Expression of SARS-coronavirus envelope protein in Escherichia coli cells alters membrane permeability.
Identifieur interne : 002A70 ( PubMed/Curation ); précédent : 002A69; suivant : 002A71Expression of SARS-coronavirus envelope protein in Escherichia coli cells alters membrane permeability.
Auteurs : Y. Liao [Singapour] ; J. Lescar ; J P Tam ; D X LiuSource :
- Biochemical and biophysical research communications [ 0006-291X ] ; 2004.
Descripteurs français
- KwdFr :
- Analyse de mutations d'ADN, Animaux, Cellules HeLa, Conformation des protéines, Cystéine (métabolisme), Escherichia coli (génétique), Escherichia coli (physiologie), Humains, Mutagenèse dirigée, Perméabilité de la membrane cellulaire, Protéines de l'enveloppe virale (), Protéines de l'enveloppe virale (génétique), Protéines de l'enveloppe virale (métabolisme), Virus du SRAS (métabolisme).
- MESH :
- génétique : Escherichia coli, Protéines de l'enveloppe virale.
- métabolisme : Cystéine, Protéines de l'enveloppe virale, Virus du SRAS.
- physiologie : Escherichia coli.
- Analyse de mutations d'ADN, Animaux, Cellules HeLa, Conformation des protéines, Humains, Mutagenèse dirigée, Perméabilité de la membrane cellulaire, Protéines de l'enveloppe virale.
English descriptors
- KwdEn :
- Animals, Cell Membrane Permeability, Cysteine (metabolism), DNA Mutational Analysis, Escherichia coli (genetics), Escherichia coli (physiology), HeLa Cells, Humans, Mutagenesis, Site-Directed, Protein Conformation, SARS Virus (metabolism), Viral Envelope Proteins (chemistry), Viral Envelope Proteins (genetics), Viral Envelope Proteins (metabolism).
- MESH :
- chemical , chemistry : Viral Envelope Proteins.
- chemical , genetics : Viral Envelope Proteins.
- chemical , metabolism : Cysteine, Viral Envelope Proteins.
- genetics : Escherichia coli.
- metabolism : SARS Virus.
- physiology : Escherichia coli.
- Animals, Cell Membrane Permeability, DNA Mutational Analysis, HeLa Cells, Humans, Mutagenesis, Site-Directed, Protein Conformation.
Abstract
To promote viral entry, replication, release, and spread to neighboring cells, many cytolytic animal viruses encode proteins responsible for modification of host cell membrane permeability and for formation of ion channels in host cell membranes during their life cycles. In this study, we show that the envelope (E) protein of severe acute respiratory syndrome-associated coronavirus can induce membrane permeability changes when expressed in Escherichia coli. E protein expressed in bacterial and mammalian cells under reducing conditions existed as monomers, but formed homodimer and homotrimer under non-reducing conditions. Site-directed mutagenesis studies revealed that two cysteine residues of the E protein were essential for oligomerization, leading to induction of membrane permeability. This is the first report demonstrating that a coronavirus-encoded protein could modify membrane permeability in E. coli cells.
DOI: 10.1016/j.bbrc.2004.10.050
PubMed: 15522242
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Lescar</name></author><author><name sortKey="Tam, J P" sort="Tam, J P" uniqKey="Tam J" first="J P" last="Tam">J P Tam</name></author><author><name sortKey="Liu, D X" sort="Liu, D X" uniqKey="Liu D" first="D X" last="Liu">D X Liu</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2004">2004</date><idno type="RBID">pubmed:15522242</idno><idno type="pmid">15522242</idno><idno type="doi">10.1016/j.bbrc.2004.10.050</idno><idno type="wicri:Area/PubMed/Corpus">002A70</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">002A70</idno><idno type="wicri:Area/PubMed/Curation">002A70</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">002A70</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Expression of SARS-coronavirus envelope protein in Escherichia coli cells alters membrane permeability.</title><author><name sortKey="Liao, Y" sort="Liao, Y" uniqKey="Liao Y" first="Y" last="Liao">Y. 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In this study, we show that the envelope (E) protein of severe acute respiratory syndrome-associated coronavirus can induce membrane permeability changes when expressed in Escherichia coli. E protein expressed in bacterial and mammalian cells under reducing conditions existed as monomers, but formed homodimer and homotrimer under non-reducing conditions. Site-directed mutagenesis studies revealed that two cysteine residues of the E protein were essential for oligomerization, leading to induction of membrane permeability. This is the first report demonstrating that a coronavirus-encoded protein could modify membrane permeability in E. coli cells.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">15522242</PMID><DateCompleted><Year>2005</Year><Month>01</Month><Day>25</Day></DateCompleted><DateRevised><Year>2020</Year><Month>04</Month><Day>04</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0006-291X</ISSN><JournalIssue CitedMedium="Print"><Volume>325</Volume><Issue>1</Issue><PubDate><Year>2004</Year><Month>Dec</Month><Day>03</Day></PubDate></JournalIssue><Title>Biochemical and biophysical research communications</Title><ISOAbbreviation>Biochem. Biophys. Res. Commun.</ISOAbbreviation></Journal><ArticleTitle>Expression of SARS-coronavirus envelope protein in Escherichia coli cells alters membrane permeability.</ArticleTitle><Pagination><MedlinePgn>374-80</MedlinePgn></Pagination><Abstract><AbstractText>To promote viral entry, replication, release, and spread to neighboring cells, many cytolytic animal viruses encode proteins responsible for modification of host cell membrane permeability and for formation of ion channels in host cell membranes during their life cycles. In this study, we show that the envelope (E) protein of severe acute respiratory syndrome-associated coronavirus can induce membrane permeability changes when expressed in Escherichia coli. E protein expressed in bacterial and mammalian cells under reducing conditions existed as monomers, but formed homodimer and homotrimer under non-reducing conditions. Site-directed mutagenesis studies revealed that two cysteine residues of the E protein were essential for oligomerization, leading to induction of membrane permeability. 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