Paramyxovirus Glycoproteins and the Membrane Fusion Process

被引：46
作者：
Aguilar H.C. [1 ,2 ,3 ]
Henderson B.A. [1 ,3 ]
Zamora J.L. [1 ]
Johnston G.P. [3 ]
机构：
[1] Paul G. Allen School for Global Animal Health, Washington State University, 240 Ott Road, Pullman, 99164-0790, WA
[2] Department of Veterinary Microbiology and Pathology, Washington State University, Pullman, 99164, WA
[3] School of Molecular Biosciences, Washington State University, Pullman, 99164, WA
来源：
Current Clinical Microbiology Reports | 2016年 / 3卷 / 3期
关键词：
Association model; Attachment; Attachment glycoprotein; Dissociation model; F-triggering; Fusion; Fusion cascade; Fusion glycoprotein; Fusion model; Fusion pore formation; Hemifusion; Hendra; Hexamer of trimers; hMPV; Measles; Membrane fusion; Mumps; NDV; Nipah; Paramyxoviridae; Paramyxovirus; Post-fusion; Pre-fusion; Pre-hairpin intermediate; RSV; Syncytia; Viral entry; Viral receptors;
D O I：
10.1007/s40588-016-0040-8
中图分类号：
学科分类号：
摘要：
The family Paramyxoviridae includes many viruses that significantly affect human and animal health. An essential step in the paramyxovirus life cycle is viral entry into host cells, mediated by virus-cell membrane fusion. Upon viral entry, infection results in expression of the paramyxoviral glycoproteins on the infected cell surface. This can lead to cell-cell fusion (syncytia formation), often linked to pathogenesis. Thus, membrane fusion is essential for both viral entry and cell-cell fusion and an attractive target for therapeutic development. While there are important differences between viral-cell and cell-cell membrane fusion, many aspects are conserved. The paramyxoviruses generally utilize two envelope glycoproteins to orchestrate membrane fusion. Here, we discuss the roles of these glycoproteins in distinct steps of the membrane fusion process. These findings can offer insights into evolutionary relationships among Paramyxoviridae genera and offer future targets for prophylactic and therapeutic development. © 2016, Springer International Publishing AG.
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页码：142 / 154
页数：12
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