A single tyrosine in the severe acute respiratory syndrome coronavirus membrane protein cytoplasmic tail is important for efficient interaction with spike protein.
Identifieur interne : 002588 ( Main/Exploration ); précédent : 002587; suivant : 002589A single tyrosine in the severe acute respiratory syndrome coronavirus membrane protein cytoplasmic tail is important for efficient interaction with spike protein.
Auteurs : Corrin E. Mcbride [États-Unis] ; Carolyn E. MachamerSource :
- Journal of virology [ 1098-5514 ] ; 2010.
Descripteurs français
- KwdFr :
- ADN viral (génétique), Appareil de Golgi (métabolisme), Appareil de Golgi (virologie), Assemblage viral (génétique), Assemblage viral (physiologie), Cellules HeLa, Données de séquences moléculaires, Glycoprotéine de spicule des coronavirus, Glycoprotéines membranaires (), Glycoprotéines membranaires (génétique), Glycoprotéines membranaires (physiologie), Humains, Lignée cellulaire, Motifs et domaines d'intéraction protéique, Mutagenèse dirigée, Plasmides (génétique), Protéines de l'enveloppe virale (), Protéines de l'enveloppe virale (génétique), Protéines de l'enveloppe virale (physiologie), Protéines de la matrice virale (), Protéines de la matrice virale (génétique), Protéines de la matrice virale (physiologie), Protéines recombinantes (), Protéines recombinantes (génétique), Protéines recombinantes (métabolisme), Similitude de séquences d'acides aminés, Substitution d'acide aminé, Séquence d'acides aminés, Séquence nucléotidique, Transfection, Tyrosine (), Virus du SRAS (génétique), Virus du SRAS (pathogénicité), Virus du SRAS (physiologie).
- MESH :
- génétique : ADN viral, Assemblage viral, Glycoprotéines membranaires, Plasmides, Protéines de l'enveloppe virale, Protéines de la matrice virale, Protéines recombinantes, Virus du SRAS.
- métabolisme : Appareil de Golgi, Protéines recombinantes.
- pathogénicité : Virus du SRAS.
- physiologie : Assemblage viral, Glycoprotéines membranaires, Protéines de l'enveloppe virale, Protéines de la matrice virale, Virus du SRAS.
- virologie : Appareil de Golgi.
- Cellules HeLa, Données de séquences moléculaires, Glycoprotéine de spicule des coronavirus, Glycoprotéines membranaires, Humains, Lignée cellulaire, Motifs et domaines d'intéraction protéique, Mutagenèse dirigée, Protéines de l'enveloppe virale, Protéines de la matrice virale, Protéines recombinantes, Similitude de séquences d'acides aminés, Substitution d'acide aminé, Séquence d'acides aminés, Séquence nucléotidique, Transfection, Tyrosine.
English descriptors
- KwdEn :
- Amino Acid Sequence, Amino Acid Substitution, Base Sequence, Cell Line, DNA, Viral (genetics), Golgi Apparatus (metabolism), Golgi Apparatus (virology), HeLa Cells, Humans, Membrane Glycoproteins (chemistry), Membrane Glycoproteins (genetics), Membrane Glycoproteins (physiology), Molecular Sequence Data, Mutagenesis, Site-Directed, Plasmids (genetics), Protein Interaction Domains and Motifs, Recombinant Proteins (chemistry), Recombinant Proteins (genetics), Recombinant Proteins (metabolism), SARS Virus (genetics), SARS Virus (pathogenicity), SARS Virus (physiology), Sequence Homology, Amino Acid, Spike Glycoprotein, Coronavirus, Transfection, Tyrosine (chemistry), Viral Envelope Proteins (chemistry), Viral Envelope Proteins (genetics), Viral Envelope Proteins (physiology), Viral Matrix Proteins (chemistry), Viral Matrix Proteins (genetics), Viral Matrix Proteins (physiology), Virus Assembly (genetics), Virus Assembly (physiology).
- MESH :
- chemical , chemistry : Membrane Glycoproteins, Recombinant Proteins, Tyrosine, Viral Envelope Proteins, Viral Matrix Proteins.
- chemical , genetics : DNA, Viral, Membrane Glycoproteins, Recombinant Proteins, Viral Envelope Proteins, Viral Matrix Proteins.
- genetics : Plasmids, SARS Virus, Virus Assembly.
- metabolism : Golgi Apparatus, Recombinant Proteins.
- pathogenicity : SARS Virus.
- chemical , physiology : Membrane Glycoproteins, SARS Virus, Viral Envelope Proteins, Viral Matrix Proteins, Virus Assembly.
- virology : Golgi Apparatus.
