Antigenic structure analysis of glycosylated protein 3 of porcine reproductive and respiratory syndrome virus

被引：37

作者：

Zhou, Yan-Jun ^{[1
]}

An, Tong-Qing ^{[1
]}

He, Yun-Xia ^{[1
]}

Liu, Jin-Xia ^{[1
]}

Qiu, Hua-Ji ^{[1
]}

Wang, Yun-Feng ^{[1
]}

Tong, Guangzhi ^{[1
]}

机构：

[1] Chinese Acad Agr Sci, Harbin Vet Res Inst, Natl Key Lab Vet Biotechnol, Harbin 150001, Peoples R China

来源：

VIRUS RESEARCH | 2006年 / 118卷 / 1-2期

基金：

中国国家自然科学基金;

关键词：

PRRSV; GP3; epitope;

D O I：

10.1016/j.virusres.2005.11.019

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

The function of the glycosylated protein 3 (GP3), a porcine reproductive and respiratory syndrome virus (PRRSV) associated protein is poorly known. In the present study, the gene encoding GP3 (ORF3), lacking the highly hydrophobic domain in the N- and C-termini was expressed as GST-fusion proteins in E. coli. Monoclonal antibodies (MAbs) against GP3 were developed and used to probe a series of GP3 peptides using ELISA. After precise analysis by sequential deletion of the terminal amino acid residues from each peptide, the minimal epitopes recognized by the MAbs were localized to W(74)CRIGHDRCGED(85) and Y(67)EPGRSLW(74). The epitope sequences were well conserved among most of the North American-type isolates, with the exception of two amino acid mutations in both epitopes in a few of these isolates. Mutational analysis revealed that these mutants were not recognized by any of the five MAbs, indicating that genetic variation could lead to altered antigenicity. Eight out of nine peptide fragments, 58-72aa, 73-87aa, 88-101aa, 102-115aa, 50-65aa, 66-81aa, 80-95aa and 94-109aa were recognized by PRRSV-positive pig serum as determined by Western blot analysis. The results herein may elucidate partially the antigenic structure of GP3 and variations of PRRSV. (c) 2005 Elsevier B.V. All rights reserved.

引用

页码：98 / 104

页数：7

共 23 条

[1] Monoclonal antibody analysis of porcine reproductive and respiratory syndrome virus epitopes associated with antibody-dependent enhancement and neutralization of virus infectionle [J].