Studies on membrane topology, N-glycosylation and functionality of SARS-CoV membrane protein.
Identifieur interne : 002A07 ( Main/Exploration ); précédent : 002A06; suivant : 002A08Studies on membrane topology, N-glycosylation and functionality of SARS-CoV membrane protein.
Auteurs : Daniel Voss [Allemagne] ; Susanne Pfefferle ; Christian Drosten ; Lea Stevermann ; Elisabetta Traggiai ; Antonio Lanzavecchia ; Stephan BeckerSource :
- Virology journal [ 1743-422X ] ; 2009.
Descripteurs français
- KwdFr :
- Animaux, Appareil de Golgi (virologie), Délétion de séquence, Glycoprotéine de spicule des coronavirus, Glycoprotéines membranaires (métabolisme), Glycosylation, Humains, Lignée cellulaire, Mutagenèse dirigée, Protéines de l'enveloppe virale (métabolisme), Protéines de la matrice virale (génétique), Protéines de la matrice virale (métabolisme), Pénétration virale, Réplication virale, Substitution d'acide aminé, Virus du SRAS (), Virus du SRAS (physiologie).
- MESH :
- génétique : Protéines de la matrice virale.
- métabolisme : Glycoprotéines membranaires, Protéines de l'enveloppe virale, Protéines de la matrice virale.
- physiologie : Virus du SRAS.
- virologie : Appareil de Golgi.
- Animaux, Délétion de séquence, Glycoprotéine de spicule des coronavirus, Glycosylation, Humains, Lignée cellulaire, Mutagenèse dirigée, Pénétration virale, Réplication virale, Substitution d'acide aminé, Virus du SRAS.
English descriptors
- KwdEn :
- Amino Acid Substitution, Animals, Cell Line, Chlorocebus aethiops, Glycosylation, Golgi Apparatus (virology), Humans, Membrane Glycoproteins (metabolism), Mutagenesis, Site-Directed, SARS Virus (chemistry), SARS Virus (physiology), Sequence Deletion, Spike Glycoprotein, Coronavirus, Viral Envelope Proteins (metabolism), Viral Matrix Proteins (genetics), Viral Matrix Proteins (metabolism), Virus Internalization, Virus Replication.
- MESH :
- chemical , genetics : Viral Matrix Proteins.
- chemical , metabolism : Membrane Glycoproteins, Viral Envelope Proteins, Viral Matrix Proteins.
- chemistry : SARS Virus.
- physiology : SARS Virus.
- virology : Golgi Apparatus.
- Amino Acid Substitution, Animals, Cell Line, Chlorocebus aethiops, Glycosylation, Humans, Mutagenesis, Site-Directed, Sequence Deletion, Spike Glycoprotein, Coronavirus, Virus Internalization, Virus Replication.
Abstract
The glycosylated membrane protein M of the severe acute respiratory syndrome associated coronavirus (SARS-CoV) is the main structural component of the virion and mediates assembly and budding of viral particles. The membrane topology of SARS-CoV M and the functional significance of its N-glycosylation are not completely understood as is its interaction with the surface glycoprotein S. Using biochemical and immunofluorescence analyses we found that M consists of a short glycosylated N-terminal ectodomain, three transmembrane segments and a long, immunogenic C-terminal endodomain. Although the N-glycosylation site of M seems to be highly conserved between group 1 and 3 coronaviruses, studies using a recombinant SARS-CoV expressing a glycosylation-deficient M revealed that N-glycosylation of M neither influence the shape of the virions nor their infectivity in cell culture. Further functional analysis of truncated M proteins showed that the N-terminal 134 amino acids comprising the three transmembrane domains are sufficient to mediate accumulation of M in the Golgi complex and to enforce recruitment of the viral spike protein S to the sites of virus assembly and budding in the ERGIC.
DOI: 10.1186/1743-422X-6-79
PubMed: 19534833
Affiliations:
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Le document en format XML
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(chemistry)</term><term>SARS Virus (physiology)</term><term>Sequence Deletion</term><term>Spike Glycoprotein, Coronavirus</term><term>Viral Envelope Proteins (metabolism)</term><term>Viral Matrix Proteins (genetics)</term><term>Viral Matrix Proteins (metabolism)</term><term>Virus Internalization</term><term>Virus Replication</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux</term><term>Appareil de Golgi (virologie)</term><term>Délétion de séquence</term><term>Glycoprotéine de spicule des coronavirus</term><term>Glycoprotéines membranaires (métabolisme)</term><term>Glycosylation</term><term>Humains</term><term>Lignée cellulaire</term><term>Mutagenèse dirigée</term><term>Protéines de l'enveloppe virale (métabolisme)</term><term>Protéines de la matrice virale (génétique)</term><term>Protéines de la matrice virale (métabolisme)</term><term>Pénétration virale</term><term>Réplication virale</term><term>Substitution d'acide aminé</term><term>Virus du SRAS 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type="abstract" xml:lang="en">The glycosylated membrane protein M of the severe acute respiratory syndrome associated coronavirus (SARS-CoV) is the main structural component of the virion and mediates assembly and budding of viral particles. The membrane topology of SARS-CoV M and the functional significance of its N-glycosylation are not completely understood as is its interaction with the surface glycoprotein S. Using biochemical and immunofluorescence analyses we found that M consists of a short glycosylated N-terminal ectodomain, three transmembrane segments and a long, immunogenic C-terminal endodomain. Although the N-glycosylation site of M seems to be highly conserved between group 1 and 3 coronaviruses, studies using a recombinant SARS-CoV expressing a glycosylation-deficient M revealed that N-glycosylation of M neither influence the shape of the virions nor their infectivity in cell culture. Further functional analysis of truncated M proteins showed that the N-terminal 134 amino acids comprising the three transmembrane domains are sufficient to mediate accumulation of M in the Golgi complex and to enforce recruitment of the viral spike protein S to the sites of virus assembly and budding in the ERGIC.</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="Drosten, Christian" sort="Drosten, Christian" uniqKey="Drosten C" first="Christian" last="Drosten">Christian Drosten</name><name sortKey="Lanzavecchia, Antonio" sort="Lanzavecchia, Antonio" uniqKey="Lanzavecchia A" first="Antonio" last="Lanzavecchia">Antonio Lanzavecchia</name><name sortKey="Pfefferle, Susanne" sort="Pfefferle, Susanne" uniqKey="Pfefferle S" first="Susanne" last="Pfefferle">Susanne Pfefferle</name><name sortKey="Stevermann, Lea" sort="Stevermann, Lea" uniqKey="Stevermann L" first="Lea" last="Stevermann">Lea Stevermann</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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