Recognition of cellular receptors by bovine coronavirus.
Identifieur interne : 003531 ( PubMed/Curation ); précédent : 003530; suivant : 003532Recognition of cellular receptors by bovine coronavirus.
Auteurs : B. Schultze [Allemagne] ; G. HerrlerSource :
- Archives of virology. Supplementum [ 0939-1983 ] ; 1994.
Descripteurs français
- KwdFr :
- Acides sialiques (métabolisme), Coronavirus bovin (), Coronavirus bovin (métabolisme), Données de séquences moléculaires, Glycolipides (métabolisme), Glycoprotéine de spicule des coronavirus, Glycoprotéines (métabolisme), Glycoprotéines membranaires (), Glycoprotéines membranaires (métabolisme), Influenzavirus C, Liaison aux protéines, Protéines de l'enveloppe virale (métabolisme), Récepteurs viraux (), Récepteurs viraux (métabolisme), Séquence glucidique.
- MESH :
- métabolisme : Acides sialiques, Coronavirus bovin, Glycolipides, Glycoprotéines, Glycoprotéines membranaires, Protéines de l'enveloppe virale, Récepteurs viraux.
- Coronavirus bovin, Données de séquences moléculaires, Glycoprotéine de spicule des coronavirus, Glycoprotéines membranaires, Influenzavirus C, Liaison aux protéines, Récepteurs viraux, Séquence glucidique.
English descriptors
- KwdEn :
- Carbohydrate Sequence, Coronavirus, Bovine (chemistry), Coronavirus, Bovine (metabolism), Glycolipids (metabolism), Glycoproteins (metabolism), Influenzavirus C, Membrane Glycoproteins (chemistry), Membrane Glycoproteins (metabolism), Molecular Sequence Data, Protein Binding, Receptors, Virus (chemistry), Receptors, Virus (metabolism), Sialic Acids (metabolism), Spike Glycoprotein, Coronavirus, Viral Envelope Proteins (metabolism).
- MESH :
- chemical , chemistry : Membrane Glycoproteins, Receptors, Virus.
- chemical , metabolism : Glycolipids, Glycoproteins, Membrane Glycoproteins, Receptors, Virus, Sialic Acids, Viral Envelope Proteins.
- chemistry : Coronavirus, Bovine.
- metabolism : Coronavirus, Bovine.
- Carbohydrate Sequence, Influenzavirus C, Molecular Sequence Data, Protein Binding, Spike Glycoprotein, Coronavirus.
Abstract
Bovine coronavirus (BCV) initiates infection by attachment to cell surface receptors the crucial component of which is N-acetyl-9-O-acetylneuraminic acid. Inactivation of receptors by neuraminidase treatment and restoration of receptors by enzymatic resialylation of asialo-cells is described as a method to determine (i) the type of sialic acid that is recognized; (ii) the linkage specificity of the viral binding activity; (iii) the minimal amount of sialic acid required for virus attachment. Evidence is presented that both glycoproteins and glycolipids can serve as receptors for BCV provided they contain 9-O-acetylated sialic acid. A model is introduced proposing that after initial binding to sialic acid-containing receptors, the S-protein of BCV interacts with a specific protein receptor. This interaction may result in a conformational change that exposes a fusogenic domain and thus induces the fusion between the viral and the cellular membrane.
