Biochemical evidence for the presence of mixed membrane topologies of the severe acute respiratory syndrome coronavirus envelope protein expressed in mammalian cells.
Identifieur interne : 003F65 ( Main/Curation ); précédent : 003F64; suivant : 003F66Biochemical evidence for the presence of mixed membrane topologies of the severe acute respiratory syndrome coronavirus envelope protein expressed in mammalian cells.
Auteurs : Q. Yuan [Singapour] ; Y. Liao ; J. Torres ; J P Tam ; D X LiuSource :
- FEBS letters [ 0014-5793 ] ; 2006.
Descripteurs français
- KwdFr :
- Cellules HeLa, Cytoplasme (), Cytoplasme (métabolisme), Données de séquences moléculaires, Glycosylation, Humains, Interactions hydrophobes et hydrophiles, Membrane cellulaire (), Membrane cellulaire (métabolisme), Perméabilité, Protéines de l'enveloppe virale (analyse), Protéines de l'enveloppe virale (génétique), Protéines de l'enveloppe virale (métabolisme), Protéines membranaires (analyse), Protéines membranaires (génétique), Protéines membranaires (métabolisme), Séquence d'acides aminés, Virus du SRAS (métabolisme).
- MESH :
- analyse : Protéines de l'enveloppe virale, Protéines membranaires.
- génétique : Protéines de l'enveloppe virale, Protéines membranaires.
- métabolisme : Cytoplasme, Membrane cellulaire, Protéines de l'enveloppe virale, Protéines membranaires, Virus du SRAS.
- Cellules HeLa, Cytoplasme, Données de séquences moléculaires, Glycosylation, Humains, Interactions hydrophobes et hydrophiles, Membrane cellulaire, Perméabilité, Séquence d'acides aminés.
English descriptors
- KwdEn :
- Amino Acid Sequence, Cell Membrane (chemistry), Cell Membrane (metabolism), Cytoplasm (chemistry), Cytoplasm (metabolism), Glycosylation, HeLa Cells, Humans, Hydrophobic and Hydrophilic Interactions, Membrane Proteins (analysis), Membrane Proteins (genetics), Membrane Proteins (metabolism), Molecular Sequence Data, Permeability, SARS Virus (metabolism), Viral Envelope Proteins (analysis), Viral Envelope Proteins (genetics), Viral Envelope Proteins (metabolism).
- MESH :
- chemical , analysis : Membrane Proteins, Viral Envelope Proteins.
- chemistry : Cell Membrane, Cytoplasm.
- chemical , genetics : Membrane Proteins, Viral Envelope Proteins.
- metabolism : Cell Membrane, Cytoplasm, Membrane Proteins, SARS Virus, Viral Envelope Proteins.
- Amino Acid Sequence, Glycosylation, HeLa Cells, Humans, Hydrophobic and Hydrophilic Interactions, Molecular Sequence Data, Permeability.
Abstract
Coronavirus envelope (E) protein is a small integral membrane protein with multi-functions in virion assembly, morphogenesis and virus-host interaction. Different coronavirus E proteins share striking similarities in biochemical properties and biological functions, but seem to adopt distinct membrane topology. In this report, we study the membrane topology of the SARS-CoV E protein by immunofluorescent staining of cells differentially permeabilized with detergents and proteinase K protection assay. It was revealed that both the N- and C-termini of the SARS-CoV E protein are exposed to the cytoplasmic side of the membranes (N(cyto)C(cyto)). In contrast, parallel experiments showed that the E protein from infectious bronchitis virus (IBV) spanned the membranes once, with the N-terminus exposed luminally and the C-terminus exposed cytoplasmically (N(exo(lum)-)C(cyto)). Intriguingly, a minor proportion of the SARS-CoV E protein was found to be modified by N-linked glycosylation on Asn 66 and inserted into the membranes once with the C-terminus exposed to the luminal side. The presence of two distinct membrane topologies of the SARS-CoV E protein may provide a useful clue to the pathogenesis of SARS-CoV.
DOI: 10.1016/j.febslet.2006.04.076
PubMed: 16684538
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Torres</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="2006">2006</date><idno type="RBID">pubmed:16684538</idno><idno type="pmid">16684538</idno><idno type="doi">10.1016/j.febslet.2006.04.076</idno><idno type="wicri:Area/PubMed/Corpus">002241</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">002241</idno><idno type="wicri:Area/PubMed/Curation">002241</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">002241</idno><idno type="wicri:Area/PubMed/Checkpoint">002273</idno><idno type="wicri:explorRef" wicri:stream="Checkpoint" wicri:step="PubMed">002273</idno><idno type="wicri:Area/Ncbi/Merge">001496</idno><idno type="wicri:Area/Ncbi/Curation">001496</idno><idno type="wicri:Area/Ncbi/Checkpoint">001496</idno><idno type="wicri:doubleKey">0014-5793:2006:Yuan Q:biochemical:evidence:for</idno><idno type="wicri:Area/Main/Merge">004174</idno><idno type="wicri:Area/Main/Curation">003F65</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Biochemical evidence for the presence of mixed membrane topologies of the severe acute respiratory syndrome coronavirus envelope protein expressed in mammalian cells.</title><author><name sortKey="Yuan, Q" sort="Yuan, Q" uniqKey="Yuan Q" first="Q" last="Yuan">Q. Yuan</name><affiliation wicri:level="1"><nlm:affiliation>School of Biological Science, Nanyang Technological University, 60 Nanyang Drive, Singapore 637551, Singapore.</nlm:affiliation><country xml:lang="fr">Singapour</country><wicri:regionArea>School of Biological Science, Nanyang Technological University, 60 Nanyang Drive, Singapore 637551</wicri:regionArea><wicri:noRegion>Singapore 637551</wicri:noRegion></affiliation></author><author><name sortKey="Liao, Y" sort="Liao, Y" uniqKey="Liao Y" first="Y" last="Liao">Y. Liao</name></author><author><name sortKey="Torres, J" sort="Torres, J" uniqKey="Torres J" first="J" last="Torres">J. 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Different coronavirus E proteins share striking similarities in biochemical properties and biological functions, but seem to adopt distinct membrane topology. In this report, we study the membrane topology of the SARS-CoV E protein by immunofluorescent staining of cells differentially permeabilized with detergents and proteinase K protection assay. It was revealed that both the N- and C-termini of the SARS-CoV E protein are exposed to the cytoplasmic side of the membranes (N(cyto)C(cyto)). In contrast, parallel experiments showed that the E protein from infectious bronchitis virus (IBV) spanned the membranes once, with the N-terminus exposed luminally and the C-terminus exposed cytoplasmically (N(exo(lum)-)C(cyto)). Intriguingly, a minor proportion of the SARS-CoV E protein was found to be modified by N-linked glycosylation on Asn 66 and inserted into the membranes once with the C-terminus exposed to the luminal side. The presence of two distinct membrane topologies of the SARS-CoV E protein may provide a useful clue to the pathogenesis of SARS-CoV.</div></front></TEI></record>Pour manipuler ce document sous Unix (Dilib)
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