Single-amino-acid mutation in the HA alters the recognition of H9N2 influenza virus by a monoclonal antibody

文献类型： 外文期刊

第一作者： Ping, Jihui

作者： Ping, Jihui;Li, Chengjun;Deng, Guohua;Jiang, Yongping;Tian, Guobin;Bu, Zhigao;Chen, Hualan;Ping, Jihui;Zhang, Shuxia

作者机构：

关键词： avian influenza virus;H9N2 subtype;genetic basis;antigenic variation

期刊名称：BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS （ 影响因子：3.575； 五年影响因子：3.381 ）

ISSN： 0006-291X

年卷期： 2008 年 371 卷 1 期

页码：

收录情况： SCI

摘要： We explored the molecular basis of antigenic variation by comparing two H9N2 subtype avian influenza viruses, A/Chicken/Shandong/6/96 (CK/SD/6) and A/Chicken/Guangxi/10/99 (CK/GX/10), that react differently to a monoclonal antibody C/B3. To assess the genetic basis for this antigenic difference, we used reverse genetics to generate a series of chimera and mutants of these two viruses. We found that a single-amino-acid substitution of asparagine for serine at position 145 (S145N) in the HA protein prevents the reaction of CK/SD/6 virus with C/B3. Substitution of serine for asparagine at the same position (N145S) enables the CK/GX/10 to react with C/B3 in hemaglutinin inhibition, immunofluorescence and neutralization assays. We further demonstrated that the amino acid N145 in the H9 HA protein is glycosylated. Our results provide experimental evidence that the glycosylation of HA oligosaccharide attachment sites implicated in antibody binding could have a role in antigenic variation. (C) 2008 Elsevier Inc. All rights reserved.

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