Biochemical evidence for the presence of mixed membrane topologies of the severe acute respiratory syndrome coronavirus envelope protein expressed in mammalian cells
Identifieur interne : 000792 ( new/Analysis ); précédent : 000791; suivant : 000793Biochemical 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 [Singapour] ; J. Torres [Singapour] ; J. P. Tam [Singapour] ; D. X. Liu [Singapour]Source :
- Febs Letters [ 0014-5793 ] ; 2006.
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 (NcytoCcyto). 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 (Nexo(lum)Ccyto). 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.
Url:
DOI: 10.1016/j.febslet.2006.04.076
PubMed: 16684538
PubMed Central: 7094218
Affiliations:
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PMC:7094218Le document en format XML
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Yuan</name><affiliation wicri:level="1"><nlm:aff id="aff1">School of Biological Science, Nanyang Technological University, 60 Nanyang Drive, Singapore 637551, Singapore</nlm:aff><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><affiliation wicri:level="1"><nlm:aff id="aff1">School of Biological Science, Nanyang Technological University, 60 Nanyang Drive, Singapore 637551, Singapore</nlm:aff><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="Torres, J" sort="Torres, J" uniqKey="Torres J" first="J." last="Torres">J. Torres</name><affiliation wicri:level="1"><nlm:aff id="aff1">School of Biological Science, Nanyang Technological University, 60 Nanyang Drive, Singapore 637551, Singapore</nlm:aff><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="Tam, J P" sort="Tam, J P" uniqKey="Tam J" first="J. P." last="Tam">J. P. Tam</name><affiliation wicri:level="1"><nlm:aff id="aff1">School of Biological Science, Nanyang Technological University, 60 Nanyang Drive, Singapore 637551, Singapore</nlm:aff><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="Liu, D X" sort="Liu, D X" uniqKey="Liu D" first="D. X." last="Liu">D. X. Liu</name><affiliation wicri:level="1"><nlm:aff id="aff1">School of Biological Science, Nanyang Technological University, 60 Nanyang Drive, Singapore 637551, Singapore</nlm:aff><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><affiliation wicri:level="1"><nlm:aff id="aff2">Institute of Molecular and Cell Biology, 61 Biopolis Drive, Proteos, Singapore 138673, Singapore</nlm:aff><country xml:lang="fr">Singapour</country><wicri:regionArea>Institute of Molecular and Cell Biology, 61 Biopolis Drive, Proteos, Singapore 138673</wicri:regionArea><wicri:noRegion>Singapore 138673</wicri:noRegion></affiliation></author></analytic><series><title level="j">Febs Letters</title><idno type="ISSN">0014-5793</idno><idno type="eISSN">1873-3468</idno><imprint><date when="2006">2006</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p>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<sub>cyto</sub>C<sub>cyto</sub>). 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<sub>exo(lum)</sub>C<sub>cyto</sub>). 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.</p></div></front><back><div1 type="bibliography"><listBibl><biblStruct><analytic><author><name sortKey="An, S" uniqKey="An S">S. An</name></author><author><name sortKey="Chen, C J" uniqKey="Chen C">C.J. Chen</name></author><author><name sortKey="Yu, X" uniqKey="Yu X">X. Yu</name></author><author><name sortKey="Leibowitz, J L" uniqKey="Leibowitz J">J.L. Leibowitz</name></author><author><name sortKey="Makino, S" uniqKey="Makino S">S. Makino</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Arbely, E" uniqKey="Arbely E">E. Arbely</name></author><author><name sortKey="Khattari, Z" uniqKey="Khattari Z">Z. Khattari</name></author><author><name sortKey="Brotons, G" uniqKey="Brotons G">G. Brotons</name></author><author><name sortKey="Akkawi, M" uniqKey="Akkawi M">M. 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Wang</name></author><author><name sortKey="Yang, X F" uniqKey="Yang X">X.F. Yang</name></author></analytic></biblStruct></listBibl></div1></back></TEI><affiliations><list><country><li>Singapour</li></country></list><tree><country name="Singapour"><noRegion><name sortKey="Yuan, Q" sort="Yuan, Q" uniqKey="Yuan Q" first="Q." last="Yuan">Q. Yuan</name></noRegion><name sortKey="Liao, Y" sort="Liao, Y" uniqKey="Liao Y" first="Y." last="Liao">Y. Liao</name><name sortKey="Liu, D X" sort="Liu, D X" uniqKey="Liu D" first="D. X." last="Liu">D. X. Liu</name><name sortKey="Liu, D X" sort="Liu, D X" uniqKey="Liu D" first="D. X." last="Liu">D. X. Liu</name><name sortKey="Tam, J P" sort="Tam, J P" uniqKey="Tam J" first="J. P." last="Tam">J. P. Tam</name><name sortKey="Torres, J" sort="Torres, J" uniqKey="Torres J" first="J." last="Torres">J. Torres</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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