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

Wahyu Surya; Yan Li; Carmina Verdià-Bàguena; Vicente M. Aguilella; Jaume Torres

doi:10.1016/j.virusres.2015.02.023

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

Wahyu Surya, Yan Li, Carmina Verdià-Bàguena, Vicente M. Aguilella, Jaume Torres^*

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

68 Citations (Scopus)

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.

Original language	English
Pages (from-to)	61-66
Number of pages	6
Journal	Virus Research
Volume	201
DOIs	https://doi.org/10.1016/j.virusres.2015.02.023
Publication status	Published - Apr 2 2015
Externally published	Yes

Bibliographical note

Publisher Copyright:
© 2015 Elsevier B.V.

ASJC Scopus Subject Areas

Cancer Research
Virology
Infectious Diseases

Keywords

Envelope protein
Ion channel
Middle East respiratory syndrome coronavirus (MERS)
Oligomeric state
Purification

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

Access to Document

10.1016/j.virusres.2015.02.023

Cite this

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title = "MERS coronavirus envelope protein has a single transmembrane domain that forms pentameric ion channels",

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.",

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author = "Wahyu Surya and Yan Li and Carmina Verdi{\`a}-B{\`a}guena and Aguilella, {Vicente M.} and Jaume Torres",

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doi = "10.1016/j.virusres.2015.02.023",

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T1 - MERS coronavirus envelope protein has a single transmembrane domain that forms pentameric ion channels

AU - Surya, Wahyu

AU - Li, Yan

AU - Verdià-Bàguena, Carmina

AU - Aguilella, Vicente M.

AU - Torres, Jaume

PY - 2015/4/2

Y1 - 2015/4/2

N2 - 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.

AB - 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.

KW - Envelope protein

KW - Ion channel

KW - Middle East respiratory syndrome coronavirus (MERS)

KW - Oligomeric state

KW - Purification

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

Abstract

Bibliographical note

ASJC Scopus Subject Areas

Keywords

UN SDGs

Access to Document

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