中国科学院机构知识库网格
Chinese Academy of Sciences Institutional Repositories Grid
Structure and Receptor Binding Specificity of Hemagglutinin H13 from Avian Influenza A Virus H13N6

文献类型:期刊论文

作者Lu, Xishan1,2; Qi, Jianxun2; Shi, Yi2,7; Wang, Ming1; Smith, David F.3,4; Heimburg-Molinaro, Jamie3,4; Zhang, Yanfang6; Paulson, James C.5; Xiao, Haixia6; Gao, George F.1,2,6,7,8
刊名JOURNAL OF VIROLOGY
出版日期2013-08-01
卷号87期号:16页码:9077-9085
英文摘要Interspecies transmission (host switching/jumping) of influenza viruses is a key scientific question that must be addressed. In addition to the vigorous research on highly pathogenic avian influenza viruses (HPAIVs), studies of the mechanism of interspecies transmission of low-pathogenic avian influenza viruses (LPAIVs) could also provide insights into host tropism and virulence evolution. Influenza A viruses harboring hemagglutinin (HA) H13 (e. g., H13N6) are LPAIVs. In this study, soluble H13 HA glycoprotein was purified, and its receptor binding activity was characterized. The results revealed that H13 exclusively binds the avian alpha 2-3-linked sialic acid receptor; no binding to the mammalian alpha 2-6-linked sialic acid receptor was detected. Furthermore, the molecular basis of the H13 receptor binding specificity was revealed by comparative analysis of the crystal structures of both receptor-bound H13 and H5 HAs, which might be contributed by the hydrophobic residue V186. Work with an H13N186 mutant confirmed the importance of V186 in the receptor binding specificity of H13 HA, which shows that the mutant protein reduced the binding of an avian receptor analog but increased the binding of a human receptor analog. Detailed structural analysis also demonstrated that the conserved binding sites of the recently well-studied broadly neutralizing human monoclonal antibodies targeting the HA2 domain are found in H13. Our results expand our understanding of virulence evolution, receptor binding preference, and species tropism of the LPAIVs and HPAIVs.
WOS标题词Science & Technology ; Life Sciences & Biomedicine
类目[WOS]Virology
研究领域[WOS]Virology
关键词[WOS]SWINE-ORIGIN ; MAXIMUM-LIKELIHOOD ; INFECTION ; SUBTYPES ; GULLS ; GLYCOPROTEIN ; TRANSMISSION ; RECOGNITION ; EPITHELIUM ; INHIBITOR
收录类别SCI
语种英语
WOS记录号WOS:000322535600024
源URL[http://124.16.173.210/handle/834782/1267]  
专题天津工业生物技术研究所_蛋白质工程与疫苗实验室 高福_期刊论文
作者单位1.China Agr Univ, Coll Vet Med, Beijing 100094, Peoples R China
2.Chinese Acad Sci, Inst Microbiol, CAS Key Lab Pathogen Microbiol & Immunol, Beijing, Peoples R China
3.Emory Univ, Sch Med, Dept Biochem, O Wayne Rollins Res Ctr, Atlanta, GA 30322 USA
4.Emory Univ, Sch Med, Glyc Ctr, O Wayne Rollins Res Ctr, Atlanta, GA USA
5.Scripps Res Inst, Dept Cell & Mol Biol, La Jolla, CA 92037 USA
6.Chinese Acad Sci, Tianjin Inst Ind Biotechnol, Lab Prot Engn & Vaccines, Tianjin, Peoples R China
7.Chinese Acad Sci, Res Network Immun & Hlth, Beijing Inst Life Sci, Beijing, Peoples R China
8.Chinese Ctr Dis Control & Prevent, Inst Viral Dis Control & Prevent, Beijing, Peoples R China
推荐引用方式
GB/T 7714
Lu, Xishan,Qi, Jianxun,Shi, Yi,et al. Structure and Receptor Binding Specificity of Hemagglutinin H13 from Avian Influenza A Virus H13N6[J]. JOURNAL OF VIROLOGY,2013,87(16):9077-9085.
APA Lu, Xishan.,Qi, Jianxun.,Shi, Yi.,Wang, Ming.,Smith, David F..,...&Gao, George F..(2013).Structure and Receptor Binding Specificity of Hemagglutinin H13 from Avian Influenza A Virus H13N6.JOURNAL OF VIROLOGY,87(16),9077-9085.
MLA Lu, Xishan,et al."Structure and Receptor Binding Specificity of Hemagglutinin H13 from Avian Influenza A Virus H13N6".JOURNAL OF VIROLOGY 87.16(2013):9077-9085.

入库方式: OAI收割

来源:天津工业生物技术研究所

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