Growth and spectroscopy of ZnWO₄:Ho³⁺ crystal

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• 作者：Fugui Yang ; Chaoyang Tu ; Hongyan Wang ; Yanping Wei ; Zhenyu You ; Guohua Jia ; Jianfu Li ; Zhaojie Zhu ; Xiuai Lu ; Yan Wang
• 关键词：Avian influenza virus ; H9N2 subtype ; Genetic basis ; Antigenic variation
• 刊名：Journal of Alloys and Compounds
• 出版年：2008
• 出版时间：8 May 2008
• 年：2008
• 卷：455
• 期：1-2
• 页码：269-273
• 全文大小：148 K

文摘

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.