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

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...

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Autores principales: Surya, Wahyu, Li, Yan, Verdià-Bàguena, Carmina, Aguilella, Vicente M., Torres, Jaume
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier B.V. 2015
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7114494/
https://www.ncbi.nlm.nih.gov/pubmed/25733052
http://dx.doi.org/10.1016/j.virusres.2015.02.023
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author Surya, Wahyu
Li, Yan
Verdià-Bàguena, Carmina
Aguilella, Vicente M.
Torres, Jaume
author_facet Surya, Wahyu
Li, Yan
Verdià-Bàguena, Carmina
Aguilella, Vicente M.
Torres, Jaume
author_sort Surya, Wahyu
collection PubMed
description 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.
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spelling pubmed-71144942020-04-02 MERS coronavirus envelope protein has a single transmembrane domain that forms pentameric ion channels Surya, Wahyu Li, Yan Verdià-Bàguena, Carmina Aguilella, Vicente M. Torres, Jaume Virus Res Article 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. Elsevier B.V. 2015-04-02 2015-02-27 /pmc/articles/PMC7114494/ /pubmed/25733052 http://dx.doi.org/10.1016/j.virusres.2015.02.023 Text en Copyright © 2015 Elsevier B.V. All rights reserved. Since January 2020 Elsevier has created a COVID-19 resource centre with free information in English and Mandarin on the novel coronavirus COVID-19. The COVID-19 resource centre is hosted on Elsevier Connect, the company's public news and information website. Elsevier hereby grants permission to make all its COVID-19-related research that is available on the COVID-19 resource centre - including this research content - immediately available in PubMed Central and other publicly funded repositories, such as the WHO COVID database with rights for unrestricted research re-use and analyses in any form or by any means with acknowledgement of the original source. These permissions are granted for free by Elsevier for as long as the COVID-19 resource centre remains active.
spellingShingle Article
Surya, Wahyu
Li, Yan
Verdià-Bàguena, Carmina
Aguilella, Vicente M.
Torres, Jaume
MERS coronavirus envelope protein has a single transmembrane domain that forms pentameric ion channels
title MERS coronavirus envelope protein has a single transmembrane domain that forms pentameric ion channels
title_full MERS coronavirus envelope protein has a single transmembrane domain that forms pentameric ion channels
title_fullStr MERS coronavirus envelope protein has a single transmembrane domain that forms pentameric ion channels
title_full_unstemmed MERS coronavirus envelope protein has a single transmembrane domain that forms pentameric ion channels
title_short MERS coronavirus envelope protein has a single transmembrane domain that forms pentameric ion channels
title_sort mers coronavirus envelope protein has a single transmembrane domain that forms pentameric ion channels
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7114494/
https://www.ncbi.nlm.nih.gov/pubmed/25733052
http://dx.doi.org/10.1016/j.virusres.2015.02.023
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