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

被引：41

作者：

Ping, Jihui ^{[1
,2
]}

Li, Chengjun ^{[1
]}

Deng, Guohua ^{[1
]}

Jiang, Yongping ^{[1
]}

Tian, Guobin ^{[1
]}

Zhang, Shuxia ^{[2
]}

Bu, Zhigao ^{[1
]}

Chen, Hualan ^{[1
]}

机构：

[1] CAAS, Harbin Vet Res Inst, Harbin 150001, Heilongjiang, Peoples R China

[2] Nanjing Agr Univ, Jiangsu 210095, Peoples R China

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2008年 / 371卷 / 01期

关键词：

avian influenza virus; H9N2; subtype; genetic basis; antigenic variation;

D O I：

10.1016/j.bbrc.2008.04.045

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

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.

引用

页码：168 / 171

页数：4