Self-assembly of severe acute respiratory syndrome coronavirus membrane protein.
Identifieur interne : 002455 ( Main/Exploration ); précédent : 002454; suivant : 002456Self-assembly of severe acute respiratory syndrome coronavirus membrane protein.
Auteurs : Ying-Tzu Tseng [Taïwan] ; Shiu-Mei Wang ; Kuo-Jung Huang ; Amber I-Ru Lee ; Chien-Cheng Chiang ; Chin-Tien WangSource :
- The Journal of biological chemistry [ 1083-351X ] ; 2010.
Descripteurs français
- KwdFr :
- Animaux, Appareil de Golgi (génétique), Appareil de Golgi (métabolisme), Appareil de Golgi (virologie), Cellules HeLa, Cellules Vero, Glycosylation, Humains, Membrane cellulaire (génétique), Membrane cellulaire (métabolisme), Membrane cellulaire (virologie), Multimérisation de protéines (physiologie), Protéines de fusion recombinantes (génétique), Protéines de fusion recombinantes (métabolisme), Protéines de la matrice virale (génétique), Protéines de la matrice virale (métabolisme), Protéines membranaires (génétique), Protéines membranaires (métabolisme), Protéines nucléocapside (génétique), Protéines nucléocapside (métabolisme), Structure tertiaire des protéines, Virus du SRAS (génétique), Virus du SRAS (métabolisme).
- MESH :
- génétique : Appareil de Golgi, Membrane cellulaire, Protéines de fusion recombinantes, Protéines de la matrice virale, Protéines membranaires, Protéines nucléocapside, Virus du SRAS.
- métabolisme : Appareil de Golgi, Membrane cellulaire, Protéines de fusion recombinantes, Protéines de la matrice virale, Protéines membranaires, Protéines nucléocapside, Virus du SRAS.
- physiologie : Multimérisation de protéines.
- virologie : Appareil de Golgi, Membrane cellulaire.
- Animaux, Cellules HeLa, Cellules Vero, Glycosylation, Humains, Structure tertiaire des protéines.
English descriptors
- KwdEn :
- Animals, Cell Membrane (genetics), Cell Membrane (metabolism), Cell Membrane (virology), Chlorocebus aethiops, Glycosylation, Golgi Apparatus (genetics), Golgi Apparatus (metabolism), Golgi Apparatus (virology), HeLa Cells, Humans, Membrane Proteins (genetics), Membrane Proteins (metabolism), Nucleocapsid Proteins (genetics), Nucleocapsid Proteins (metabolism), Protein Multimerization (physiology), Protein Structure, Tertiary, Recombinant Fusion Proteins (genetics), Recombinant Fusion Proteins (metabolism), SARS Virus (genetics), SARS Virus (metabolism), Vero Cells, Viral Matrix Proteins (genetics), Viral Matrix Proteins (metabolism).
- MESH :
- chemical , genetics : Membrane Proteins, Nucleocapsid Proteins, Recombinant Fusion Proteins, Viral Matrix Proteins.
- genetics : Cell Membrane, Golgi Apparatus, SARS Virus.
- metabolism : Cell Membrane, Golgi Apparatus, Membrane Proteins, Nucleocapsid Proteins, Recombinant Fusion Proteins, SARS Virus, Viral Matrix Proteins.
- physiology : Protein Multimerization.
- virology : Cell Membrane, Golgi Apparatus.
- Animals, Chlorocebus aethiops, Glycosylation, HeLa Cells, Humans, Protein Structure, Tertiary, Vero Cells.
Abstract
Coronavirus membrane (M) protein can form virus-like particles (VLPs) when coexpressed with nucleocapsid (N) or envelope (E) proteins, suggesting a pivotal role for M in virion assembly. Here we demonstrate the self-assembly and release of severe acute respiratory syndrome coronavirus (SARS-CoV) M protein in medium in the form of membrane-enveloped vesicles with densities lower than those of VLPs formed by M plus N. Although efficient N-N interactions require the presence of RNA, we found that M-M interactions were RNA-independent. SARS-CoV M was observed in both the Golgi area and plasma membranes of a variety of cells. Blocking M glycosylation does not appear to significantly affect M plasma membrane labeling intensity, M-containing vesicle release, or VLP formation. Results from a genetic analysis indicate involvement of the third transmembrane domain of M in plasma membrane-targeting signal. Fusion proteins containing M amino-terminal 50 residues encompassing the first transmembrane domain were found to be sufficient for membrane binding, multimerization, and Golgi retention. Surprisingly, we found that fusion proteins lacking all three transmembrane domains were still capable of membrane binding, Golgi retention, and interacting with M. The data suggest that multiple SARS-CoV M regions are involved in M self-assembly and subcellular localization.
