenschaften, 1985,72(4) : 212-213.
  • 6GERSHONI J M, STEIN B, VENISOVA G. Combinatorial libraries,epitope structure and the prediction of protein confor-mations[J]. Immunol Today, 1997,18 (3) : 108-110.
  • 7SAIZ J C, GONZALEZ M J, BOREA M V, et al. Identification of neutralizing antigenic sites on VP1 and VP2 of type A5 foot-and-mouth disease virus,defined by neutralization-resistant va- riants[J]. J Viro1,1991,65(5) :2518-2524.
  • 8JACKSON T,KING A M,STUART D I,et al. Structure and receptor binding[J]. Virus Res, 2003,91 (1) : 33-46.
  • 9MELOEN R H,LANGEVELD J P,SCHAAPER W M,etal. Synthetic peptide vaccines:unexpected fulfillment of discarded hope? [J]. Biologicals, 2001,29 (3/4) : 233-236.
  • 10CARRILLO C, WIGDOROVITZ A, OLIVEROS J C, et al. Protective immune response to foot-and-mouth disease virus with VP1 expressed in transgenic plants[J]. J Virol, 1998,72 (2) : 1688-1690.

二级参考文献13

  • 1吴玉章,朱锡华,张凌.Pre-S2蛋白抗体结合部位的确定[J].免疫学杂志,1993,9(1):8-12. 被引量:5
  • 2吴玉章,朱锡华.蛋白质抗原表位的研究[J].科学(中文版),1994(1):93-94. 被引量:18
  • 3吴玉章,朱锡华,张凌.Pre-S_(2)蛋白B细胞表位的精细特异性[J].免疫学杂志,1994,10(2):80-82. 被引量:6
  • 4丁达夫 汤海旭 等.同源蛋白质三级结构的预测.理论物理与生命科学[M].上海:上海科学技术出版社,1997.119-148.
  • 5Grubman M J, Baxt B.Clin Microbiol Rev, 2004,17:465-493.
  • 6Eric B, Carmen M, Ruiz-Jarabo, et al .Virology, 2001,288 : 192-202.
  • 7Haste Andersen P, Nielsen M, Lund O.Protein Sci, 2006,15 ( 11 ) : 2558-2567.
  • 8Durek T, Torbeev VY, Kent SB.Proc Natl Acad Sci USA, 2007, 104 ( 12 ) : 4846-51.
  • 9Mahler M, Btuthner M, Pollard KM.Clin Immunol, 2003,107( 2 ) : 65-79.
  • 10Maeda K, Mizukoshi F, Hamano M, et al .J Clin Microbiol, 2004,42( 3 ):1095 - 1098.

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