- Amino Acid Sequence, Amino Acid Substitution, Base Sequence, Cell Line, HeLa Cells, Humans, Molecular Sequence Data, Mutagenesis, Site-Directed, Protein Interaction Domains and Motifs, Sequence Homology, Amino Acid, Spike Glycoprotein, Coronavirus, Transfection.
Abstract
Severe acute respiratory syndrome coronavirus (SARS-CoV) encodes 3 major envelope proteins: spike (S), membrane (M), and envelope (E). Previous work identified a dibasic endoplasmic reticulum retrieval signal in the cytoplasmic tail of SARS-CoV S that promotes efficient interaction with SARS-CoV M. The dibasic signal was shown to be important for concentrating S near the virus assembly site rather than for direct interaction with M. Here, we investigated the sequence requirements of the SARS-CoV M protein that are necessary for interaction with SARS-CoV S. The SARS-CoV M tail was shown to be necessary for S localization in the Golgi region when the proteins were exogenously coexpressed in cells. This was specific, since SARS-CoV M did not retain an unrelated glycoprotein in the Golgi. Importantly, we found that an essential tyrosine residue in the SARS-CoV M cytoplasmic tail, Y(195), was important for S-M interaction. When Y(195) was mutated to alanine, M(Y195A) no longer retained S intracellularly at the Golgi. Unlike wild-type M, M(Y195A) did not reduce the amount of SARS-CoV S carbohydrate processing or surface levels when the two proteins were coexpressed. Mutating Y(195) also disrupted SARS-CoV S-M interaction in vitro. These results suggest that Y(195) is necessary for efficient SARS-CoV S-M interaction and, thus, has a significant involvement in assembly of infectious virus.
DOI: 10.1128/JVI.02458-09
PubMed: 20007283
Affiliations:
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Le 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, 725 N. Wolfe St., 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, 725 N. Wolfe St., 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">Journal of virology</title><idno type="eISSN">1098-5514</idno><imprint><date when="2010" type="published">2010</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>Base Sequence</term><term>Cell Line</term><term>DNA, Viral (genetics)</term><term>Golgi Apparatus (metabolism)</term><term>Golgi Apparatus (virology)</term><term>HeLa Cells</term><term>Humans</term><term>Membrane Glycoproteins (chemistry)</term><term>Membrane Glycoproteins (genetics)</term><term>Membrane Glycoproteins (physiology)</term><term>Molecular Sequence Data</term><term>Mutagenesis, Site-Directed</term><term>Plasmids (genetics)</term><term>Protein Interaction Domains and Motifs</term><term>Recombinant Proteins (chemistry)</term><term>Recombinant Proteins (genetics)</term><term>Recombinant Proteins (metabolism)</term><term>SARS Virus (genetics)</term><term>SARS Virus (pathogenicity)</term><term>SARS Virus (physiology)</term><term>Sequence Homology, Amino Acid</term><term>Spike Glycoprotein, Coronavirus</term><term>Transfection</term><term>Tyrosine (chemistry)</term><term>Viral Envelope Proteins (chemistry)</term><term>Viral Envelope Proteins (genetics)</term><term>Viral Envelope Proteins (physiology)</term><term>Viral Matrix Proteins (chemistry)</term><term>Viral Matrix Proteins (genetics)</term><term>Viral Matrix Proteins (physiology)</term><term>Virus Assembly (genetics)</term><term>Virus Assembly (physiology)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>ADN viral (génétique)</term><term>Appareil de Golgi (métabolisme)</term><term>Appareil de Golgi (virologie)</term><term>Assemblage viral (génétique)</term><term>Assemblage viral (physiologie)</term><term>Cellules HeLa</term><term>Données de séquences moléculaires</term><term>Glycoprotéine de spicule des coronavirus</term><term>Glycoprotéines membranaires ()</term><term>Glycoprotéines membranaires (génétique)</term><term>Glycoprotéines membranaires (physiologie)</term><term>Humains</term><term>Lignée cellulaire</term><term>Motifs et domaines d'intéraction protéique</term><term>Mutagenèse dirigée</term><term>Plasmides (génétique)</term><term>Protéines de l'enveloppe virale ()</term><term>Protéines de l'enveloppe virale (génétique)</term><term>Protéines de l'enveloppe virale (physiologie)</term><term>Protéines de la matrice virale ()</term><term>Protéines de la matrice virale (génétique)</term><term>Protéines de la matrice virale (physiologie)</term><term>Protéines recombinantes ()</term><term>Protéines recombinantes (génétique)</term><term>Protéines recombinantes (métabolisme)</term><term>Similitude de séquences d'acides aminés</term><term>Substitution d'acide aminé</term><term>Séquence d'acides aminés</term><term>Séquence nucléotidique</term><term>Transfection</term><term>Tyrosine ()</term><term>Virus du SRAS (génétique)</term><term>Virus du SRAS (pathogénicité)</term><term>Virus du SRAS (physiologie)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Membrane Glycoproteins</term><term>Recombinant Proteins</term><term>Tyrosine</term><term>Viral Envelope Proteins</term><term>Viral Matrix Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>DNA, Viral</term><term>Membrane Glycoproteins</term><term>Recombinant Proteins</term><term>Viral Envelope Proteins</term><term>Viral Matrix Proteins</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Plasmids</term><term>SARS Virus</term><term>Virus Assembly</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>ADN viral</term><term>Assemblage viral</term><term>Glycoprotéines membranaires</term><term>Plasmides</term><term>Protéines de l'enveloppe virale</term><term>Protéines de la matrice virale</term><term>Protéines recombinantes</term><term>Virus du SRAS</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Golgi Apparatus</term><term>Recombinant Proteins</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Appareil de Golgi</term><term>Protéines recombinantes</term></keywords><keywords scheme="MESH" qualifier="pathogenicity" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" qualifier="pathogénicité" xml:lang="fr"><term>Virus du SRAS</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Assemblage viral</term><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" type="chemical" qualifier="physiology" xml:lang="en"><term>Membrane Glycoproteins</term><term>SARS Virus</term><term>Viral Envelope Proteins</term><term>Viral Matrix Proteins</term><term>Virus Assembly</term></keywords><keywords scheme="MESH" qualifier="virologie" xml:lang="fr"><term>Appareil de Golgi</term></keywords><keywords scheme="MESH" qualifier="virology" xml:lang="en"><term>Golgi Apparatus</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Amino Acid Substitution</term><term>Base Sequence</term><term>Cell Line</term><term>HeLa Cells</term><term>Humans</term><term>Molecular Sequence Data</term><term>Mutagenesis, Site-Directed</term><term>Protein Interaction Domains and Motifs</term><term>Sequence Homology, Amino Acid</term><term>Spike Glycoprotein, Coronavirus</term><term>Transfection</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Cellules HeLa</term><term>Données de séquences moléculaires</term><term>Glycoprotéine de spicule des coronavirus</term><term>Glycoprotéines membranaires</term><term>Humains</term><term>Lignée cellulaire</term><term>Motifs et domaines d'intéraction protéique</term><term>Mutagenèse dirigée</term><term>Protéines de l'enveloppe virale</term><term>Protéines de la matrice virale</term><term>Protéines recombinantes</term><term>Similitude de séquences d'acides aminés</term><term>Substitution d'acide aminé</term><term>Séquence d'acides aminés</term><term>Séquence nucléotidique</term><term>Transfection</term><term>Tyrosine</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Severe acute respiratory syndrome coronavirus (SARS-CoV) encodes 3 major envelope proteins: spike (S), membrane (M), and envelope (E). Previous work identified a dibasic endoplasmic reticulum retrieval signal in the cytoplasmic tail of SARS-CoV S that promotes efficient interaction with SARS-CoV M. The dibasic signal was shown to be important for concentrating S near the virus assembly site rather than for direct interaction with M. Here, we investigated the sequence requirements of the SARS-CoV M protein that are necessary for interaction with SARS-CoV S. The SARS-CoV M tail was shown to be necessary for S localization in the Golgi region when the proteins were exogenously coexpressed in cells. This was specific, since SARS-CoV M did not retain an unrelated glycoprotein in the Golgi. Importantly, we found that an essential tyrosine residue in the SARS-CoV M cytoplasmic tail, Y(195), was important for S-M interaction. When Y(195) was mutated to alanine, M(Y195A) no longer retained S intracellularly at the Golgi. Unlike wild-type M, M(Y195A) did not reduce the amount of SARS-CoV S carbohydrate processing or surface levels when the two proteins were coexpressed. Mutating Y(195) also disrupted SARS-CoV S-M interaction in vitro. These results suggest that Y(195) is necessary for efficient SARS-CoV S-M interaction and, thus, has a significant involvement in assembly of infectious virus.</div></front></TEI><affiliations><list><country><li>États-Unis</li></country><region><li>Maryland</li></region></list><tree><noCountry><name sortKey="Machamer, Carolyn E" sort="Machamer, Carolyn E" uniqKey="Machamer C" first="Carolyn E" last="Machamer">Carolyn E. Machamer</name></noCountry><country name="États-Unis"><region name="Maryland"><name sortKey="Mcbride, Corrin E" sort="Mcbride, Corrin E" uniqKey="Mcbride C" first="Corrin E" last="Mcbride">Corrin E. Mcbride</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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