Palmitoylation of SARS-CoV S protein is necessary for partitioning into detergent-resistant membranes and cell-cell fusion but not interaction with M protein.
Identifieur interne : 002486 ( Main/Curation ); précédent : 002485; suivant : 002487Palmitoylation of SARS-CoV S protein is necessary for partitioning into detergent-resistant membranes and cell-cell fusion but not interaction with M protein.
Auteurs : Corrin E. Mcbride [États-Unis] ; Carolyn E. MachamerSource :
- Virology [ 1096-0341 ] ; 2010.
Descripteurs français
- KwdFr :
- Animaux, Cellules Vero, Détergents, Fusion cellulaire, Glycoprotéine de spicule des coronavirus, Glycoprotéines membranaires (métabolisme), Humains, Lipoylation, Membrane cellulaire (), Membrane cellulaire (physiologie), Protéines de l'enveloppe virale (métabolisme), Protéines de la matrice virale (génétique), Protéines de la matrice virale (métabolisme), Régulation de l'expression des gènes viraux (physiologie), Souris, Virus du SRAS (génétique), Virus du SRAS (métabolisme).
- MESH :
- génétique : Protéines de la matrice virale, Virus du SRAS.
- métabolisme : Glycoprotéines membranaires, Protéines de l'enveloppe virale, Protéines de la matrice virale, Virus du SRAS.
- physiologie : Membrane cellulaire, Régulation de l'expression des gènes viraux.
- Animaux, Cellules Vero, Détergents, Fusion cellulaire, Glycoprotéine de spicule des coronavirus, Humains, Lipoylation, Membrane cellulaire, Souris.
English descriptors
- KwdEn :
- Animals, Cell Fusion, Cell Membrane (chemistry), Cell Membrane (physiology), Chlorocebus aethiops, Detergents, Gene Expression Regulation, Viral (physiology), Humans, Lipoylation, Membrane Glycoproteins (metabolism), Mice, SARS Virus (genetics), SARS Virus (metabolism), Spike Glycoprotein, Coronavirus, Vero Cells, Viral Envelope Proteins (metabolism), Viral Matrix Proteins (genetics), Viral Matrix Proteins (metabolism).
- MESH :
- chemical , genetics : Viral Matrix Proteins.
- chemical , metabolism : Membrane Glycoproteins, Viral Envelope Proteins, Viral Matrix Proteins.
- chemical : Detergents, Spike Glycoprotein, Coronavirus.
- chemistry : Cell Membrane.
- genetics : SARS Virus.
- metabolism : SARS Virus.
- physiology : Cell Membrane, Gene Expression Regulation, Viral.
- Animals, Cell Fusion, Chlorocebus aethiops, Humans, Lipoylation, Mice, Vero Cells.
Abstract
Coronaviruses are enveloped RNA viruses that generally cause mild disease in humans. However, the recently emerged coronavirus that caused severe acute respiratory syndrome (SARS-CoV) is the most pathogenic human coronavirus discovered to date. The SARS-CoV spike (S) protein mediates virus entry by binding cellular receptors and inducing fusion between the viral envelope and the host cell membrane. Coronavirus S proteins are palmitoylated, which may affect function. Here, we created a non-palmitoylated SARS-CoV S protein by mutating all nine cytoplasmic cysteine residues. Palmitoylation of SARS-CoV S was required for partitioning into detergent-resistant membranes and for cell-cell fusion. Surprisingly, however, palmitoylation of S was not required for interaction with SARS-CoV M protein. This contrasts with the requirement for palmitoylation of mouse hepatitis virus S protein for interaction with M protein and may point to important differences in assembly and infectivity of these two coronaviruses.
DOI: 10.1016/j.virol.2010.05.031
PubMed: 20580052
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pubmed:20580052Le document en format XML
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Mcbride</name><affiliation wicri:level="2"><nlm:affiliation>Department of Cell Biology, The Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Cell Biology, The Johns Hopkins University School of Medicine, Baltimore, MD 21205</wicri:regionArea><placeName><region type="state">Maryland</region></placeName></affiliation></author><author><name sortKey="Machamer, Carolyn E" sort="Machamer, Carolyn E" uniqKey="Machamer C" first="Carolyn E" last="Machamer">Carolyn E. Machamer</name></author></analytic><series><title level="j">Virology</title><idno type="eISSN">1096-0341</idno><imprint><date when="2010" type="published">2010</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term><term>Cell Fusion</term><term>Cell Membrane (chemistry)</term><term>Cell Membrane (physiology)</term><term>Chlorocebus aethiops</term><term>Detergents</term><term>Gene Expression Regulation, Viral (physiology)</term><term>Humans</term><term>Lipoylation</term><term>Membrane Glycoproteins (metabolism)</term><term>Mice</term><term>SARS Virus (genetics)</term><term>SARS Virus (metabolism)</term><term>Spike Glycoprotein, Coronavirus</term><term>Vero Cells</term><term>Viral Envelope Proteins (metabolism)</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>Détergents</term><term>Fusion cellulaire</term><term>Glycoprotéine de spicule des coronavirus</term><term>Glycoprotéines membranaires (métabolisme)</term><term>Humains</term><term>Lipoylation</term><term>Membrane cellulaire ()</term><term>Membrane cellulaire (physiologie)</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>Régulation de l'expression des gènes viraux (physiologie)</term><term>Souris</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>Viral Matrix Proteins</term></keywords><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" type="chemical" xml:lang="en"><term>Detergents</term><term>Spike Glycoprotein, Coronavirus</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Cell Membrane</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Protéines de la matrice virale</term><term>Virus du SRAS</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>SARS Virus</term></keywords><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><term>Virus du SRAS</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Membrane cellulaire</term><term>Régulation de l'expression des gènes viraux</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Cell Membrane</term><term>Gene Expression Regulation, Viral</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Cell Fusion</term><term>Chlorocebus aethiops</term><term>Humans</term><term>Lipoylation</term><term>Mice</term><term>Vero Cells</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Cellules Vero</term><term>Détergents</term><term>Fusion cellulaire</term><term>Glycoprotéine de spicule des coronavirus</term><term>Humains</term><term>Lipoylation</term><term>Membrane cellulaire</term><term>Souris</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Coronaviruses are enveloped RNA viruses that generally cause mild disease in humans. However, the recently emerged coronavirus that caused severe acute respiratory syndrome (SARS-CoV) is the most pathogenic human coronavirus discovered to date. The SARS-CoV spike (S) protein mediates virus entry by binding cellular receptors and inducing fusion between the viral envelope and the host cell membrane. Coronavirus S proteins are palmitoylated, which may affect function. Here, we created a non-palmitoylated SARS-CoV S protein by mutating all nine cytoplasmic cysteine residues. Palmitoylation of SARS-CoV S was required for partitioning into detergent-resistant membranes and for cell-cell fusion. Surprisingly, however, palmitoylation of S was not required for interaction with SARS-CoV M protein. This contrasts with the requirement for palmitoylation of mouse hepatitis virus S protein for interaction with M protein and may point to important differences in assembly and infectivity of these two coronaviruses.</div></front></TEI></record>Pour manipuler ce document sous Unix (Dilib)
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