Biochemical and functional characterization of the membrane association and membrane permeabilizing activity of the severe acute respiratory syndrome coronavirus envelope protein.
Identifieur interne : 003F67 ( Main/Exploration ); précédent : 003F66; suivant : 003F68Biochemical and functional characterization of the membrane association and membrane permeabilizing activity of the severe acute respiratory syndrome coronavirus envelope protein.
Auteurs : Y. Liao [Singapour] ; Q. Yuan ; J. Torres ; J P Tam ; D X LiuSource :
- Virology [ 0042-6822 ] ; 2006.
Descripteurs français
- KwdFr :
- Analyse de mutations d'ADN, Animaux, Appareil de Golgi (métabolisme), Cellules HeLa, Cricetinae, Données de séquences moléculaires, Humains, Immunohistochimie, Lignée cellulaire, Maturation post-traductionnelle des protéines, Membrane cellulaire (métabolisme), Microdomaines membranaires (métabolisme), Microscopie de fluorescence, Mutagenèse dirigée, Mutation faux-sens, Palmitoyl coenzyme A (métabolisme), Perméabilité de la membrane cellulaire, Protéines de l'enveloppe virale (), Protéines de l'enveloppe virale (génétique), Protéines de l'enveloppe virale (métabolisme), Protéines de l'enveloppe virale (physiologie), Réticulum endoplasmique (métabolisme), Structure tertiaire des protéines, Substitution d'acide aminé, Séquence d'acides aminés.
- MESH :
- génétique : Protéines de l'enveloppe virale.
- métabolisme : Appareil de Golgi, Membrane cellulaire, Microdomaines membranaires, Palmitoyl coenzyme A, Protéines de l'enveloppe virale, Réticulum endoplasmique.
- physiologie : Protéines de l'enveloppe virale.
- Analyse de mutations d'ADN, Animaux, Cellules HeLa, Cricetinae, Données de séquences moléculaires, Humains, Immunohistochimie, Lignée cellulaire, Maturation post-traductionnelle des protéines, Microscopie de fluorescence, Mutagenèse dirigée, Mutation faux-sens, Perméabilité de la membrane cellulaire, Protéines de l'enveloppe virale, Structure tertiaire des protéines, Substitution d'acide aminé, Séquence d'acides aminés.
English descriptors
- KwdEn :
- Amino Acid Sequence, Amino Acid Substitution, Animals, Cell Line, Cell Membrane (metabolism), Cell Membrane Permeability, Cricetinae, DNA Mutational Analysis, Endoplasmic Reticulum (metabolism), Golgi Apparatus (metabolism), HeLa Cells, Humans, Immunohistochemistry, Membrane Microdomains (metabolism), Microscopy, Fluorescence, Molecular Sequence Data, Mutagenesis, Site-Directed, Mutation, Missense, Palmitoyl Coenzyme A (metabolism), Protein Processing, Post-Translational, Protein Structure, Tertiary, Viral Envelope Proteins (chemistry), Viral Envelope Proteins (genetics), Viral Envelope Proteins (metabolism), Viral Envelope Proteins (physiology).
- MESH :
- chemical , chemistry : Viral Envelope Proteins.
- chemical , genetics : Viral Envelope Proteins.
- chemical , metabolism : Palmitoyl Coenzyme A, Viral Envelope Proteins.
- metabolism : Cell Membrane, Endoplasmic Reticulum, Golgi Apparatus, Membrane Microdomains.
- chemical , physiology : Viral Envelope Proteins.
- Amino Acid Sequence, Amino Acid Substitution, Animals, Cell Line, Cell Membrane Permeability, Cricetinae, DNA Mutational Analysis, HeLa Cells, Humans, Immunohistochemistry, Microscopy, Fluorescence, Molecular Sequence Data, Mutagenesis, Site-Directed, Mutation, Missense, Protein Processing, Post-Translational, Protein Structure, Tertiary.
Abstract
A diverse group of cytolytic animal viruses encodes small, hydrophobic proteins to modify host cell membrane permeability to ions and small molecules during their infection cycles. In this study, we show that expression of the SARS-CoV E protein in mammalian cells alters the membrane permeability of these cells. Immunofluorescent staining and cell fractionation studies demonstrate that this protein is an integral membrane protein. It is mainly localized to the ER and the Golgi apparatus. The protein can be translocated to the cell surface and is partially associated with lipid rafts. Further biochemical characterization of the protein reveals that it is posttranslationally modified by palmitoylation on all three cysteine residues. Systematic mutagenesis studies confirm that the membrane permeabilizing activity of the SARS-CoV E protein is associated with its transmembrane domain.
