CAS OpenIR  > 中科院上海应用物理研究所2011-2019年
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.
2013
Source PublicationCELL REPORTS
ISSN2211-1247
Volume3Issue:3Pages:CONCATENATE(Sheet1!I39,-Sheet1!J39)
AbstractA 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.
Indexed BySCI
Language英语
Funding Project应物所项目组
WOS IDWOS:000321896000021
Citation statistics
Cited Times:63[WOS]   [WOS Record]     [Related Records in WOS]
Document Type期刊论文
Identifierhttp://ir.sinap.ac.cn/handle/331007/13677
Collection中科院上海应用物理研究所2011-2019年
Recommended Citation
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).
Files in This Item: Download All
File Name/Size DocType Version Access License
Bat-Derived Influenz(1672KB) 开放获取CC BY-NC-SAView Download
Related Services
Recommend this item
Bookmark
Usage statistics
Export to Endnote
Google Scholar
Similar articles in Google Scholar
[Sun, Xiaoman]'s Articles
[Shi, Yi]'s Articles
[Lu, Xishan]'s Articles
Baidu academic
Similar articles in Baidu academic
[Sun, Xiaoman]'s Articles
[Shi, Yi]'s Articles
[Lu, Xishan]'s Articles
Bing Scholar
Similar articles in Bing Scholar
[Sun, Xiaoman]'s Articles
[Shi, Yi]'s Articles
[Lu, Xishan]'s Articles
Terms of Use
No data!
Social Bookmark/Share
File name: Bat-Derived Influenza Hemagglutinin H17 Does Not Bind Canonical Avian or Human Receptors and Most Likely Uses a Unique Entry Mechanism.pdf
Format: Adobe PDF
All comments (0)
No comment.
 

Items in the repository are protected by copyright, with all rights reserved, unless otherwise indicated.