DOI: 10.1074/jbc.M109.030270
PubMed: 20154085
Affiliations:
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Le document en format XML
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Fusion Proteins</term><term>SARS Virus</term><term>Viral Matrix Proteins</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Appareil de Golgi</term><term>Membrane cellulaire</term><term>Protéines de fusion recombinantes</term><term>Protéines de la matrice virale</term><term>Protéines membranaires</term><term>Protéines nucléocapside</term><term>Virus du SRAS</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Multimérisation de protéines</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Protein Multimerization</term></keywords><keywords scheme="MESH" qualifier="virologie" xml:lang="fr"><term>Appareil de Golgi</term><term>Membrane cellulaire</term></keywords><keywords scheme="MESH" qualifier="virology" xml:lang="en"><term>Cell Membrane</term><term>Golgi Apparatus</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Chlorocebus aethiops</term><term>Glycosylation</term><term>HeLa Cells</term><term>Humans</term><term>Protein Structure, Tertiary</term><term>Vero Cells</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Cellules HeLa</term><term>Cellules Vero</term><term>Glycosylation</term><term>Humains</term><term>Structure tertiaire des protéines</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Coronavirus membrane (M) protein can form virus-like particles (VLPs) when coexpressed with nucleocapsid (N) or envelope (E) proteins, suggesting a pivotal role for M in virion assembly. Here we demonstrate the self-assembly and release of severe acute respiratory syndrome coronavirus (SARS-CoV) M protein in medium in the form of membrane-enveloped vesicles with densities lower than those of VLPs formed by M plus N. Although efficient N-N interactions require the presence of RNA, we found that M-M interactions were RNA-independent. SARS-CoV M was observed in both the Golgi area and plasma membranes of a variety of cells. Blocking M glycosylation does not appear to significantly affect M plasma membrane labeling intensity, M-containing vesicle release, or VLP formation. Results from a genetic analysis indicate involvement of the third transmembrane domain of M in plasma membrane-targeting signal. Fusion proteins containing M amino-terminal 50 residues encompassing the first transmembrane domain were found to be sufficient for membrane binding, multimerization, and Golgi retention. Surprisingly, we found that fusion proteins lacking all three transmembrane domains were still capable of membrane binding, Golgi retention, and interacting with M. The data suggest that multiple SARS-CoV M regions are involved in M self-assembly and subcellular localization.</div></front></TEI><affiliations><list><country><li>Taïwan</li></country></list><tree><noCountry><name sortKey="Chiang, Chien Cheng" sort="Chiang, Chien Cheng" uniqKey="Chiang C" first="Chien-Cheng" last="Chiang">Chien-Cheng Chiang</name><name sortKey="Huang, Kuo Jung" sort="Huang, Kuo Jung" uniqKey="Huang K" first="Kuo-Jung" last="Huang">Kuo-Jung Huang</name><name sortKey="Lee, Amber I Ru" sort="Lee, Amber I Ru" uniqKey="Lee A" first="Amber I-Ru" last="Lee">Amber I-Ru Lee</name><name sortKey="Wang, Chin Tien" sort="Wang, Chin Tien" uniqKey="Wang C" first="Chin-Tien" last="Wang">Chin-Tien Wang</name><name sortKey="Wang, Shiu Mei" sort="Wang, Shiu Mei" uniqKey="Wang S" first="Shiu-Mei" last="Wang">Shiu-Mei Wang</name></noCountry><country name="Taïwan"><noRegion><name sortKey="Tseng, Ying Tzu" sort="Tseng, Ying Tzu" uniqKey="Tseng Y" first="Ying-Tzu" last="Tseng">Ying-Tzu Tseng</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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