DOI: 10.1016/j.virol.2006.01.028
PubMed: 16507314
Affiliations:
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Le document en format XML
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Liao</name><affiliation wicri:level="1"><nlm:affiliation>School of Biological Science, Nanyang Technological University, 60 Nanyang Drive, Singapore 637551, Singapore.</nlm:affiliation><country xml:lang="fr">Singapour</country><wicri:regionArea>School of Biological Science, Nanyang Technological University, 60 Nanyang Drive, Singapore 637551</wicri:regionArea><wicri:noRegion>Singapore 637551</wicri:noRegion></affiliation></author><author><name sortKey="Yuan, Q" sort="Yuan, Q" uniqKey="Yuan Q" first="Q" last="Yuan">Q. Yuan</name></author><author><name sortKey="Torres, J" sort="Torres, J" uniqKey="Torres J" first="J" last="Torres">J. Torres</name></author><author><name sortKey="Tam, J P" sort="Tam, J P" uniqKey="Tam J" first="J P" last="Tam">J P Tam</name></author><author><name sortKey="Liu, D X" sort="Liu, D X" uniqKey="Liu D" first="D X" last="Liu">D X Liu</name></author></analytic><series><title level="j">Virology</title><idno type="ISSN">0042-6822</idno><imprint><date when="2006" type="published">2006</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence</term><term>Amino Acid Substitution</term><term>Animals</term><term>Cell Line</term><term>Cell Membrane (metabolism)</term><term>Cell Membrane Permeability</term><term>Cricetinae</term><term>DNA Mutational Analysis</term><term>Endoplasmic Reticulum (metabolism)</term><term>Golgi Apparatus (metabolism)</term><term>HeLa Cells</term><term>Humans</term><term>Immunohistochemistry</term><term>Membrane Microdomains (metabolism)</term><term>Microscopy, Fluorescence</term><term>Molecular Sequence Data</term><term>Mutagenesis, Site-Directed</term><term>Mutation, Missense</term><term>Palmitoyl Coenzyme A (metabolism)</term><term>Protein Processing, Post-Translational</term><term>Protein Structure, Tertiary</term><term>Viral Envelope Proteins (chemistry)</term><term>Viral Envelope Proteins (genetics)</term><term>Viral Envelope Proteins (metabolism)</term><term>Viral Envelope Proteins (physiology)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Analyse de mutations d'ADN</term><term>Animaux</term><term>Appareil de Golgi (métabolisme)</term><term>Cellules HeLa</term><term>Cricetinae</term><term>Données de séquences moléculaires</term><term>Humains</term><term>Immunohistochimie</term><term>Lignée cellulaire</term><term>Maturation post-traductionnelle des protéines</term><term>Membrane cellulaire (métabolisme)</term><term>Microdomaines membranaires (métabolisme)</term><term>Microscopie de fluorescence</term><term>Mutagenèse dirigée</term><term>Mutation faux-sens</term><term>Palmitoyl coenzyme A (métabolisme)</term><term>Perméabilité de la membrane cellulaire</term><term>Protéines de l'enveloppe virale ()</term><term>Protéines de l'enveloppe virale (génétique)</term><term>Protéines de l'enveloppe virale (métabolisme)</term><term>Protéines de l'enveloppe virale (physiologie)</term><term>Réticulum endoplasmique (métabolisme)</term><term>Structure tertiaire des protéines</term><term>Substitution d'acide aminé</term><term>Séquence d'acides aminés</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Palmitoyl Coenzyme A</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Protéines de l'enveloppe virale</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Cell Membrane</term><term>Endoplasmic Reticulum</term><term>Golgi Apparatus</term><term>Membrane Microdomains</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Appareil de Golgi</term><term>Membrane cellulaire</term><term>Microdomaines membranaires</term><term>Palmitoyl coenzyme A</term><term>Protéines de l'enveloppe virale</term><term>Réticulum endoplasmique</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Protéines de l'enveloppe virale</term></keywords><keywords scheme="MESH" type="chemical" qualifier="physiology" xml:lang="en"><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Amino Acid Substitution</term><term>Animals</term><term>Cell Line</term><term>Cell Membrane Permeability</term><term>Cricetinae</term><term>DNA Mutational Analysis</term><term>HeLa Cells</term><term>Humans</term><term>Immunohistochemistry</term><term>Microscopy, Fluorescence</term><term>Molecular Sequence Data</term><term>Mutagenesis, Site-Directed</term><term>Mutation, Missense</term><term>Protein Processing, Post-Translational</term><term>Protein Structure, Tertiary</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Analyse de mutations d'ADN</term><term>Animaux</term><term>Cellules HeLa</term><term>Cricetinae</term><term>Données de séquences moléculaires</term><term>Humains</term><term>Immunohistochimie</term><term>Lignée cellulaire</term><term>Maturation post-traductionnelle des protéines</term><term>Microscopie de fluorescence</term><term>Mutagenèse dirigée</term><term>Mutation faux-sens</term><term>Perméabilité de la membrane cellulaire</term><term>Protéines de l'enveloppe virale</term><term>Structure tertiaire des protéines</term><term>Substitution d'acide aminé</term><term>Séquence d'acides aminés</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">A diverse group of cytolytic animal viruses encodes small, hydrophobic proteins to modify host cell membrane permeability to ions and small molecules during their infection cycles. In this study, we show that expression of the SARS-CoV E protein in mammalian cells alters the membrane permeability of these cells. Immunofluorescent staining and cell fractionation studies demonstrate that this protein is an integral membrane protein. It is mainly localized to the ER and the Golgi apparatus. The protein can be translocated to the cell surface and is partially associated with lipid rafts. Further biochemical characterization of the protein reveals that it is posttranslationally modified by palmitoylation on all three cysteine residues. Systematic mutagenesis studies confirm that the membrane permeabilizing activity of the SARS-CoV E protein is associated with its transmembrane domain.</div></front></TEI><affiliations><list><country><li>Singapour</li></country></list><tree><noCountry><name sortKey="Liu, D X" sort="Liu, D X" uniqKey="Liu D" first="D X" last="Liu">D X Liu</name><name sortKey="Tam, J P" sort="Tam, J P" uniqKey="Tam J" first="J P" last="Tam">J P Tam</name><name sortKey="Torres, J" sort="Torres, J" uniqKey="Torres J" first="J" last="Torres">J. Torres</name><name sortKey="Yuan, Q" sort="Yuan, Q" uniqKey="Yuan Q" first="Q" last="Yuan">Q. Yuan</name></noCountry><country name="Singapour"><noRegion><name sortKey="Liao, Y" sort="Liao, Y" uniqKey="Liao Y" first="Y" last="Liao">Y. Liao</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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