Single-amino-acid mutation in the HA alters the recognition of H9N2 influenza virus by a monoclonal antibody.
作者： Jihui Ping , Chengjun Li , Guohua Deng , Yongping Jiang , Guobin Tian
DOI: 10.1016/J.BBRC.2008.04.045
关键词:
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 genetic for this difference, we used reverse genetics generate series chimera mutants these viruses. found single-amino-acid substitution asparagine serine at position 145 (S145N) in HA protein prevents reaction CK/SD/6 virus with Substitution same (N145S) enables CK/GX/10 C/B3 hemaglutinin inhibition, immunofluorescence neutralization assays. further demonstrated amino acid N145 H9 is glycosylated. Our results provide experimental evidence glycosylation oligosaccharide attachment sites implicated binding could have role variation.
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