SARS-coronavirus spike S2 domain flanked by cysteine residues C822 and C833 is important for activation of membrane fusion
Identifieur interne : 002A24 ( Main/Exploration ); précédent : 002A23; suivant : 002A25SARS-coronavirus spike S2 domain flanked by cysteine residues C822 and C833 is important for activation of membrane fusion
Auteurs : Ikenna G. Madu ; Sandrine Belouzard ; Gary R. WhittakerSource :
- Virology [ 0042-6822 ] ; 2009.
Descripteurs français
- KwdFr :
- Animaux, Cricetinae, Cystéine (génétique), Données de séquences moléculaires, Fusion cellulaire, Fusion membranaire, Glycoprotéine de spicule des coronavirus, Glycoprotéines membranaires (génétique), Humains, Lignée cellulaire, Mutagenèse dirigée, Protéines de l'enveloppe virale (génétique), Séquence conservée, Séquence d'acides aminés, Virus du SRAS (génétique), Virus du SRAS (physiologie).
- MESH :
- génétique : Cystéine, Glycoprotéines membranaires, Protéines de l'enveloppe virale, Virus du SRAS.
- physiologie : Virus du SRAS.
- Animaux, Cricetinae, Données de séquences moléculaires, Fusion cellulaire, Fusion membranaire, Glycoprotéine de spicule des coronavirus, Humains, Lignée cellulaire, Mutagenèse dirigée, Séquence conservée, Séquence d'acides aminés.
English descriptors
- KwdEn :
- Amino Acid Sequence, Animals, Cell Fusion, Cell Line, Chlorocebus aethiops, Conserved Sequence, Cricetinae, Cysteine (genetics), Humans, Membrane Fusion, Membrane Glycoproteins (genetics), Molecular Sequence Data, Mutagenesis, Site-Directed, SARS Virus (genetics), SARS Virus (physiology), Spike Glycoprotein, Coronavirus, Viral Envelope Proteins (genetics).
- MESH :
- chemical , genetics : Cysteine, Membrane Glycoproteins, Viral Envelope Proteins.
- genetics : SARS Virus.
- physiology : SARS Virus.
- Amino Acid Sequence, Animals, Cell Fusion, Cell Line, Chlorocebus aethiops, Conserved Sequence, Cricetinae, Humans, Membrane Fusion, Molecular Sequence Data, Mutagenesis, Site-Directed, Spike Glycoprotein, Coronavirus.
Abstract
The S2 domain of the coronavirus spike (S) protein is known to be responsible for mediating membrane fusion. In addition to a well-recognized cleavage site at the S1–S2 boundary, a second proteolytic cleavage site has been identified in the severe acute respiratory syndrome coronavirus (SARS-CoV) S2 domain (R797). C-terminal to this S2 cleavage site is a conserved region flanked by cysteine residues C822 and C833. Here, we investigated the importance of this well conserved region for SARS-CoV S-mediated fusion activation. We show that the residues between C822–C833 are well conserved across all coronaviruses. Mutagenic analysis of SARS-CoV S, combined with cell–cell fusion and pseudotyped virion infectivity assays, showed a critical role for the core-conserved residues C822, D830, L831, and C833. Based on available predictive models, we propose that the conserved domain flanked by cysteines 822 and 833 forms a loop structure that interacts with components of the SARS-CoV S trimer to control the activation of membrane fusion.
