Cooperative involvement of the S1 and S2 subunits of the murine coronavirus spike protein in receptor binding and extended host range.
Identifieur interne : 003F41 ( Main/Exploration ); précédent : 003F40; suivant : 003F42Cooperative involvement of the S1 and S2 subunits of the murine coronavirus spike protein in receptor binding and extended host range.
Auteurs : Cornelis A M. De Haan [Pays-Bas] ; Eddie Te Lintelo ; Zhen Li ; Matthijs Raaben ; Tom Wurdinger ; Berend Jan Bosch ; Peter J M. RottierSource :
- Journal of virology [ 0022-538X ] ; 2006.
Descripteurs français
- KwdFr :
- Animaux, Antigène carcinoembryonnaire (métabolisme), Attachement viral, Chats, Glycoprotéine de spicule des coronavirus, Glycoprotéines membranaires (génétique), Glycoprotéines membranaires (métabolisme), Gènes rapporteurs, Humains, Héparitine sulfate, Liaison aux protéines, Lignée cellulaire, Luciferases (analyse), Luciferases (génétique), Mutation faux-sens, Protéines de l'enveloppe virale (génétique), Protéines de l'enveloppe virale (métabolisme), Récepteurs viraux (métabolisme), Souris, Substitution d'acide aminé, Virus de l'hépatite murine (génétique), Virus de l'hépatite murine (physiologie).
- MESH :
- analyse : Luciferases.
- génétique : Glycoprotéines membranaires, Luciferases, Protéines de l'enveloppe virale, Virus de l'hépatite murine.
- métabolisme : Antigène carcinoembryonnaire, Glycoprotéines membranaires, Protéines de l'enveloppe virale, Récepteurs viraux.
- physiologie : Virus de l'hépatite murine.
- Animaux, Attachement viral, Chats, Glycoprotéine de spicule des coronavirus, Gènes rapporteurs, Humains, Héparitine sulfate, Liaison aux protéines, Lignée cellulaire, Mutation faux-sens, Souris, Substitution d'acide aminé.
English descriptors
- KwdEn :
- Amino Acid Substitution, Animals, Carcinoembryonic Antigen (metabolism), Cats, Cell Line, Genes, Reporter, Heparitin Sulfate, Humans, Luciferases (analysis), Luciferases (genetics), Membrane Glycoproteins (genetics), Membrane Glycoproteins (metabolism), Mice, Murine hepatitis virus (genetics), Murine hepatitis virus (physiology), Mutation, Missense, Protein Binding, Receptors, Virus (metabolism), Spike Glycoprotein, Coronavirus, Viral Envelope Proteins (genetics), Viral Envelope Proteins (metabolism), Virus Attachment.
- MESH :
- chemical , analysis : Luciferases.
- chemical , genetics : Luciferases, Membrane Glycoproteins, Viral Envelope Proteins.
- chemical , metabolism : Carcinoembryonic Antigen, Membrane Glycoproteins, Receptors, Virus, Viral Envelope Proteins.
- genetics : Murine hepatitis virus.
- physiology : Murine hepatitis virus.
- Amino Acid Substitution, Animals, Cats, Cell Line, Genes, Reporter, Heparitin Sulfate, Humans, Mice, Mutation, Missense, Protein Binding, Spike Glycoprotein, Coronavirus, Virus Attachment.
Abstract
To study the process of spike (S)-receptor interaction during coronavirus entry, we evaluated the contributions of mutations in different regions of the murine hepatitis virus (MHV) S protein to natural receptor murine carcinoembryonic antigen-related cell adhesion molecule 1a (CEACAM1a) dependence and to the acquisition of extended host range. Extended-host-range variants of MHV strain A59 were previously obtained from persistently infected cells (J. H. Schickli, B. D. Zelus, D. E. Wentworth, S. G. Sawicki, and K. V. Holmes, J. Virol. 71:9499-9504, 1997). These variant viruses contain several mutations in the S protein that confer to the viruses the ability to enter cells in a heparan sulfate-dependent manner (C. A. de Haan, Z. Li, E. te Lintelo, B. J. Bosch, B. J. Haijema, and P. J. M. Rottier, J. Virol. 79:14451-14456, 2005). While the parental MHV-A59 is fully dependent on murine CEACAM1a for its entry, viruses carrying the variant mutations in the amino-terminal part of their S protein had become dependent on both CEACAM1a and heparan sulfate. Substitutions in a restricted, downstream part of the S protein encompassing heptad repeat region 1 (HR1) and putative fusion peptide (FP) did not alter the CEACAM1a dependence. However, when the mutations in both parts of the S protein were combined, the resulting viruses became independent of CEACAM1a and acquired the extended host range. In addition, these viruses showed a decreased binding to and inhibition by soluble CEACAM1a. The observations suggest that the amino-terminal region of the S protein, including the receptor-binding domain, and a region in the central part of the S protein containing HR1 and FP, i.e., regions far apart in the linear sequence, communicate and may even interact physically in the higher-order structure of the spike.
