Bat-Derived Influenza Hemagglutinin H17 Does Not Bind Canonical Avian or Human Receptors and Most Likely Uses a Unique Entry Mechanism
Sun, Xiaoman ; Shi, Yi ; Lu, Xishan ; He, Jianhua(何建华) ; Gao, Feng ; Yan, Jinghua ; Qi, Jianxun ; Gao, George F.
刊名CELL REPORTS
2013
卷号3期号:3页码:CONCATENATE(Sheet1!I39,-Sheet1!J39)
ISSN号2211-1247
英文摘要A new influenza-like virus genome (H17N10) was recently discovered in bats and offers a new perspective about the origin and evolution of influenza viruses. The viral envelope glycoprotein hemagglutinin (HA) is responsible for influenza virus receptor binding, fusion, and entry into the cell; therefore, the structure and function of HA H17 was characterized. The 2.70 angstrom resolution crystal structure revealed that H17 has a typical influenza A virus HA fold, but with some special features, including a distorted putative sialic acid (SA) binding site and low thermostability. No binding to either the canonical human alpha 2,6 SA-linkage or avian alpha 2,3 SA-linkage receptor was observed. Furthermore, H17 glycan binding was not detected using a chip covering more than 600 glycans. Our results demonstrate that H17 is unique among characterized HAs and that the bat-derived influenza virus may use a different entry mechanism compared to canonical influenza viruses.
收录类别SCI
语种英语
WOS记录号WOS:000321896000021
公开日期2014-06-13
内容类型期刊论文
源URL[http://ir.sinap.ac.cn/handle/331007/13677]  
专题上海应用物理研究所_中科院上海应用物理研究所2011-2017年
推荐引用方式
GB/T 7714
Sun, Xiaoman,Shi, Yi,Lu, Xishan,et al. Bat-Derived Influenza Hemagglutinin H17 Does Not Bind Canonical Avian or Human Receptors and Most Likely Uses a Unique Entry Mechanism[J]. CELL REPORTS,2013,3(3):CONCATENATE(Sheet1!I39,-Sheet1!J39).
APA Sun, Xiaoman.,Shi, Yi.,Lu, Xishan.,He, Jianhua.,Gao, Feng.,...&Gao, George F..(2013).Bat-Derived Influenza Hemagglutinin H17 Does Not Bind Canonical Avian or Human Receptors and Most Likely Uses a Unique Entry Mechanism.CELL REPORTS,3(3),CONCATENATE(Sheet1!I39,-Sheet1!J39).
MLA Sun, Xiaoman,et al."Bat-Derived Influenza Hemagglutinin H17 Does Not Bind Canonical Avian or Human Receptors and Most Likely Uses a Unique Entry Mechanism".CELL REPORTS 3.3(2013):CONCATENATE(Sheet1!I39,-Sheet1!J39).
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