Url:
DOI: 10.1016/j.virol.2009.07.038
PubMed: 19717178
PubMed Central: 3594805
Affiliations:
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Madu</name></author><author><name sortKey="Belouzard, Sandrine" sort="Belouzard, Sandrine" uniqKey="Belouzard S" first="Sandrine" last="Belouzard">Sandrine Belouzard</name></author><author><name sortKey="Whittaker, Gary R" sort="Whittaker, Gary R" uniqKey="Whittaker G" first="Gary R." last="Whittaker">Gary R. Whittaker</name></author></analytic><series><title level="j">Virology</title><idno type="ISSN">0042-6822</idno><idno type="eISSN">1096-0341</idno><imprint><date when="2009">2009</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence</term><term>Animals</term><term>Cell Fusion</term><term>Cell Line</term><term>Chlorocebus aethiops</term><term>Conserved Sequence</term><term>Cricetinae</term><term>Cysteine (genetics)</term><term>Humans</term><term>Membrane Fusion</term><term>Membrane Glycoproteins (genetics)</term><term>Molecular Sequence Data</term><term>Mutagenesis, Site-Directed</term><term>SARS Virus (genetics)</term><term>SARS Virus (physiology)</term><term>Spike Glycoprotein, Coronavirus</term><term>Viral Envelope Proteins (genetics)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux</term><term>Cricetinae</term><term>Cystéine (génétique)</term><term>Données de séquences moléculaires</term><term>Fusion cellulaire</term><term>Fusion membranaire</term><term>Glycoprotéine de spicule des coronavirus</term><term>Glycoprotéines membranaires (génétique)</term><term>Humains</term><term>Lignée cellulaire</term><term>Mutagenèse dirigée</term><term>Protéines de l'enveloppe virale (génétique)</term><term>Séquence conservée</term><term>Séquence d'acides aminés</term><term>Virus du SRAS (génétique)</term><term>Virus du SRAS (physiologie)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Cysteine</term><term>Membrane Glycoproteins</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Cystéine</term><term>Glycoprotéines membranaires</term><term>Protéines de l'enveloppe virale</term><term>Virus du SRAS</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Virus du SRAS</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Animals</term><term>Cell Fusion</term><term>Cell Line</term><term>Chlorocebus aethiops</term><term>Conserved Sequence</term><term>Cricetinae</term><term>Humans</term><term>Membrane Fusion</term><term>Molecular Sequence Data</term><term>Mutagenesis, Site-Directed</term><term>Spike Glycoprotein, Coronavirus</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Cricetinae</term><term>Données de séquences moléculaires</term><term>Fusion cellulaire</term><term>Fusion membranaire</term><term>Glycoprotéine de spicule des coronavirus</term><term>Humains</term><term>Lignée cellulaire</term><term>Mutagenèse dirigée</term><term>Séquence conservée</term><term>Séquence d'acides aminés</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p>The S2 domain of the coronavirus spike (S) protein is known to be responsible for mediating membrane fusion. In addition to a well-recognized cleavage site at the S1–S2 boundary, a second proteolytic cleavage site has been identified in the severe acute respiratory syndrome coronavirus (SARS-CoV) S2 domain (R797). C-terminal to this S2 cleavage site is a conserved region flanked by cysteine residues C822 and C833. Here, we investigated the importance of this well conserved region for SARS-CoV S-mediated fusion activation. We show that the residues between C822–C833 are well conserved across all coronaviruses. Mutagenic analysis of SARS-CoV S, combined with cell–cell fusion and pseudotyped virion infectivity assays, showed a critical role for the core-conserved residues C822, D830, L831, and C833. Based on available predictive models, we propose that the conserved domain flanked by cysteines 822 and 833 forms a loop structure that interacts with components of the SARS-CoV S trimer to control the activation of membrane fusion.</p></div></front><back><div1 type="bibliography"><listBibl><biblStruct><analytic><author><name sortKey="Bartosch, B" uniqKey="Bartosch B">B. Bartosch</name></author><author><name sortKey="Dubuisson, J" uniqKey="Dubuisson J">J. Dubuisson</name></author><author><name sortKey="Cosset, F L" uniqKey="Cosset F">F.L. Cosset</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Belouzard, S" uniqKey="Belouzard S">S. Belouzard</name></author><author><name sortKey="Chu, V C" uniqKey="Chu V">V.C. Chu</name></author><author><name sortKey="Whittaker, G R" uniqKey="Whittaker G">G.R. Whittaker</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Bergeron, E" uniqKey="Bergeron E">E. 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Deng</name></author></analytic></biblStruct></listBibl></div1></back></TEI><affiliations><list></list><tree><noCountry><name sortKey="Belouzard, Sandrine" sort="Belouzard, Sandrine" uniqKey="Belouzard S" first="Sandrine" last="Belouzard">Sandrine Belouzard</name><name sortKey="Madu, Ikenna G" sort="Madu, Ikenna G" uniqKey="Madu I" first="Ikenna G." last="Madu">Ikenna G. Madu</name><name sortKey="Whittaker, Gary R" sort="Whittaker, Gary R" uniqKey="Whittaker G" first="Gary R." last="Whittaker">Gary R. Whittaker</name></noCountry></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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