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MERS coronavirus envelope protein has a single transmembrane domain that forms pentameric ion channels.

Identifieur interne : 000E51 ( PubMed/Curation ); précédent : 000E50; suivant : 000E52

MERS coronavirus envelope protein has a single transmembrane domain that forms pentameric ion channels.

Auteurs : Wahyu Surya [Singapour] ; Yan Li [Singapour] ; Carmina Verdià-Bàguena [Espagne] ; Vicente M. Aguilella [Espagne] ; Jaume Torres [Singapour]

Source :

Virus research [ 1872-7492 ] ; 2015.

RBID : pubmed:25733052

Descripteurs français

English descriptors

KwdEn :
- Humans, Ion Channels (chemistry), Ion Channels (metabolism), Middle East Respiratory Syndrome Coronavirus (chemistry), Middle East Respiratory Syndrome Coronavirus (physiology), Protein Conformation, Protein Multimerization, Viral Envelope Proteins (chemistry), Viral Envelope Proteins (metabolism).
MESH :
- chemical , chemistry : Ion Channels, Viral Envelope Proteins.
- chemical , metabolism : Ion Channels, Viral Envelope Proteins.
- chemistry : Middle East Respiratory Syndrome Coronavirus.
- physiology : Middle East Respiratory Syndrome Coronavirus.
- Humans, Protein Conformation, Protein Multimerization.

Abstract

The Middle East respiratory syndrome coronavirus (MERS-CoV) is a newly identified pathogen able of human transmission that causes a mortality of almost 40%. As in the case of SARS-CoV, MERS virus lacking E protein represents a potential vaccine. In both cases, abolishment of channel activity may be a contributor to the attenuation observed in E-deleted viruses. Herein, we report that purified MERS-CoV E protein, like SARS-CoV E protein, is almost fully α-helical, has a single α-helical transmembrane domain, and forms pentameric ion channels in lipid bilayers. Based on these similarities, and the proposed involvement of channel activity as virulence factor in SARS-CoV E protein, MERS-CoV E protein may constitute a potential drug target.

DOI: 10.1016/j.virusres.2015.02.023
PubMed: 25733052

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Le document en format XML

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<front><div type="abstract" xml:lang="en">The Middle East respiratory syndrome coronavirus (MERS-CoV) is a newly identified pathogen able of human transmission that causes a mortality of almost 40%. As in the case of SARS-CoV, MERS virus lacking E protein represents a potential vaccine. In both cases, abolishment of channel activity may be a contributor to the attenuation observed in E-deleted viruses. Herein, we report that purified MERS-CoV E protein, like SARS-CoV E protein, is almost fully α-helical, has a single α-helical transmembrane domain, and forms pentameric ion channels in lipid bilayers. Based on these similarities, and the proposed involvement of channel activity as virulence factor in SARS-CoV E protein, MERS-CoV E protein may constitute a potential drug target. </div>
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MERS coronavirus envelope protein has a single transmembrane domain that forms pentameric ion channels.

MERS coronavirus envelope protein has a single transmembrane domain that forms pentameric ion channels.

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