Impact of a potential glycosylation site at neuraminidase amino acid 264 of influenza A/H9N2 virus

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• 作者：Hongxia Shao^a ; ^b ; ¹ ; Xiaoxiang Zhou^a ; ^b ; ¹ ; Zhonglei Fan^a ; ^b ; ¹ ; Zhimin Wan^a ; ^c ; Kun Qian^a ; ^b ; Daniel Perez^c ; Aijian Qin^a ; ^b ; ^{aijian@yzu.edu.cn} ; Jianqiang Ye^a ; ^b ; ^{jqye@yzu.edu.cn}
• 关键词：H9N2 ; NA264N ; Virus rescuing ; Viral replication ; Pathogenesis
• 刊名：Veterinary Microbiology
• 出版年：2016
• 出版时间：30 November 2016
• 年：2016
• 卷：196
• 期：Complete
• 页码：9-13
• 全文大小：1261 K
• 卷排序：196

文摘

Large sequence analysis revealed that a mutation from histidine to asparagine at position 264 (H264N) of H9N2 NA generated a potential glycosylation site at residues 264–266 (N-X-S). H9N2 isolates with NA264N have been prevalent since 2010 in China, but not in other countries. Using four reverse genetic viruses first demonstrates the impact of NA264N of H9N2 influenza A virus in vitro and in vivo.