Analysis of SARS-CoV E protein ion channel activity by tuning the protein and lipid charge.
Identifieur interne : 001195 ( PubMed/Corpus ); précédent : 001194; suivant : 001196Analysis of SARS-CoV E protein ion channel activity by tuning the protein and lipid charge.
Auteurs : Carmina Verdiá-Báguena ; Jose L. Nieto-Torres ; Antonio Alcaraz ; Marta L. Dediego ; Luis Enjuanes ; Vicente M. AguilellaSource :
- Biochimica et biophysica acta [ 0006-3002 ] ; 2013.
English descriptors
- KwdEn :
- Amino Acid Sequence, Hydrogen-Ion Concentration, Ion Channels (chemistry), Ion Transport, Lipid Bilayers (chemistry), Membrane Potentials, Models, Molecular, Molecular Sequence Data, Phosphatidylcholines (chemistry), Phosphatidylserines (chemistry), Potassium (chemistry), Protein Structure, Tertiary, SARS Virus (chemistry), Static Electricity, Viral Envelope Proteins (chemistry).
- MESH :
- chemical , chemistry : Ion Channels, Lipid Bilayers, Phosphatidylcholines, Phosphatidylserines, Potassium, Viral Envelope Proteins.
- chemistry : SARS Virus.
- Amino Acid Sequence, Hydrogen-Ion Concentration, Ion Transport, Membrane Potentials, Models, Molecular, Molecular Sequence Data, Protein Structure, Tertiary, Static Electricity.
Abstract
A partial characterization of the ion channels formed by the SARS coronavirus (CoV) envelope (E) protein was previously reported (C. Verdiá-Báguena et al., 2012 [12]). Here, we provide new significant insights on the involvement of lipids in the structure and function of the CoV E protein channel on the basis of three series of experiments. First, reversal potential measurements over a wide range of pH allow the dissection of the contributions to channel selectivity coming from ionizable residues of the protein transmembrane domain and also from the negatively charged groups of diphytanoyl phosphatidylserine (DPhPS) lipid. The corresponding effective pKas are consistent with the model pKas of the acidic residue candidates for titration. Second, the change of channel conductance with salt concentration reveals two distinct regimes (Donnan-controlled electrodiffusion and bulk-like electrodiffusion) fully compatible with the outcomes of selectivity experiments. Third, by measuring channel conductance in mixtures of neutral diphytanoyl phosphatidylcholine (DPhPC) lipids and negatively charged DPhPS lipids in low and high salt concentrations we conclude that the protein-lipid conformation in the channel is likely the same in charged and neutral lipids. Overall, the whole set of experiments supports the proteolipidic structure of SARS-CoV E channels and explains the large difference in channel conductance observed between neutral and charged membranes.
DOI: 10.1016/j.bbamem.2013.05.008
PubMed: 23688394
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pubmed:23688394Le document en format XML
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Dediego</name></author><author><name sortKey="Enjuanes, Luis" sort="Enjuanes, Luis" uniqKey="Enjuanes L" first="Luis" last="Enjuanes">Luis Enjuanes</name></author><author><name sortKey="Aguilella, Vicente M" sort="Aguilella, Vicente M" uniqKey="Aguilella V" first="Vicente M" last="Aguilella">Vicente M. Aguilella</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2013">2013</date><idno type="RBID">pubmed:23688394</idno><idno type="pmid">23688394</idno><idno type="doi">10.1016/j.bbamem.2013.05.008</idno><idno type="wicri:Area/PubMed/Corpus">001195</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">001195</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Analysis of SARS-CoV E protein ion channel activity by tuning the protein and lipid charge.</title><author><name sortKey="Verdia Baguena, Carmina" sort="Verdia Baguena, Carmina" uniqKey="Verdia Baguena C" first="Carmina" last="Verdiá-Báguena">Carmina Verdiá-Báguena</name><affiliation><nlm:affiliation>Department of Physics, Laboratory of Molecular Biophysics, Universitat Jaume I, 12071 Castellón, Spain.</nlm:affiliation></affiliation></author><author><name sortKey="Nieto Torres, Jose L" sort="Nieto Torres, Jose L" uniqKey="Nieto Torres J" first="Jose L" last="Nieto-Torres">Jose L. Nieto-Torres</name></author><author><name sortKey="Alcaraz, Antonio" sort="Alcaraz, Antonio" uniqKey="Alcaraz A" first="Antonio" last="Alcaraz">Antonio Alcaraz</name></author><author><name sortKey="Dediego, Marta L" sort="Dediego, Marta L" uniqKey="Dediego M" first="Marta L" last="Dediego">Marta L. Dediego</name></author><author><name sortKey="Enjuanes, Luis" sort="Enjuanes, Luis" uniqKey="Enjuanes L" first="Luis" last="Enjuanes">Luis Enjuanes</name></author><author><name sortKey="Aguilella, Vicente M" sort="Aguilella, Vicente M" uniqKey="Aguilella V" first="Vicente M" last="Aguilella">Vicente M. Aguilella</name></author></analytic><series><title level="j">Biochimica et biophysica acta</title><idno type="ISSN">0006-3002</idno><imprint><date when="2013" type="published">2013</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence</term><term>Hydrogen-Ion Concentration</term><term>Ion Channels (chemistry)</term><term>Ion Transport</term><term>Lipid Bilayers (chemistry)</term><term>Membrane Potentials</term><term>Models, Molecular</term><term>Molecular Sequence Data</term><term>Phosphatidylcholines (chemistry)</term><term>Phosphatidylserines (chemistry)</term><term>Potassium (chemistry)</term><term>Protein Structure, Tertiary</term><term>SARS