Identification of a receptor-binding domain of the spike glycoprotein of human coronavirus HCoV-229E.
Identifieur interne : 005F77 ( Main/Exploration ); précédent : 005F76; suivant : 005F78Identification of a receptor-binding domain of the spike glycoprotein of human coronavirus HCoV-229E.
Auteurs : Aurelio Bonavia [États-Unis] ; Bruce D. Zelus ; David E. Wentworth ; Pierre J. Talbot ; Kathryn V. HolmesSource :
- Journal of virology [ 0022-538X ] ; 2003.
Descripteurs français
- KwdFr :
- Aminopeptidases (métabolisme), Animaux, Baculoviridae (génétique), Cellules 3T3, Cellules cultivées, Coronavirus humain 229E (métabolisme), Glycoprotéine de spicule des coronavirus, Glycoprotéines membranaires (), Glycoprotéines membranaires (génétique), Glycoprotéines membranaires (isolement et purification), Glycoprotéines membranaires (métabolisme), Humains, Protéines de l'enveloppe virale (), Protéines de l'enveloppe virale (génétique), Protéines de l'enveloppe virale (isolement et purification), Protéines de l'enveloppe virale (métabolisme), Protéines recombinantes (génétique), Protéines recombinantes (métabolisme), Relation structure-activité, Récepteurs viraux (métabolisme), Sites de fixation, Souris, Spodoptera.
- MESH :
- génétique : Baculoviridae, Glycoprotéines membranaires, Protéines de l'enveloppe virale, Protéines recombinantes.
- isolement et purification : Glycoprotéines membranaires, Protéines de l'enveloppe virale.
- métabolisme : Aminopeptidases, Coronavirus humain 229E, Glycoprotéines membranaires, Protéines de l'enveloppe virale, Protéines recombinantes, Récepteurs viraux.
- Animaux, Cellules 3T3, Cellules cultivées, Glycoprotéine de spicule des coronavirus, Glycoprotéines membranaires, Humains, Protéines de l'enveloppe virale, Relation structure-activité, Sites de fixation, Souris, Spodoptera.
English descriptors
- KwdEn :
- 3T3 Cells, Aminopeptidases (metabolism), Animals, Baculoviridae (genetics), Binding Sites, Cells, Cultured, Coronavirus 229E, Human (metabolism), Humans, Membrane Glycoproteins (chemistry), Membrane Glycoproteins (genetics), Membrane Glycoproteins (isolation & purification), Membrane Glycoproteins (metabolism), Mice, Receptors, Virus (metabolism), Recombinant Proteins (genetics), Recombinant Proteins (metabolism), Spike Glycoprotein, Coronavirus, Spodoptera, Structure-Activity Relationship, Viral Envelope Proteins (chemistry), Viral Envelope Proteins (genetics), Viral Envelope Proteins (isolation & purification), Viral Envelope Proteins (metabolism).
- MESH :
- chemical , chemistry : Membrane Glycoproteins, Viral Envelope Proteins.
- chemical , genetics : Membrane Glycoproteins, Recombinant Proteins, Viral Envelope Proteins.
- chemical , isolation & purification : Membrane Glycoproteins, Viral Envelope Proteins.
- chemical , metabolism : Aminopeptidases, Membrane Glycoproteins, Receptors, Virus, Recombinant Proteins, Viral Envelope Proteins.
- genetics : Baculoviridae.
- metabolism : Coronavirus 229E, Human.
- 3T3 Cells, Animals, Binding Sites, Cells, Cultured, Humans, Mice, Spike Glycoprotein, Coronavirus, Spodoptera, Structure-Activity Relationship.
Abstract
Human coronavirus HCoV-229E uses human aminopeptidase N (hAPN) as its receptor (C. L. Yeager et al., Nature 357:420-422, 1992). To identify the receptor-binding domain of the viral spike glycoprotein (S), we expressed soluble truncated histidine-tagged S glycoproteins by using baculovirus expression vectors. Truncated S proteins purified by nickel affinity chromatography were shown to be glycosylated and to react with polyclonal anti-HCoV-229E antibodies and monoclonal antibodies to the viral S protein. A truncated protein (S(547)) that contains the N-terminal 547 amino acids bound to 3T3 mouse cells that express hAPN but not to mouse 3T3 cells transfected with empty vector. Binding of S(547) to hAPN was blocked by an anti-hAPN monoclonal antibody that inhibits binding of virus to hAPN and blocks virus infection of human cells and was also blocked by polyclonal anti-HCoV-229E antibody. S proteins that contain the N-terminal 268 or 417 amino acids did not bind to hAPN-3T3 cells. Antibody to the region from amino acid 417 to the C terminus of S blocked binding of S(547) to hAPN-3T3 cells. Thus, the data suggest that the domain of the spike protein between amino acids 417 and 547 is required for the binding of HCoV-229E to its hAPN receptor.
DOI: 10.1128/jvi.77.4.2530-2538.2003
PubMed: 12551991
Affiliations:
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Le document en format XML
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<term>Binding Sites</term>
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<term>Humans</term>
<term>Membrane Glycoproteins (chemistry)</term>
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<front><div type="abstract" xml:lang="en">Human coronavirus HCoV-229E uses human aminopeptidase N (hAPN) as its receptor (C. L. Yeager et al., Nature 357:420-422, 1992). To identify the receptor-binding domain of the viral spike glycoprotein (S), we expressed soluble truncated histidine-tagged S glycoproteins by using baculovirus expression vectors. Truncated S proteins purified by nickel affinity chromatography were shown to be glycosylated and to react with polyclonal anti-HCoV-229E antibodies and monoclonal antibodies to the viral S protein. A truncated protein (S(547)) that contains the N-terminal 547 amino acids bound to 3T3 mouse cells that express hAPN but not to mouse 3T3 cells transfected with empty vector. Binding of S(547) to hAPN was blocked by an anti-hAPN monoclonal antibody that inhibits binding of virus to hAPN and blocks virus infection of human cells and was also blocked by polyclonal anti-HCoV-229E antibody. S proteins that contain the N-terminal 268 or 417 amino acids did not bind to hAPN-3T3 cells. Antibody to the region from amino acid 417 to the C terminus of S blocked binding of S(547) to hAPN-3T3 cells. Thus, the data suggest that the domain of the spike protein between amino acids 417 and 547 is required for the binding of HCoV-229E to its hAPN receptor.</div>
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