Modes of paramyxovirus fusion: a Henipavirus perspective

被引:76
作者
Lee, Benhur [1 ,2 ]
Ataman, Zeynep Akyol [1 ]
机构
[1] Univ Calif Los Angeles, David Geffen Sch Med, Dept Microbiol Immunol & Mol Genet, Los Angeles, CA 90095 USA
[2] Univ Calif Los Angeles, David Geffen Sch Med, Dept Pathol & Lab Med, Los Angeles, CA 90095 USA
基金
美国国家卫生研究院;
关键词
NEWCASTLE-DISEASE VIRUS; HEMAGGLUTININ-NEURAMINIDASE PROTEIN; INDIVIDUAL OLIGOSACCHARIDE CHAINS; HENDRA-VIRUS; NIPAH-VIRUS; MEASLES-VIRUS; RECEPTOR-BINDING; MEMBRANE-FUSION; ATTACHMENT GLYCOPROTEIN; CRYSTAL-STRUCTURE;
D O I
10.1016/j.tim.2011.03.005
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Henipavirus is a new genus of Paramyxoviridae that uses protein-based receptors (ephrinB2 and ephrinB3) for virus entry. Paramyxovirus entry requires the coordinated action of the fusion (F) and attachment viral envelope glycoproteins. Receptor binding to the attachment protein triggers F to undergo a conformational cascade that results in membrane fusion. The accumulation of structural and functional studies on many paramyxoviral fusion and attachment proteins, including the recent elucidation of structures of Nipah virus (NiV) and Hendra virus (HeV) G glycoproteins bound and unbound to cognate ephrinB receptors, indicate that henipavirus entry and fusion could differ mechanistically from paramyxoviruses that use glycan-based receptors.
引用
收藏
页码:389 / 399
页数:11
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