Glycosylation of the Hemagglutinin Protein of H5N1 Influenza Virus Increases Its Virulence in Mice by Exacerbating the Host Immune Response

文献类型： 外文期刊

第一作者： Zhao, Dongming

作者： Zhao, Dongming;Liang, Libin;Wang, Shuai;Li, Yanbing;Liu, Liling;Guan, Yuntao;Bu, Zhigao;Chen, Hualan;Zhao, Dongming;Nakao, Tomomi;Fukuyama, Satoshi;Bu, Zhigao;Kawaoka, Yoshihiro;Kawaoka, Yoshihiro

作者机构：

关键词： H5N1 viruses;glycosylation;mouse;pathogenicity

期刊名称：JOURNAL OF VIROLOGY （ 影响因子：5.103； 五年影响因子：5.078 ）

ISSN：

年卷期：

页码：

收录情况： SCI

摘要： The highly pathogenic avian influenza (HPAI) H5N1 viruses continue to circulate in nature and threaten public health. Although several viral determinants and host factors that influence the virulence of HPAI H5N1 viruses in mammals have been identified, the detailed molecular mechanism remains poorly defined and requires further clarification. In our previous studies, we characterized two naturally isolated HPAI H5N1 viruses that had similar viral genomes but differed substantially in their lethality in mice. In this study, we explored the molecular determinants and potential mechanism for this difference in virulence. By using reverse genetics, we found that a single amino acid at position 158 of the hemagglutinin (HA) protein substantially affected the systemic replication and pathogenicity of these H5N1 influenza viruses in mice. We further found that the G158N mutation introduced an N-linked glycosylation at positions 158 to 160 of the HA protein and that this N-linked glycosylation enhanced viral productivity in infected mammalian cells and induced stronger host immune and inflammatory responses to viral infection. These findings further our understanding of the determinants of pathogenicity of H5N1 viruses in mammals.

分类号： Q934.2

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