N-glycosylation on hemagglutinin head reveals inter-branch antigenic variability of avian influenza virus H5-subtypes

文献类型： 外文期刊

第一作者： Shi, Keyi

作者： Shi, Keyi;Feng, Saixiang;Zhao, Li;Chen, Junhong;Song, Wei;Jia, Yusheng;Qu, Xiaoyun;Jia, Weixin;Liao, Ming;Liu, Zhicheng;Du, Shouwen;Liao, Ming;Liao, Ming;Du, Shouwen

作者机构：

关键词： H5-subtype AIV; N-glycosylation; Antigenicity of hemagglutinin

期刊名称：INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES （ 影响因子：7.7； 五年影响因子：7.7 ）

ISSN： 0141-8130

年卷期： 2024 年 273 卷

页码：

收录情况： SCI

摘要： H5-subtype avian influenza virus (AIV) is globally prevalent and undergoes frequent antigenic drift, necessitating regular updates to vaccines. One of the many influencing elements that cause incompatibility between vaccinations and epidemic strains is the dynamic alteration of glycosylation sites. However, the biological significance of N-glycosylation in the viral evolution and antigenic changes is unclear. Here, we performed a systematic analysis of glycosylation sites on the HA1 subunit of H5N1, providing insights into the changes of primary glycosylation sites, including 140 N, 156 N, and 170 N within the antigenic epitopes of HA1 protein. Multiple recombinant viruses were then generated based on HA genes of historical vaccine strains and deactivated for immunizing SPF chickens. Inactivated recombinant strains showed relatively closer antigenicity compared to which has identical N-glycosylation patterns. The N-glycosylation modification discrepancy highlights the interbranch antigenic diversity of H5-subtype viruses in avian influenza and serves as a vital foundation for improving vaccination tactics.

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