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SARS coronavirus E protein forms cation-selective ion channels

Severe Acute Respiratory Syndrome (SARS) is caused by a novel coronavirus (SARS-CoV). Coronaviruses including SARS-CoV encode an envelope (E) protein, a small, hydrophobic membrane protein. We report that, in planar lipid bilayers, synthetic peptides corresponding to the SARS-CoV E protein forms ion...

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Detalles Bibliográficos
Autores principales: Wilson, Lauren, Mckinlay, Carolyn, Gage, Peter, Ewart, Gary
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier Inc. 2004
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7111769/
https://www.ncbi.nlm.nih.gov/pubmed/15527857
http://dx.doi.org/10.1016/j.virol.2004.09.033
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author Wilson, Lauren
Mckinlay, Carolyn
Gage, Peter
Ewart, Gary
author_facet Wilson, Lauren
Mckinlay, Carolyn
Gage, Peter
Ewart, Gary
author_sort Wilson, Lauren
collection PubMed
description Severe Acute Respiratory Syndrome (SARS) is caused by a novel coronavirus (SARS-CoV). Coronaviruses including SARS-CoV encode an envelope (E) protein, a small, hydrophobic membrane protein. We report that, in planar lipid bilayers, synthetic peptides corresponding to the SARS-CoV E protein forms ion channels that are more permeable to monovalent cations than to monovalent anions. Affinity-purified polyclonal antibodies recognizing the N-terminal 19 residues of SARS-CoV E protein were used to establish the specificity of channel formation by inhibiting the ion currents generated in the presence of the E protein peptides.
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spelling pubmed-71117692020-04-02 SARS coronavirus E protein forms cation-selective ion channels Wilson, Lauren Mckinlay, Carolyn Gage, Peter Ewart, Gary Virology Article Severe Acute Respiratory Syndrome (SARS) is caused by a novel coronavirus (SARS-CoV). Coronaviruses including SARS-CoV encode an envelope (E) protein, a small, hydrophobic membrane protein. We report that, in planar lipid bilayers, synthetic peptides corresponding to the SARS-CoV E protein forms ion channels that are more permeable to monovalent cations than to monovalent anions. Affinity-purified polyclonal antibodies recognizing the N-terminal 19 residues of SARS-CoV E protein were used to establish the specificity of channel formation by inhibiting the ion currents generated in the presence of the E protein peptides. Elsevier Inc. 2004-12-05 2004-11-02 /pmc/articles/PMC7111769/ /pubmed/15527857 http://dx.doi.org/10.1016/j.virol.2004.09.033 Text en Copyright © 2004 Elsevier Inc. 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
Wilson, Lauren
Mckinlay, Carolyn
Gage, Peter
Ewart, Gary
SARS coronavirus E protein forms cation-selective ion channels
title SARS coronavirus E protein forms cation-selective ion channels
title_full SARS coronavirus E protein forms cation-selective ion channels
title_fullStr SARS coronavirus E protein forms cation-selective ion channels
title_full_unstemmed SARS coronavirus E protein forms cation-selective ion channels
title_short SARS coronavirus E protein forms cation-selective ion channels
title_sort sars coronavirus e protein forms cation-selective ion channels
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7111769/
https://www.ncbi.nlm.nih.gov/pubmed/15527857
http://dx.doi.org/10.1016/j.virol.2004.09.033
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