Coronavirus E protein forms ion channels with functionally and structurally-involved membrane lipids.
Identifieur interne : 001331 ( PubMed/Curation ); précédent : 001330; suivant : 001332Coronavirus E protein forms ion channels with functionally and structurally-involved membrane lipids.
Auteurs : Carmina Verdiá-Báguena [Espagne] ; Jose L. Nieto-Torres ; Antonio Alcaraz ; Marta L. Dediego ; Jaume Torres ; Vicente M. Aguilella ; Luis EnjuanesSource :
- Virology [ 1096-0341 ] ; 2012.
Descripteurs français
- KwdFr :
- Canaux ioniques (métabolisme), Coronavirus humain 229E (métabolisme), Données de séquences moléculaires, Humains, Lipides membranaires (métabolisme), Protéines de l'enveloppe virale (), Protéines de l'enveloppe virale (génétique), Protéines de l'enveloppe virale (métabolisme), Séquence d'acides aminés, Virus du SRAS (métabolisme).
- MESH :
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : Viral Envelope Proteins.
- chemical , genetics : Viral Envelope Proteins.
- chemical , metabolism : Ion Channels, Membrane Lipids, Viral Envelope Proteins.
- metabolism : Coronavirus 229E, Human, SARS Virus.
- Amino Acid Sequence, Humans, Molecular Sequence Data.
Abstract
Coronavirus (CoV) envelope (E) protein ion channel activity was determined in channels formed in planar lipid bilayers by peptides representing either the transmembrane domain of severe acute respiratory syndrome CoV (SARS-CoV) E protein, or the full-length E protein. Both of them formed a voltage independent ion conductive pore with symmetric ion transport properties. Mutations N15A and V25F located in the transmembrane domain prevented the ion conductivity. E protein derived channels showed no cation preference in non-charged lipid membranes, whereas they behaved as pores with mild cation selectivity in negatively-charged lipid membranes. The ion conductance was also controlled by the lipid composition of the membrane. Lipid charge also regulated the selectivity of a HCoV-229E E protein derived peptide. These results suggested that the lipids are functionally involved in E protein ion channel activity, forming a protein-lipid pore, a novel concept for CoV E protein ion channel entity.
DOI: 10.1016/j.virol.2012.07.005
PubMed: 22832120
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pubmed:22832120Le document en format XML
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<term>Humains</term>
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<term>Protéines de l'enveloppe virale (génétique)</term>
<term>Protéines de l'enveloppe virale (métabolisme)</term>
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<front><div type="abstract" xml:lang="en">Coronavirus (CoV) envelope (E) protein ion channel activity was determined in channels formed in planar lipid bilayers by peptides representing either the transmembrane domain of severe acute respiratory syndrome CoV (SARS-CoV) E protein, or the full-length E protein. Both of them formed a voltage independent ion conductive pore with symmetric ion transport properties. Mutations N15A and V25F located in the transmembrane domain prevented the ion conductivity. E protein derived channels showed no cation preference in non-charged lipid membranes, whereas they behaved as pores with mild cation selectivity in negatively-charged lipid membranes. The ion conductance was also controlled by the lipid composition of the membrane. Lipid charge also regulated the selectivity of a HCoV-229E E protein derived peptide. These results suggested that the lipids are functionally involved in E protein ion channel activity, forming a protein-lipid pore, a novel concept for CoV E protein ion channel entity.</div>
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<Abstract><AbstractText>Coronavirus (CoV) envelope (E) protein ion channel activity was determined in channels formed in planar lipid bilayers by peptides representing either the transmembrane domain of severe acute respiratory syndrome CoV (SARS-CoV) E protein, or the full-length E protein. Both of them formed a voltage independent ion conductive pore with symmetric ion transport properties. Mutations N15A and V25F located in the transmembrane domain prevented the ion conductivity. E protein derived channels showed no cation preference in non-charged lipid membranes, whereas they behaved as pores with mild cation selectivity in negatively-charged lipid membranes. The ion conductance was also controlled by the lipid composition of the membrane. Lipid charge also regulated the selectivity of a HCoV-229E E protein derived peptide. These results suggested that the lipids are functionally involved in E protein ion channel activity, forming a protein-lipid pore, a novel concept for CoV E protein ion channel entity.</AbstractText>
<CopyrightInformation>Copyright © 2012 Elsevier Inc. All rights reserved.</CopyrightInformation>
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