Bat-derived influenza-like viruses H17N10 and H18N11

被引:557
作者
Wu, Ying [1 ]
Wu, Yan [1 ,2 ]
Tefsen, Boris [1 ]
Shi, Yi [1 ,3 ]
Gao, George F. [1 ,2 ,3 ,4 ]
机构
[1] Chinese Acad Sci, Inst Microbiol, CAS Key Lab Pathogen Microbiol & Immunol, Beijing 100101, Peoples R China
[2] Chinese Acad Sci, Univ Chinese Acad Sci, Beijing 100049, Peoples R China
[3] Chinese Acad Sci, Beijing Inst Life Sci, RNIH, Beijing 100101, Peoples R China
[4] Chinese Ctr Dis Control & Prevent China CDC, Off Director Gen, Beijing 102206, Peoples R China
基金
中国国家自然科学基金;
关键词
bat-derived influenza-like virus; hemagglutinin (HA); neuraminidase (NA); PA; reassortment; H17N10; H18N11; HEMAGGLUTININ MEMBRANE GLYCOPROTEIN; RECEPTOR-BINDING SPECIFICITY; A VIRUS; EPITHELIAL RECEPTOR; CELLULAR RECEPTOR; CRYSTAL-STRUCTURE; HUMAN INFECTION; NEURAMINIDASE; PROTEIN; PA;
D O I
10.1016/j.tim.2014.01.010
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
070307 [化学生物学]; 071010 [生物化学与分子生物学];
摘要
Shorebirds and waterfowls are believed to be the reservoir hosts for influenza viruses, whereas swine putatively act as mixing vessels. The recent identification of two influenza-like virus genomes (designated H17N10 and H18N11) from bats has challenged this notion. A crucial question concerns the role bats might play in influenza virus ecology. Structural and functional studies of the two major surface envelope proteins, hemagglutinin (HA) and neuraminidase (NA), demonstrate that neither has canonical HA or NA functions found in influenza viruses. However, putative functional modules and domains in other encoded proteins are conserved, and the N-terminal domain of the H17N10 polymerase subunit PA has a classical structure and function. Therefore, potential genomic reassortments of such influenza-like viruses with canonical influenza viruses cannot be excluded at this point and should be assessed.
引用
收藏
页码:183 / 191
页数:9
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