SrasV1, PubMed, Corpus, bibRecord, 002364

Characterization of severe acute respiratory syndrome coronavirus membrane protein.

Identifieur interne : 002364 ( PubMed/Corpus ); précédent : 002363; suivant : 002365

Characterization of severe acute respiratory syndrome coronavirus membrane protein.

Auteurs : Daniel Voss ; Anika Kern ; Elisabetta Traggiai ; Markus Eickmann ; Konrad Stadler ; Antonio Lanzavecchia ; Stephan Becker

Source :

FEBS letters [ 0014-5793 ] ; 2006.

RBID : pubmed:16442106

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

Links to Exploration step

pubmed:16442106

Le document en format XML

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<author><name sortKey="Traggiai, Elisabetta" sort="Traggiai, Elisabetta" uniqKey="Traggiai E" first="Elisabetta" last="Traggiai">Elisabetta Traggiai</name>
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<author><name sortKey="Lanzavecchia, Antonio" sort="Lanzavecchia, Antonio" uniqKey="Lanzavecchia A" first="Antonio" last="Lanzavecchia">Antonio Lanzavecchia</name>
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<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>
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<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase</term>
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<term>Viral Matrix Proteins</term>
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<keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Cell Membrane</term>
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<keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Cell Membrane</term>
<term>Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase</term>
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<term>SARS Virus</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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Characterization of severe acute respiratory syndrome coronavirus membrane protein.

Characterization of severe acute respiratory syndrome coronavirus membrane protein.

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