DOI: 10.1128/JVI.00950-06
PubMed: 16956938
Affiliations:
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Le document en format XML
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De Haan</name><affiliation wicri:level="1"><nlm:affiliation>Virology Division, Department of Infectious Diseases and Immunology, Yalelaan 1, 3584 CL Utrecht, The Netherlands. c.a.m.dehaan@vet.uu.nl</nlm:affiliation><country xml:lang="fr">Pays-Bas</country><wicri:regionArea>Virology Division, Department of Infectious Diseases and Immunology, Yalelaan 1, 3584 CL Utrecht</wicri:regionArea><wicri:noRegion>3584 CL Utrecht</wicri:noRegion></affiliation></author><author><name sortKey="Te Lintelo, Eddie" sort="Te Lintelo, Eddie" uniqKey="Te Lintelo E" first="Eddie" last="Te Lintelo">Eddie Te Lintelo</name></author><author><name sortKey="Li, Zhen" sort="Li, Zhen" uniqKey="Li Z" first="Zhen" last="Li">Zhen Li</name></author><author><name sortKey="Raaben, Matthijs" sort="Raaben, Matthijs" uniqKey="Raaben M" first="Matthijs" last="Raaben">Matthijs Raaben</name></author><author><name sortKey="Wurdinger, Tom" sort="Wurdinger, Tom" uniqKey="Wurdinger T" first="Tom" last="Wurdinger">Tom Wurdinger</name></author><author><name sortKey="Bosch, Berend Jan" sort="Bosch, Berend Jan" uniqKey="Bosch B" first="Berend Jan" last="Bosch">Berend Jan Bosch</name></author><author><name sortKey="Rottier, Peter J M" sort="Rottier, Peter J M" uniqKey="Rottier P" first="Peter J M" last="Rottier">Peter J M. 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De Haan</name><affiliation wicri:level="1"><nlm:affiliation>Virology Division, Department of Infectious Diseases and Immunology, Yalelaan 1, 3584 CL Utrecht, The Netherlands. c.a.m.dehaan@vet.uu.nl</nlm:affiliation><country xml:lang="fr">Pays-Bas</country><wicri:regionArea>Virology Division, Department of Infectious Diseases and Immunology, Yalelaan 1, 3584 CL Utrecht</wicri:regionArea><wicri:noRegion>3584 CL Utrecht</wicri:noRegion></affiliation></author><author><name sortKey="Te Lintelo, Eddie" sort="Te Lintelo, Eddie" uniqKey="Te Lintelo E" first="Eddie" last="Te Lintelo">Eddie Te Lintelo</name></author><author><name sortKey="Li, Zhen" sort="Li, Zhen" uniqKey="Li Z" first="Zhen" last="Li">Zhen Li</name></author><author><name sortKey="Raaben, Matthijs" sort="Raaben, Matthijs" uniqKey="Raaben M" first="Matthijs" last="Raaben">Matthijs Raaben</name></author><author><name sortKey="Wurdinger, Tom" sort="Wurdinger, Tom" uniqKey="Wurdinger T" first="Tom" last="Wurdinger">Tom Wurdinger</name></author><author><name sortKey="Bosch, Berend Jan" sort="Bosch, Berend Jan" uniqKey="Bosch B" first="Berend Jan" last="Bosch">Berend Jan Bosch</name></author><author><name sortKey="Rottier, Peter J M" sort="Rottier, Peter J M" uniqKey="Rottier P" first="Peter J M" last="Rottier">Peter J M. Rottier</name></author></analytic><series><title level="j">Journal of virology</title><idno type="ISSN">0022-538X</idno><imprint><date when="2006" type="published">2006</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Substitution</term><term>Animals</term><term>Carcinoembryonic Antigen (metabolism)</term><term>Cats</term><term>Cell Line</term><term>Genes, Reporter</term><term>Heparitin Sulfate</term><term>Humans</term><term>Luciferases (analysis)</term><term>Luciferases (genetics)</term><term>Membrane Glycoproteins (genetics)</term><term>Membrane Glycoproteins (metabolism)</term><term>Mice</term><term>Murine hepatitis virus (genetics)</term><term>Murine hepatitis virus (physiology)</term><term>Mutation, Missense</term><term>Protein Binding</term><term>Receptors, Virus (metabolism)</term><term>Spike Glycoprotein, Coronavirus</term><term>Viral Envelope Proteins (genetics)</term><term>Viral Envelope Proteins (metabolism)</term><term>Virus Attachment</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux</term><term>Antigène carcinoembryonnaire (métabolisme)</term><term>Attachement viral</term><term>Chats</term><term>Glycoprotéine de spicule des coronavirus</term><term>Glycoprotéines membranaires (génétique)</term><term>Glycoprotéines membranaires (métabolisme)</term><term>Gènes rapporteurs</term><term>Humains</term><term>Héparitine sulfate</term><term>Liaison aux protéines</term><term>Lignée cellulaire</term><term>Luciferases (analyse)</term><term>Luciferases (génétique)</term><term>Mutation faux-sens</term><term>Protéines de l'enveloppe virale (génétique)</term><term>Protéines de l'enveloppe virale (métabolisme)</term><term>Récepteurs viraux (métabolisme)</term><term>Souris</term><term>Substitution d'acide aminé</term><term>Virus de l'hépatite murine (génétique)</term><term>Virus de l'hépatite murine (physiologie)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="analysis" xml:lang="en"><term>Luciferases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Luciferases</term><term>Membrane Glycoproteins</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Carcinoembryonic Antigen</term><term>Membrane Glycoproteins</term><term>Receptors, Virus</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" qualifier="analyse" xml:lang="fr"><term>Luciferases</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Murine hepatitis virus</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Glycoprotéines membranaires</term><term>Luciferases</term><term>Protéines de l'enveloppe virale</term><term>Virus de l'hépatite murine</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Antigène carcinoembryonnaire</term><term>Glycoprotéines membranaires</term><term>Protéines de l'enveloppe virale</term><term>Récepteurs viraux</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Virus de l'hépatite murine</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Murine hepatitis virus</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Substitution</term><term>Animals</term><term>Cats</term><term>Cell Line</term><term>Genes, Reporter</term><term>Heparitin Sulfate</term><term>Humans</term><term>Mice</term><term>Mutation, Missense</term><term>Protein Binding</term><term>Spike Glycoprotein, Coronavirus</term><term>Virus Attachment</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Attachement viral</term><term>Chats</term><term>Glycoprotéine de spicule des coronavirus</term><term>Gènes rapporteurs</term><term>Humains</term><term>Héparitine sulfate</term><term>Liaison aux protéines</term><term>Lignée cellulaire</term><term>Mutation faux-sens</term><term>Souris</term><term>Substitution d'acide aminé</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">To study the process of spike (S)-receptor interaction during coronavirus entry, we evaluated the contributions of mutations in different regions of the murine hepatitis virus (MHV) S protein to natural receptor murine carcinoembryonic antigen-related cell adhesion molecule 1a (CEACAM1a) dependence and to the acquisition of extended host range. Extended-host-range variants of MHV strain A59 were previously obtained from persistently infected cells (J. H. Schickli, B. D. Zelus, D. E. Wentworth, S. G. Sawicki, and K. V. Holmes, J. Virol. 71:9499-9504, 1997). These variant viruses contain several mutations in the S protein that confer to the viruses the ability to enter cells in a heparan sulfate-dependent manner (C. A. de Haan, Z. Li, E. te Lintelo, B. J. Bosch, B. J. Haijema, and P. J. M. Rottier, J. Virol. 79:14451-14456, 2005). While the parental MHV-A59 is fully dependent on murine CEACAM1a for its entry, viruses carrying the variant mutations in the amino-terminal part of their S protein had become dependent on both CEACAM1a and heparan sulfate. Substitutions in a restricted, downstream part of the S protein encompassing heptad repeat region 1 (HR1) and putative fusion peptide (FP) did not alter the CEACAM1a dependence. However, when the mutations in both parts of the S protein were combined, the resulting viruses became independent of CEACAM1a and acquired the extended host range. In addition, these viruses showed a decreased binding to and inhibition by soluble CEACAM1a. The observations suggest that the amino-terminal region of the S protein, including the receptor-binding domain, and a region in the central part of the S protein containing HR1 and FP, i.e., regions far apart in the linear sequence, communicate and may even interact physically in the higher-order structure of the spike.</div></front></TEI><affiliations><list><country><li>Pays-Bas</li></country></list><tree><noCountry><name sortKey="Bosch, Berend Jan" sort="Bosch, Berend Jan" uniqKey="Bosch B" first="Berend Jan" last="Bosch">Berend Jan Bosch</name><name sortKey="Li, Zhen" sort="Li, Zhen" uniqKey="Li Z" first="Zhen" last="Li">Zhen Li</name><name sortKey="Raaben, Matthijs" sort="Raaben, Matthijs" uniqKey="Raaben M" first="Matthijs" last="Raaben">Matthijs Raaben</name><name sortKey="Rottier, Peter J M" sort="Rottier, Peter J M" uniqKey="Rottier P" first="Peter J M" last="Rottier">Peter J M. Rottier</name><name sortKey="Te Lintelo, Eddie" sort="Te Lintelo, Eddie" uniqKey="Te Lintelo E" first="Eddie" last="Te Lintelo">Eddie Te Lintelo</name><name sortKey="Wurdinger, Tom" sort="Wurdinger, Tom" uniqKey="Wurdinger T" first="Tom" last="Wurdinger">Tom Wurdinger</name></noCountry><country name="Pays-Bas"><noRegion><name sortKey="De Haan, Cornelis A M" sort="De Haan, Cornelis A M" uniqKey="De Haan C" first="Cornelis A M" last="De Haan">Cornelis A M. De Haan</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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