SARS coronavirus E protein forms cation-selective ion channels.
Identifieur interne : 005132 ( Main/Exploration ); précédent : 005131; suivant : 005133SARS coronavirus E protein forms cation-selective ion channels.
Auteurs : Lauren Wilson [Australie] ; Carolyn Mckinlay ; Peter Gage ; Gary EwartSource :
- Virology [ 0042-6822 ] ; 2004.
Descripteurs français
- KwdFr :
- MESH :
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : Peptide Fragments, Viral Envelope Proteins.
- chemical , physiology : Ion Channels, Viral Envelope Proteins.
- physiology : SARS Virus.
- Amino Acid Sequence, Lipid Bilayers, Membrane Potentials, Molecular Sequence Data.
Abstract
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.
DOI: 10.1016/j.virol.2004.09.033
PubMed: 15527857
Affiliations:
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Le document en format XML
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<series><title level="j">Virology</title>
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<term>Membrane Potentials</term>
<term>Molecular Sequence Data</term>
<term>Peptide Fragments (chemistry)</term>
<term>SARS Virus (physiology)</term>
<term>Viral Envelope Proteins (chemistry)</term>
<term>Viral Envelope Proteins (physiology)</term>
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<keywords scheme="KwdFr" xml:lang="fr"><term>Canaux ioniques (physiologie)</term>
<term>Données de séquences moléculaires</term>
<term>Double couche lipidique</term>
<term>Fragments peptidiques ()</term>
<term>Potentiels de membrane</term>
<term>Protéines de l'enveloppe virale ()</term>
<term>Protéines de l'enveloppe virale (physiologie)</term>
<term>Séquence d'acides aminés</term>
<term>Virus du SRAS (physiologie)</term>
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<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Peptide Fragments</term>
<term>Viral Envelope Proteins</term>
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<keywords scheme="MESH" type="chemical" qualifier="physiology" xml:lang="en"><term>Ion Channels</term>
<term>Viral Envelope Proteins</term>
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<term>Protéines de l'enveloppe virale</term>
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<term>Fragments peptidiques</term>
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<term>Protéines de l'enveloppe virale</term>
<term>Séquence d'acides aminés</term>
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<front><div type="abstract" xml:lang="en">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.</div>
</front>
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<tree><noCountry><name sortKey="Ewart, Gary" sort="Ewart, Gary" uniqKey="Ewart G" first="Gary" last="Ewart">Gary Ewart</name>
<name sortKey="Gage, Peter" sort="Gage, Peter" uniqKey="Gage P" first="Peter" last="Gage">Peter Gage</name>
<name sortKey="Mckinlay, Carolyn" sort="Mckinlay, Carolyn" uniqKey="Mckinlay C" first="Carolyn" last="Mckinlay">Carolyn Mckinlay</name>
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<country name="Australie"><noRegion><name sortKey="Wilson, Lauren" sort="Wilson, Lauren" uniqKey="Wilson L" first="Lauren" last="Wilson">Lauren Wilson</name>
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