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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...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Elsevier Inc.
2004
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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. |
format | Online Article Text |
id | pubmed-7111769 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2004 |
publisher | Elsevier Inc. |
record_format | MEDLINE/PubMed |
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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