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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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. 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Suppl.</ISOAbbreviation></Journal><ArticleTitle>Recognition of cellular receptors by bovine coronavirus.</ArticleTitle><Pagination><MedlinePgn>451-9</MedlinePgn></Pagination><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></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Schultze</LastName><ForeName>B</ForeName><Initials>B</Initials><AffiliationInfo><Affiliation>Institut für Virologie, Philipps-Universität Marburg, Federal Republic of Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Herrler</LastName><ForeName>G</ForeName><Initials>G</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D003160">Comparative Study</PublicationType><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>Austria</Country><MedlineTA>Arch Virol 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