The amino-terminal residue of glycoprotein B is critical for neutralization of bovine herpesvirus 1

The amino-terminal residue of glycoprotein B is critical for neutralization of bovine herpesvirus 1
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DOI:
10.1016/j.virusres.2005.07.008
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发表时间:
2006-02-01
期刊:
影响因子:
5
通讯作者:
Kida, H
Kida, H
中科院分区:
医学3区
文献类型:
--
作者:
Okazaki, K;Fujii, S;Kida, H

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为了确定牛疱疹病毒1型(BHV 1)糖蛋白B(gB)的中和表位,本研究使用了一组单克隆抗体(MAb)、一系列截短形式的糖蛋白和MAb逃逸突变体。用单克隆抗体对糖蛋白的截短进行免疫细胞化学分析,结果表明,单克隆抗体识别的中和表位位于成熟gB的残基1和52之间。突变体、亲本和回复突变体病毒之间的序列比较表明,逃逸突变体的成熟gB的氨基末端残基从Arg变为Gln。这些发现表明gB的氨基末端残基对于中和BHV1至关重要。(c)2005 Elsevier B.V.保留所有权利。
In order to address the neutralization epitope on bovine herpesvirus 1 (BHV 1) glycoprotein B (gB), a panel of monoclonal antibodies (MAbs), a series of truncation forms of the glycoprotein and an MAb-escape mutant were used in this study. Immunocytochemistry on the truncations using MAbs against the glycoprotein revealed that the neutralization epitopes recognized by the MAbs lay between residues 1 and 52 of mature gB. Comparison of the sequences among the mutant, parent, and revertant viruses demonstrated that the amino-terminal residue of mature gB of the escape mutant was changed from Arg to Gln. These findings indicate that the amino-terminal residue of gB is critical for neutralization of BHV1. (c) 2005 Elsevier B.V. All rights reserved.