MERS coronavirus envelope protein has a single transmembrane domain that forms pentameric ion channels.
Identifieur interne : 001288 ( Main/Exploration ); précédent : 001287; suivant : 001289MERS 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.
Descripteurs français
- KwdFr :
- Canaux ioniques (), Canaux ioniques (métabolisme), Conformation des protéines, Coronavirus du syndrome respiratoire du Moyen-Orient (), Coronavirus du syndrome respiratoire du Moyen-Orient (physiologie), Humains, Multimérisation de protéines, Protéines de l'enveloppe virale (), Protéines de l'enveloppe virale (métabolisme).
- MESH :
- métabolisme : Canaux ioniques, Protéines de l'enveloppe virale.
- physiologie : Coronavirus du syndrome respiratoire du Moyen-Orient.
- Canaux ioniques, Conformation des protéines, Coronavirus du syndrome respiratoire du Moyen-Orient, Humains, Multimérisation de protéines, Protéines de l'enveloppe virale.
English descriptors
- KwdEn :
- 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
Affiliations:
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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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