A novel sorting signal for intracellular localization is present in the S protein of a porcine coronavirus but absent from severe acute respiratory syndrome-associated coronavirus.
Identifieur interne : 005488 ( Main/Exploration ); précédent : 005487; suivant : 005489A novel sorting signal for intracellular localization is present in the S protein of a porcine coronavirus but absent from severe acute respiratory syndrome-associated coronavirus.
Auteurs : Christel Schwegmann-Wessels [Allemagne] ; Marwan Al-Falah ; David Escors ; Zai Wang ; Gert Zimmer ; Hongkui Deng ; Luis Enjuanes ; Hassan Y. Naim ; Georg HerrlerSource :
- The Journal of biological chemistry [ 0021-9258 ] ; 2004.
Descripteurs français
- KwdFr :
- Amorces ADN, Animaux, Coronavirus (), Coronavirus (physiologie), Données de séquences moléculaires, Glycoprotéine de spicule des coronavirus, Glycoprotéines membranaires (), Glycoprotéines membranaires (génétique), Glycoprotéines membranaires (physiologie), Mutagenèse dirigée, Protéines de l'enveloppe virale (), Protéines de l'enveloppe virale (génétique), Protéines de l'enveloppe virale (physiologie), Substitution d'acide aminé, Suidae, Syndrome de détresse respiratoire de l'adulte (virologie), Séquence nucléotidique.
- MESH :
- génétique : Glycoprotéines membranaires, Protéines de l'enveloppe virale.
- physiologie : Coronavirus, Glycoprotéines membranaires, Protéines de l'enveloppe virale.
- virologie : Syndrome de détresse respiratoire de l'adulte.
- Amorces ADN, Animaux, Coronavirus, Données de séquences moléculaires, Glycoprotéine de spicule des coronavirus, Glycoprotéines membranaires, Mutagenèse dirigée, Protéines de l'enveloppe virale, Substitution d'acide aminé, Suidae, Séquence nucléotidique.
English descriptors
- KwdEn :
- Amino Acid Substitution, Animals, Base Sequence, Coronavirus (classification), Coronavirus (physiology), DNA Primers, Membrane Glycoproteins (chemistry), Membrane Glycoproteins (genetics), Membrane Glycoproteins (physiology), Molecular Sequence Data, Mutagenesis, Site-Directed, Respiratory Distress Syndrome, Adult (virology), Spike Glycoprotein, Coronavirus, Swine, Viral Envelope Proteins (chemistry), Viral Envelope Proteins (genetics), Viral Envelope Proteins (physiology).
- MESH :
- chemical , chemistry : Membrane Glycoproteins, Viral Envelope Proteins.
- chemical , genetics : Membrane Glycoproteins, Viral Envelope Proteins.
- chemical , physiology : Membrane Glycoproteins, Viral Envelope Proteins.
- chemical : DNA Primers, Spike Glycoprotein, Coronavirus.
- classification : Coronavirus.
- physiology : Coronavirus.
- virology : Respiratory Distress Syndrome, Adult.
- Amino Acid Substitution, Animals, Base Sequence, Molecular Sequence Data, Mutagenesis, Site-Directed, Swine.
Abstract
Coronaviruses (CoV) mature by a budding process at intracellular membranes. Here we showed that the major surface protein S of a porcine CoV (transmissible gastroenteritis virus) is not transported to the cell surface but is retained intracellularly. Site-directed mutagenesis indicated that a tyrosine-dependent signal (YXXI) in the cytoplasmic tail is essential for intracellular localization of the S protein. Surface expression of mutant proteins was evident by immunofluorescence analysis and surface biotinylation. Intracellularly retained S proteins only contained endoglycosidase H-sensitive N-glycans, whereas mutant proteins that migrated to the plasma membrane acquired N-linked oligosaccharides of the complex type. Corresponding tyrosine residues are present in the cytoplasmic tails of the S proteins of other animal CoV but not in the tail portion of the S protein of severe acute respiratory syndrome (SARS)-CoV. Changing the SEPV tetrapeptide in the cytoplasmic tail to YEPI resulted in intracellular retention of the S protein of SARS-CoV. As the S proteins of CoV have receptor binding and fusion activities and are the main target of neutralizing antibodies, the differences in the transport behavior of the S proteins suggest different strategies in the virus host interactions between SARS-CoV and other coronaviruses.
