Envelope Protein Dynamics in Paramyxovirus Entry

ABSTRACT Paramyxoviruses include major pathogens with significant global health and economic impact. This large family of enveloped RNA viruses infects cells by employing two surface glycoproteins that tightly cooperate to fuse their lipid envelopes with the target cell plasma membrane, an attachmen...

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Autores principales:	Philippe Plattet, Richard K. Plemper
Formato:	article
Lenguaje:	EN
Publicado:	American Society for Microbiology 2013
Materias:	Microbiology QR1-502
Acceso en línea:	https://doaj.org/article/4c2a07d33a244ce8b50e6e8c65aaeb81
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spelling	oai:doaj.org-article:4c2a07d33a244ce8b50e6e8c65aaeb812021-11-15T15:43:09ZEnvelope Protein Dynamics in Paramyxovirus Entry10.1128/mBio.00413-132150-7511https://doaj.org/article/4c2a07d33a244ce8b50e6e8c65aaeb812013-08-01T00:00:00Zhttps://journals.asm.org/doi/10.1128/mBio.00413-13https://doaj.org/toc/2150-7511ABSTRACT Paramyxoviruses include major pathogens with significant global health and economic impact. This large family of enveloped RNA viruses infects cells by employing two surface glycoproteins that tightly cooperate to fuse their lipid envelopes with the target cell plasma membrane, an attachment and a fusion (F) protein. Membrane fusion is believed to depend on receptor-induced conformational changes within the attachment protein that lead to the activation and subsequent refolding of F. While structural and mechanistic studies have considerably advanced our insight into paramyxovirus cell adhesion and the structural basis of F refolding, how precisely the attachment protein links receptor engagement to F triggering remained poorly understood. Recent reports based on work with several paramyxovirus family members have transformed our understanding of the triggering mechanism of the membrane fusion machinery. Here, we review these recent findings, which (i) offer a broader mechanistic understanding of the paramyxovirus cell entry system, (ii) illuminate key similarities and differences between entry strategies of different paramyxovirus family members, and (iii) suggest new strategies for the development of novel therapeutics.Philippe PlattetRichard K. PlemperAmerican Society for MicrobiologyarticleMicrobiologyQR1-502ENmBio, Vol 4, Iss 4 (2013)
institution	DOAJ
collection	DOAJ
language	EN
topic	Microbiology QR1-502
spellingShingle	Microbiology QR1-502 Philippe Plattet Richard K. Plemper Envelope Protein Dynamics in Paramyxovirus Entry
description	ABSTRACT Paramyxoviruses include major pathogens with significant global health and economic impact. This large family of enveloped RNA viruses infects cells by employing two surface glycoproteins that tightly cooperate to fuse their lipid envelopes with the target cell plasma membrane, an attachment and a fusion (F) protein. Membrane fusion is believed to depend on receptor-induced conformational changes within the attachment protein that lead to the activation and subsequent refolding of F. While structural and mechanistic studies have considerably advanced our insight into paramyxovirus cell adhesion and the structural basis of F refolding, how precisely the attachment protein links receptor engagement to F triggering remained poorly understood. Recent reports based on work with several paramyxovirus family members have transformed our understanding of the triggering mechanism of the membrane fusion machinery. Here, we review these recent findings, which (i) offer a broader mechanistic understanding of the paramyxovirus cell entry system, (ii) illuminate key similarities and differences between entry strategies of different paramyxovirus family members, and (iii) suggest new strategies for the development of novel therapeutics.
format	article
author	Philippe Plattet Richard K. Plemper
author_facet	Philippe Plattet Richard K. Plemper
author_sort	Philippe Plattet
title	Envelope Protein Dynamics in Paramyxovirus Entry
title_short	Envelope Protein Dynamics in Paramyxovirus Entry
title_full	Envelope Protein Dynamics in Paramyxovirus Entry
title_fullStr	Envelope Protein Dynamics in Paramyxovirus Entry
title_full_unstemmed	Envelope Protein Dynamics in Paramyxovirus Entry
title_sort	envelope protein dynamics in paramyxovirus entry
publisher	American Society for Microbiology
publishDate	2013
url	https://doaj.org/article/4c2a07d33a244ce8b50e6e8c65aaeb81
work_keys_str_mv	AT philippeplattet envelopeproteindynamicsinparamyxovirusentry AT richardkplemper envelopeproteindynamicsinparamyxovirusentry
_version_	1718427581212000256

Envelope Protein Dynamics in Paramyxovirus Entry

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