Characterization of severe acute respiratory syndrome coronavirus membrane protein.
Identifieur interne : 001356 ( Ncbi/Curation ); précédent : 001355; suivant : 001357Characterization of severe acute respiratory syndrome coronavirus membrane protein.
Auteurs : Daniel Voss [Allemagne] ; Anika Kern ; Elisabetta Traggiai ; Markus Eickmann ; Konrad Stadler ; Antonio Lanzavecchia ; Stephan BeckerSource :
- FEBS letters [ 0014-5793 ] ; 2006.
Descripteurs français
- KwdFr :
- Animaux, Cellules Vero, Glycosylation, Humains, Mannosyl-glycoprotéine-endo-bêta-N-acétylgluco saminidase (génétique), Mannosyl-glycoprotéine-endo-bêta-N-acétylgluco saminidase (métabolisme), Maturation post-traductionnelle des protéines (physiologie), Membrane cellulaire (génétique), Membrane cellulaire (métabolisme), Protéines de la matrice virale (génétique), Protéines de la matrice virale (métabolisme), Protéines membranaires (génétique), Protéines membranaires (métabolisme), Syndrome respiratoire aigu sévère (génétique), Syndrome respiratoire aigu sévère (métabolisme), Syndrome respiratoire aigu sévère (virologie), Transport de protéines (physiologie), Virus du SRAS (génétique), Virus du SRAS (métabolisme).
- MESH :
- génétique : Mannosyl-glycoprotéine-endo-bêta-N-acétylgluco saminidase, Membrane cellulaire, Protéines de la matrice virale, Protéines membranaires, Syndrome respiratoire aigu sévère, Virus du SRAS.
- métabolisme : Mannosyl-glycoprotéine-endo-bêta-N-acétylgluco saminidase, Membrane cellulaire, Protéines de la matrice virale, Protéines membranaires, Syndrome respiratoire aigu sévère, Virus du SRAS.
- physiologie : Maturation post-traductionnelle des protéines, Transport de protéines.
- virologie : Syndrome respiratoire aigu sévère.
- Animaux, Cellules Vero, Glycosylation, Humains.
English descriptors
- KwdEn :
- Animals, Cell Membrane (genetics), Cell Membrane (metabolism), Chlorocebus aethiops, Glycosylation, Humans, Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase (genetics), Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase (metabolism), Membrane Proteins (genetics), Membrane Proteins (metabolism), Protein Processing, Post-Translational (physiology), Protein Transport (physiology), SARS Virus (genetics), SARS Virus (metabolism), Severe Acute Respiratory Syndrome (genetics), Severe Acute Respiratory Syndrome (metabolism), Severe Acute Respiratory Syndrome (virology), Vero Cells, Viral Matrix Proteins (genetics), Viral Matrix Proteins (metabolism).
- MESH :
- chemical , genetics : Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase, Membrane Proteins, Viral Matrix Proteins.
- genetics : Cell Membrane, SARS Virus, Severe Acute Respiratory Syndrome.
- metabolism : Cell Membrane, Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase, Membrane Proteins, SARS Virus, Severe Acute Respiratory Syndrome, Viral Matrix Proteins.
- physiology : Protein Processing, Post-Translational, Protein Transport.
- virology : Severe Acute Respiratory Syndrome.
- Animals, Chlorocebus aethiops, Glycosylation, Humans, Vero Cells.
Abstract
The coronavirus membrane protein (M) is the key player in the assembly of virions at intracellular membranes between endoplasmic-reticulum and Golgi-complex. Using a newly established human monoclonal anti-M antibody we detected glycosylated and nonglycosylated membrane-associated M in severe acute respiratory syndrome-associated coronavirus (SARS-CoV) infected cells and in purified virions. Further analyses revealed that M contained a single N-glycosylation site at asparagine 4. Recombinant M was transported to the plasma membrane and gained complex-type N-glycosylation. In SARS-CoV infected cells and in purified virions, however, N-glycosylation of M remained endoglycosidase H-sensitive suggesting that trimming of the N-linked sugar side chain is inhibited.
DOI: 10.1016/j.febslet.2006.01.026
PubMed: 16442106
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pubmed:16442106Le document en format XML
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<term>Cell Membrane (metabolism)</term>
<term>Chlorocebus aethiops</term>
<term>Glycosylation</term>
<term>Humans</term>
<term>Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase (genetics)</term>
<term>Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase (metabolism)</term>
<term>Membrane Proteins (genetics)</term>
<term>Membrane Proteins (metabolism)</term>
<term>Protein Processing, Post-Translational (physiology)</term>
<term>Protein Transport (physiology)</term>
<term>SARS Virus (genetics)</term>
<term>SARS Virus (metabolism)</term>
<term>Severe Acute Respiratory Syndrome (genetics)</term>
<term>Severe Acute Respiratory Syndrome (metabolism)</term>
<term>Severe Acute Respiratory Syndrome (virology)</term>
<term>Vero Cells</term>
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<term>Viral Matrix Proteins (metabolism)</term>
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<term>Mannosyl-glycoprotéine-endo-bêta-N-acétylgluco saminidase (métabolisme)</term>
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<term>Protéines membranaires (métabolisme)</term>
<term>Syndrome respiratoire aigu sévère (génétique)</term>
<term>Syndrome respiratoire aigu sévère (métabolisme)</term>
<term>Syndrome respiratoire aigu sévère (virologie)</term>
<term>Transport de protéines (physiologie)</term>
<term>Virus du SRAS (génétique)</term>
<term>Virus du SRAS (métabolisme)</term>
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<term>Viral Matrix Proteins</term>
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<term>Protéines de la matrice virale</term>
<term>Protéines membranaires</term>
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<term>Membrane Proteins</term>
<term>SARS Virus</term>
<term>Severe Acute Respiratory Syndrome</term>
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<term>Protéines de la matrice virale</term>
<term>Protéines membranaires</term>
<term>Syndrome respiratoire aigu sévère</term>
<term>Virus du SRAS</term>
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<term>Transport de protéines</term>
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<term>Protein Transport</term>
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<term>Chlorocebus aethiops</term>
<term>Glycosylation</term>
<term>Humans</term>
<term>Vero Cells</term>
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<front><div type="abstract" xml:lang="en">The coronavirus membrane protein (M) is the key player in the assembly of virions at intracellular membranes between endoplasmic-reticulum and Golgi-complex. Using a newly established human monoclonal anti-M antibody we detected glycosylated and nonglycosylated membrane-associated M in severe acute respiratory syndrome-associated coronavirus (SARS-CoV) infected cells and in purified virions. Further analyses revealed that M contained a single N-glycosylation site at asparagine 4. Recombinant M was transported to the plasma membrane and gained complex-type N-glycosylation. In SARS-CoV infected cells and in purified virions, however, N-glycosylation of M remained endoglycosidase H-sensitive suggesting that trimming of the N-linked sugar side chain is inhibited.</div>
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