Characterization of severe acute respiratory syndrome coronavirus membrane protein.
Identifieur interne : 003F57 ( Main/Exploration ); précédent : 003F56; suivant : 003F58Characterization 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
Affiliations:
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Le document en format XML
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Elisabetta" uniqKey="Traggiai E" first="Elisabetta" last="Traggiai">Elisabetta Traggiai</name></author><author><name sortKey="Eickmann, Markus" sort="Eickmann, Markus" uniqKey="Eickmann M" first="Markus" last="Eickmann">Markus Eickmann</name></author><author><name sortKey="Stadler, Konrad" sort="Stadler, Konrad" uniqKey="Stadler K" first="Konrad" last="Stadler">Konrad Stadler</name></author><author><name sortKey="Lanzavecchia, Antonio" sort="Lanzavecchia, Antonio" uniqKey="Lanzavecchia A" first="Antonio" last="Lanzavecchia">Antonio Lanzavecchia</name></author><author><name sortKey="Becker, Stephan" sort="Becker, Stephan" uniqKey="Becker S" first="Stephan" last="Becker">Stephan Becker</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2006">2006</date><idno type="RBID">pubmed:16442106</idno><idno type="pmid">16442106</idno><idno type="doi">10.1016/j.febslet.2006.01.026</idno><idno type="wicri:Area/PubMed/Corpus">002364</idno><idno 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last="Eickmann">Markus Eickmann</name></author><author><name sortKey="Stadler, Konrad" sort="Stadler, Konrad" uniqKey="Stadler K" first="Konrad" last="Stadler">Konrad Stadler</name></author><author><name sortKey="Lanzavecchia, Antonio" sort="Lanzavecchia, Antonio" uniqKey="Lanzavecchia A" first="Antonio" last="Lanzavecchia">Antonio Lanzavecchia</name></author><author><name sortKey="Becker, Stephan" sort="Becker, Stephan" uniqKey="Becker S" first="Stephan" last="Becker">Stephan Becker</name></author></analytic><series><title level="j">FEBS letters</title><idno type="ISSN">0014-5793</idno><imprint><date when="2006" type="published">2006</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term><term>Cell Membrane (genetics)</term><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><term>Viral Matrix Proteins (genetics)</term><term>Viral Matrix Proteins (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux</term><term>Cellules Vero</term><term>Glycosylation</term><term>Humains</term><term>Mannosyl-glycoprotéine-endo-bêta-N-acétylgluco saminidase (génétique)</term><term>Mannosyl-glycoprotéine-endo-bêta-N-acétylgluco saminidase (métabolisme)</term><term>Maturation post-traductionnelle des protéines (physiologie)</term><term>Membrane cellulaire (génétique)</term><term>Membrane cellulaire (métabolisme)</term><term>Protéines de la matrice virale (génétique)</term><term>Protéines de la matrice virale (métabolisme)</term><term>Protéines membranaires (génétique)</term><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></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase</term><term>Membrane Proteins</term><term>Viral Matrix Proteins</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Cell Membrane</term><term>SARS Virus</term><term>Severe Acute Respiratory Syndrome</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Mannosyl-glycoprotéine-endo-bêta-N-acétylgluco saminidase</term><term>Membrane cellulaire</term><term>Protéines de la matrice virale</term><term>Protéines membranaires</term><term>Syndrome respiratoire aigu sévère</term><term>Virus du SRAS</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Cell Membrane</term><term>Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase</term><term>Membrane Proteins</term><term>SARS Virus</term><term>Severe Acute Respiratory Syndrome</term><term>Viral Matrix Proteins</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Mannosyl-glycoprotéine-endo-bêta-N-acétylgluco saminidase</term><term>Membrane cellulaire</term><term>Protéines de la matrice virale</term><term>Protéines membranaires</term><term>Syndrome respiratoire aigu sévère</term><term>Virus du SRAS</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Maturation post-traductionnelle des protéines</term><term>Transport de protéines</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Protein Processing, Post-Translational</term><term>Protein Transport</term></keywords><keywords scheme="MESH" qualifier="virologie" xml:lang="fr"><term>Syndrome respiratoire aigu sévère</term></keywords><keywords scheme="MESH" qualifier="virology" xml:lang="en"><term>Severe Acute Respiratory Syndrome</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Chlorocebus aethiops</term><term>Glycosylation</term><term>Humans</term><term>Vero Cells</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Cellules Vero</term><term>Glycosylation</term><term>Humains</term></keywords></textClass></profileDesc></teiHeader><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></front></TEI><affiliations><list><country><li>Allemagne</li></country><region><li>District de Giessen</li><li>Hesse (Land)</li></region><settlement><li>Marbourg</li></settlement></list><tree><noCountry><name sortKey="Becker, Stephan" sort="Becker, Stephan" uniqKey="Becker S" first="Stephan" last="Becker">Stephan Becker</name><name sortKey="Eickmann, Markus" sort="Eickmann, Markus" uniqKey="Eickmann M" first="Markus" last="Eickmann">Markus Eickmann</name><name sortKey="Kern, Anika" sort="Kern, Anika" uniqKey="Kern A" first="Anika" last="Kern">Anika Kern</name><name sortKey="Lanzavecchia, Antonio" sort="Lanzavecchia, Antonio" uniqKey="Lanzavecchia A" first="Antonio" last="Lanzavecchia">Antonio Lanzavecchia</name><name sortKey="Stadler, Konrad" sort="Stadler, Konrad" uniqKey="Stadler K" first="Konrad" last="Stadler">Konrad Stadler</name><name sortKey="Traggiai, Elisabetta" sort="Traggiai, Elisabetta" uniqKey="Traggiai E" first="Elisabetta" last="Traggiai">Elisabetta Traggiai</name></noCountry><country name="Allemagne"><region name="Hesse (Land)"><name sortKey="Voss, Daniel" sort="Voss, Daniel" uniqKey="Voss D" first="Daniel" last="Voss">Daniel Voss</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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