DOI: 10.1007/978-3-7091-9326-6_44
PubMed: 8032275
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pubmed:8032275Le document en format XML
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<wicri:regionArea>Institut für Virologie, Philipps-Universität Marburg</wicri:regionArea>
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<author><name sortKey="Herrler, G" sort="Herrler, G" uniqKey="Herrler G" first="G" last="Herrler">G. Herrler</name>
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<term>Coronavirus, Bovine (chemistry)</term>
<term>Coronavirus, Bovine (metabolism)</term>
<term>Glycolipids (metabolism)</term>
<term>Glycoproteins (metabolism)</term>
<term>Influenzavirus C</term>
<term>Membrane Glycoproteins (chemistry)</term>
<term>Membrane Glycoproteins (metabolism)</term>
<term>Molecular Sequence Data</term>
<term>Protein Binding</term>
<term>Receptors, Virus (chemistry)</term>
<term>Receptors, Virus (metabolism)</term>
<term>Sialic Acids (metabolism)</term>
<term>Spike Glycoprotein, Coronavirus</term>
<term>Viral Envelope Proteins (metabolism)</term>
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<keywords scheme="KwdFr" xml:lang="fr"><term>Acides sialiques (métabolisme)</term>
<term>Coronavirus bovin ()</term>
<term>Coronavirus bovin (métabolisme)</term>
<term>Données de séquences moléculaires</term>
<term>Glycolipides (métabolisme)</term>
<term>Glycoprotéine de spicule des coronavirus</term>
<term>Glycoprotéines (métabolisme)</term>
<term>Glycoprotéines membranaires ()</term>
<term>Glycoprotéines membranaires (métabolisme)</term>
<term>Influenzavirus C</term>
<term>Liaison aux protéines</term>
<term>Protéines de l'enveloppe virale (métabolisme)</term>
<term>Récepteurs viraux ()</term>
<term>Récepteurs viraux (métabolisme)</term>
<term>Séquence glucidique</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Membrane Glycoproteins</term>
<term>Receptors, Virus</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Glycolipids</term>
<term>Glycoproteins</term>
<term>Membrane Glycoproteins</term>
<term>Receptors, Virus</term>
<term>Sialic Acids</term>
<term>Viral Envelope Proteins</term>
</keywords>
<keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Coronavirus, Bovine</term>
</keywords>
<keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Coronavirus, Bovine</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Acides sialiques</term>
<term>Coronavirus bovin</term>
<term>Glycolipides</term>
<term>Glycoprotéines</term>
<term>Glycoprotéines membranaires</term>
<term>Protéines de l'enveloppe virale</term>
<term>Récepteurs viraux</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Carbohydrate Sequence</term>
<term>Influenzavirus C</term>
<term>Molecular Sequence Data</term>
<term>Protein Binding</term>
<term>Spike Glycoprotein, Coronavirus</term>
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<keywords scheme="MESH" xml:lang="fr"><term>Coronavirus bovin</term>
<term>Données de séquences moléculaires</term>
<term>Glycoprotéine de spicule des coronavirus</term>
<term>Glycoprotéines membranaires</term>
<term>Influenzavirus C</term>
<term>Liaison aux protéines</term>
<term>Récepteurs viraux</term>
<term>Séquence glucidique</term>
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<front><div type="abstract" xml:lang="en">Bovine coronavirus (BCV) initiates infection by attachment to cell surface receptors the crucial component of which is N-acetyl-9-O-acetylneuraminic acid. Inactivation of receptors by neuraminidase treatment and restoration of receptors by enzymatic resialylation of asialo-cells is described as a method to determine (i) the type of sialic acid that is recognized; (ii) the linkage specificity of the viral binding activity; (iii) the minimal amount of sialic acid required for virus attachment. Evidence is presented that both glycoproteins and glycolipids can serve as receptors for BCV provided they contain 9-O-acetylated sialic acid. A model is introduced proposing that after initial binding to sialic acid-containing receptors, the S-protein of BCV interacts with a specific protein receptor. This interaction may result in a conformational change that exposes a fusogenic domain and thus induces the fusion between the viral and the cellular membrane.</div>
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<Abstract><AbstractText>Bovine coronavirus (BCV) initiates infection by attachment to cell surface receptors the crucial component of which is N-acetyl-9-O-acetylneuraminic acid. Inactivation of receptors by neuraminidase treatment and restoration of receptors by enzymatic resialylation of asialo-cells is described as a method to determine (i) the type of sialic acid that is recognized; (ii) the linkage specificity of the viral binding activity; (iii) the minimal amount of sialic acid required for virus attachment. Evidence is presented that both glycoproteins and glycolipids can serve as receptors for BCV provided they contain 9-O-acetylated sialic acid. A model is introduced proposing that after initial binding to sialic acid-containing receptors, the S-protein of BCV interacts with a specific protein receptor. This interaction may result in a conformational change that exposes a fusogenic domain and thus induces the fusion between the viral and the cellular membrane.</AbstractText>
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