DOI: 10.1074/jbc.M407233200
PubMed: 15304515
Affiliations:
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Le document en format XML
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Naim</name></author><author><name sortKey="Herrler, Georg" sort="Herrler, Georg" uniqKey="Herrler G" first="Georg" last="Herrler">Georg Herrler</name></author></analytic><series><title level="j">The Journal of biological chemistry</title><idno type="ISSN">0021-9258</idno><imprint><date when="2004" type="published">2004</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Substitution</term><term>Animals</term><term>Base Sequence</term><term>Coronavirus (classification)</term><term>Coronavirus (physiology)</term><term>DNA Primers</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>Respiratory Distress Syndrome, Adult (virology)</term><term>Spike Glycoprotein, Coronavirus</term><term>Swine</term><term>Viral Envelope Proteins (chemistry)</term><term>Viral Envelope Proteins (genetics)</term><term>Viral Envelope Proteins (physiology)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Amorces ADN</term><term>Animaux</term><term>Coronavirus ()</term><term>Coronavirus (physiologie)</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>Mutagenèse dirigée</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>Substitution d'acide aminé</term><term>Suidae</term><term>Syndrome de détresse respiratoire de l'adulte (virologie)</term><term>Séquence nucléotidique</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Membrane Glycoproteins</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Membrane Glycoproteins</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="physiology" xml:lang="en"><term>Membrane Glycoproteins</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" type="chemical" xml:lang="en"><term>DNA Primers</term><term>Spike Glycoprotein, Coronavirus</term></keywords><keywords scheme="MESH" qualifier="classification" xml:lang="en"><term>Coronavirus</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Glycoprotéines membranaires</term><term>Protéines de l'enveloppe virale</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Coronavirus</term><term>Glycoprotéines membranaires</term><term>Protéines de l'enveloppe virale</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Coronavirus</term></keywords><keywords scheme="MESH" qualifier="virologie" xml:lang="fr"><term>Syndrome de détresse respiratoire de l'adulte</term></keywords><keywords scheme="MESH" qualifier="virology" xml:lang="en"><term>Respiratory Distress Syndrome, Adult</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Substitution</term><term>Animals</term><term>Base Sequence</term><term>Molecular Sequence Data</term><term>Mutagenesis, Site-Directed</term><term>Swine</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Amorces ADN</term><term>Animaux</term><term>Coronavirus</term><term>Données de séquences moléculaires</term><term>Glycoprotéine de spicule des coronavirus</term><term>Glycoprotéines membranaires</term><term>Mutagenèse dirigée</term><term>Protéines de l'enveloppe virale</term><term>Substitution d'acide aminé</term><term>Suidae</term><term>Séquence nucléotidique</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Coronaviruses (CoV) mature by a budding process at intracellular membranes. Here we showed that the major surface protein S of a porcine CoV (transmissible gastroenteritis virus) is not transported to the cell surface but is retained intracellularly. Site-directed mutagenesis indicated that a tyrosine-dependent signal (YXXI) in the cytoplasmic tail is essential for intracellular localization of the S protein. Surface expression of mutant proteins was evident by immunofluorescence analysis and surface biotinylation. Intracellularly retained S proteins only contained endoglycosidase H-sensitive N-glycans, whereas mutant proteins that migrated to the plasma membrane acquired N-linked oligosaccharides of the complex type. Corresponding tyrosine residues are present in the cytoplasmic tails of the S proteins of other animal CoV but not in the tail portion of the S protein of severe acute respiratory syndrome (SARS)-CoV. Changing the SEPV tetrapeptide in the cytoplasmic tail to YEPI resulted in intracellular retention of the S protein of SARS-CoV. As the S proteins of CoV have receptor binding and fusion activities and are the main target of neutralizing antibodies, the differences in the transport behavior of the S proteins suggest different strategies in the virus host interactions between SARS-CoV and other coronaviruses.</div></front></TEI><affiliations><list><country><li>Allemagne</li></country><region><li>Basse-Saxe</li></region><settlement><li>Hanovre</li></settlement></list><tree><noCountry><name sortKey="Al Falah, Marwan" sort="Al Falah, Marwan" uniqKey="Al Falah M" first="Marwan" last="Al-Falah">Marwan Al-Falah</name><name sortKey="Deng, Hongkui" sort="Deng, Hongkui" uniqKey="Deng H" first="Hongkui" last="Deng">Hongkui Deng</name><name sortKey="Enjuanes, Luis" sort="Enjuanes, Luis" uniqKey="Enjuanes L" first="Luis" last="Enjuanes">Luis Enjuanes</name><name sortKey="Escors, David" sort="Escors, David" uniqKey="Escors D" first="David" last="Escors">David Escors</name><name sortKey="Herrler, Georg" sort="Herrler, Georg" uniqKey="Herrler G" first="Georg" last="Herrler">Georg Herrler</name><name sortKey="Naim, Hassan Y" sort="Naim, Hassan Y" uniqKey="Naim H" first="Hassan Y" last="Naim">Hassan Y. Naim</name><name sortKey="Wang, Zai" sort="Wang, Zai" uniqKey="Wang Z" first="Zai" last="Wang">Zai Wang</name><name sortKey="Zimmer, Gert" sort="Zimmer, Gert" uniqKey="Zimmer G" first="Gert" last="Zimmer">Gert Zimmer</name></noCountry><country name="Allemagne"><region name="Basse-Saxe"><name sortKey="Schwegmann Wessels, Christel" sort="Schwegmann Wessels, Christel" uniqKey="Schwegmann Wessels C" first="Christel" last="Schwegmann-Wessels">Christel Schwegmann-Wessels</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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