Paramyxovirus Fusion and Entry: Multiple Paths to a Common End

被引:174
作者
Chang, Andres [1 ]
Dutch, Rebecca E. [1 ]
机构
[1] Univ Kentucky, Coll Med, Dept Mol & Cellular Biochem, Lexington, KY 40536 USA
来源
VIRUSES-BASEL | 2012年 / 4卷 / 04期
关键词
paramyxovirus; membrane fusion; viral entry; RESPIRATORY SYNCYTIAL VIRUS; NEWCASTLE-DISEASE VIRUS; HEMAGGLUTININ-NEURAMINIDASE PROTEIN; RECEPTOR-BINDING SITE; EMERGENT DEADLY PARAMYXOVIRUS; HUMAN METAPNEUMOVIRUS LACKING; CONSERVED GLYCINE RESIDUES; PROMOTED MEMBRANE-FUSION; REPLICATION IN-VITRO; N-LINKED GLYCAN;
D O I
10.3390/v4040613
中图分类号
Q93 [微生物学];
学科分类号
071005 [微生物学];
摘要
The paramyxovirus family contains many common human pathogenic viruses, including measles, mumps, the parainfluenza viruses, respiratory syncytial virus, human metapneumovirus, and the zoonotic henipaviruses, Hendra and Nipah. While the expression of a type 1 fusion protein and a type 2 attachment protein is common to all paramyxoviruses, there is considerable variation in viral attachment, the activation and triggering of the fusion protein, and the process of viral entry. In this review, we discuss recent advances in the understanding of paramyxovirus F protein-mediated membrane fusion, an essential process in viral infectivity. We also review the role of the other surface glycoproteins in receptor binding and viral entry, and the implications for viral infection. Throughout, we concentrate on the commonalities and differences in fusion triggering and viral entry among the members of the family. Finally, we highlight key unanswered questions and how further studies can identify novel targets for the development of therapeutic treatments against these human pathogens.
引用
收藏
页码:613 / 636
页数:24
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