Virus (chemistry)</term><term>Static Electricity</term><term>Viral Envelope Proteins (chemistry)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Ion Channels</term><term>Lipid Bilayers</term><term>Phosphatidylcholines</term><term>Phosphatidylserines</term><term>Potassium</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Hydrogen-Ion Concentration</term><term>Ion Transport</term><term>Membrane Potentials</term><term>Models, Molecular</term><term>Molecular Sequence Data</term><term>Protein Structure, Tertiary</term><term>Static Electricity</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">A partial characterization of the ion channels formed by the SARS coronavirus (CoV) envelope (E) protein was previously reported (C. Verdiá-Báguena et al., 2012 [12]). Here, we provide new significant insights on the involvement of lipids in the structure and function of the CoV E protein channel on the basis of three series of experiments. First, reversal potential measurements over a wide range of pH allow the dissection of the contributions to channel selectivity coming from ionizable residues of the protein transmembrane domain and also from the negatively charged groups of diphytanoyl phosphatidylserine (DPhPS) lipid. The corresponding effective pKas are consistent with the model pKas of the acidic residue candidates for titration. Second, the change of channel conductance with salt concentration reveals two distinct regimes (Donnan-controlled electrodiffusion and bulk-like electrodiffusion) fully compatible with the outcomes of selectivity experiments. Third, by measuring channel conductance in mixtures of neutral diphytanoyl phosphatidylcholine (DPhPC) lipids and negatively charged DPhPS lipids in low and high salt concentrations we conclude that the protein-lipid conformation in the channel is likely the same in charged and neutral lipids. Overall, the whole set of experiments supports the proteolipidic structure of SARS-CoV E channels and explains the large difference in channel conductance observed between neutral and charged membranes. </div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">23688394</PMID><DateCompleted><Year>2013</Year><Month>08</Month><Day>27</Day></DateCompleted><DateRevised><Year>2020</Year><Month>04</Month><Day>07</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0006-3002</ISSN><JournalIssue CitedMedium="Print"><Volume>1828</Volume><Issue>9</Issue><PubDate><Year>2013</Year><Month>Sep</Month></PubDate></JournalIssue><Title>Biochimica et biophysica acta</Title><ISOAbbreviation>Biochim. Biophys. Acta</ISOAbbreviation></Journal><ArticleTitle>Analysis of SARS-CoV E protein ion channel activity by tuning the protein and lipid charge.</ArticleTitle><Pagination><MedlinePgn>2026-31</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.bbamem.2013.05.008</ELocationID><ELocationID EIdType="pii" ValidYN="Y">S0005-2736(13)00154-5</ELocationID><Abstract><AbstractText>A partial characterization of the ion channels formed by the SARS coronavirus (CoV) envelope (E) protein was previously reported (C. Verdiá-Báguena et al., 2012 [12]). Here, we provide new significant insights on the involvement of lipids in the structure and function of the CoV E protein channel on the basis of three series of experiments. First, reversal potential measurements over a wide range of pH allow the dissection of the contributions to channel selectivity coming from ionizable residues of the protein transmembrane domain and also from the negatively charged groups of diphytanoyl phosphatidylserine (DPhPS) lipid. The corresponding effective pKas are consistent with the model pKas of the acidic residue candidates for titration. Second, the change of channel conductance with salt concentration reveals two distinct regimes (Donnan-controlled electrodiffusion and bulk-like electrodiffusion) fully compatible with the outcomes of selectivity experiments. Third, by measuring channel conductance in mixtures of neutral diphytanoyl phosphatidylcholine (DPhPC) lipids and negatively charged DPhPS lipids in low and high salt concentrations we conclude that the protein-lipid conformation in the channel is likely the same in charged and neutral lipids. Overall, the whole set of experiments supports the proteolipidic structure of SARS-CoV E channels and explains the large difference in channel conductance observed between neutral and charged membranes. </AbstractText><CopyrightInformation>Copyright © 2013 Elsevier B.V. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Verdiá-Báguena</LastName><ForeName>Carmina</ForeName><Initials>C</Initials><AffiliationInfo><Affiliation>Department of Physics, Laboratory of Molecular Biophysics, Universitat Jaume I, 12071 Castellón, Spain.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Nieto-Torres</LastName><ForeName>Jose L</ForeName><Initials>JL</Initials></Author><Author ValidYN="Y"><LastName>Alcaraz</LastName><ForeName>Antonio</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Dediego</LastName><ForeName>Marta L</ForeName><Initials>ML</Initials></Author><Author ValidYN="Y"><LastName>Enjuanes</LastName><ForeName>Luis</ForeName><Initials>L</Initials></Author><Author ValidYN="Y"><LastName>Aguilella</LastName><ForeName>Vicente M</ForeName><Initials>VM</Initials></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>P01 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