Complex formation between the spike protein and the membrane protein during mouse hepatitis virus assembly.
Identifieur interne : 003C20 ( Ncbi/Merge ); précédent : 003C19; suivant : 003C21Complex formation between the spike protein and the membrane protein during mouse hepatitis virus assembly.
Auteurs : D J Opstelten [Pays-Bas] ; M C Horzinek ; P J RottierSource :
- Advances in experimental medicine and biology [ 0065-2598 ] ; 1993.
Descripteurs français
- KwdFr :
- Animaux, Glycoprotéine de spicule des coronavirus, Glycoprotéines membranaires (métabolisme), Liaison aux protéines, Lignée cellulaire, Morphogenèse, Protéines de l'enveloppe virale (métabolisme), Protéines de la matrice virale (métabolisme), Virion (métabolisme), Virus de l'hépatite murine (métabolisme), Virus de l'hépatite murine (ultrastructure).
- MESH :
English descriptors
- KwdEn :
- MESH :
- chemical , metabolism : Membrane Glycoproteins, Viral Envelope Proteins, Viral Matrix Proteins.
- metabolism : Murine hepatitis virus, Virion.
- ultrastructure : Murine hepatitis virus.
- Animals, Cell Line, Morphogenesis, Protein Binding, Spike Glycoprotein, Coronavirus.
Abstract
Using different approaches we have demonstrated the formation of a complex between the S protein and the M protein in the process of mouse hepatitis virus (MHV) assembly. Preservation of the M/S heterocomplexes was critically dependent on the solubilization conditions. Pulse-chase labeling of MHV-infected cells followed by a co-immunoprecipitation assay revealed that newly synthesized S and M engage in complex formation with different kinetics, the S protein reacting much slower. Sedimentation experiments showed the M/S heteromultimer complexes to be very large. A model for the role of the complex formation in MHV assembly is presented.
DOI: 10.1007/978-1-4615-2996-5_30
PubMed: 8209729
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pubmed:8209729Le document en format XML
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<term>Murine hepatitis virus (metabolism)</term>
<term>Murine hepatitis virus (ultrastructure)</term>
<term>Protein Binding</term>
<term>Spike Glycoprotein, Coronavirus</term>
<term>Viral Envelope Proteins (metabolism)</term>
<term>Viral Matrix Proteins (metabolism)</term>
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<term>Glycoprotéines membranaires (métabolisme)</term>
<term>Liaison aux protéines</term>
<term>Lignée cellulaire</term>
<term>Morphogenèse</term>
<term>Protéines de l'enveloppe virale (métabolisme)</term>
<term>Protéines de la matrice virale (métabolisme)</term>
<term>Virion (métabolisme)</term>
<term>Virus de l'hépatite murine (métabolisme)</term>
<term>Virus de l'hépatite murine (ultrastructure)</term>
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<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Membrane Glycoproteins</term>
<term>Viral Envelope Proteins</term>
<term>Viral Matrix Proteins</term>
</keywords>
<keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Murine hepatitis virus</term>
<term>Virion</term>
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<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Glycoprotéines membranaires</term>
<term>Protéines de l'enveloppe virale</term>
<term>Protéines de la matrice virale</term>
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<term>Virus de l'hépatite murine</term>
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<term>Cell Line</term>
<term>Morphogenesis</term>
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<term>Glycoprotéine de spicule des coronavirus</term>
<term>Liaison aux protéines</term>
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<front><div type="abstract" xml:lang="en">Using different approaches we have demonstrated the formation of a complex between the S protein and the M protein in the process of mouse hepatitis virus (MHV) assembly. Preservation of the M/S heterocomplexes was critically dependent on the solubilization conditions. Pulse-chase labeling of MHV-infected cells followed by a co-immunoprecipitation assay revealed that newly synthesized S and M engage in complex formation with different kinetics, the S protein reacting much slower. Sedimentation experiments showed the M/S heteromultimer complexes to be very large. A model for the role of the complex formation in MHV assembly is presented.</div>
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<Abstract><AbstractText>Using different approaches we have demonstrated the formation of a complex between the S protein and the M protein in the process of mouse hepatitis virus (MHV) assembly. Preservation of the M/S heterocomplexes was critically dependent on the solubilization conditions. Pulse-chase labeling of MHV-infected cells followed by a co-immunoprecipitation assay revealed that newly synthesized S and M engage in complex formation with different kinetics, the S protein reacting much slower. Sedimentation experiments showed the M/S heteromultimer complexes to be very large. A model for the role of the complex formation in MHV assembly is presented.</AbstractText>
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