The spike protein of infectious bronchitis virus is retained intracellularly by a tyrosine motif.
Identifieur interne : 002F85 ( Main/Exploration ); précédent : 002F84; suivant : 002F86The spike protein of infectious bronchitis virus is retained intracellularly by a tyrosine motif.
Auteurs : Christine Winter [Allemagne] ; Christel Schwegmann-Wessels ; Ulrich Neumann ; Georg HerrlerSource :
- Journal of virology [ 1098-5514 ] ; 2008.
Descripteurs français
- KwdFr :
- Animaux, Cellules cultivées, Cricetinae, Endocytose, Glycoprotéine de spicule des coronavirus, Glycoprotéines membranaires (), Glycoprotéines membranaires (métabolisme), Immunoprécipitation, Protéines de l'enveloppe virale (), Protéines de l'enveloppe virale (métabolisme), Technique d'immunofluorescence, Tyrosine (métabolisme), Virus de la bronchite infectieuse (métabolisme).
- MESH :
- métabolisme : Glycoprotéines membranaires, Protéines de l'enveloppe virale, Tyrosine, Virus de la bronchite infectieuse.
- Animaux, Cellules cultivées, Cricetinae, Endocytose, Glycoprotéine de spicule des coronavirus, Glycoprotéines membranaires, Immunoprécipitation, Protéines de l'enveloppe virale, Technique d'immunofluorescence.
English descriptors
- KwdEn :
- Animals, Cells, Cultured, Cricetinae, Endocytosis, Fluorescent Antibody Technique, Immunoprecipitation, Infectious bronchitis virus (metabolism), Membrane Glycoproteins (chemistry), Membrane Glycoproteins (metabolism), Spike Glycoprotein, Coronavirus, Tyrosine (metabolism), Viral Envelope Proteins (chemistry), Viral Envelope Proteins (metabolism).
- MESH :
- chemical , chemistry : Membrane Glycoproteins, Viral Envelope Proteins.
- metabolism : Infectious bronchitis virus, Membrane Glycoproteins, Tyrosine, Viral Envelope Proteins.
- Animals, Cells, Cultured, Cricetinae, Endocytosis, Fluorescent Antibody Technique, Immunoprecipitation, Spike Glycoprotein, Coronavirus.
Abstract
We have analyzed the intracellular transport of the spike (S) protein of infectious bronchitis virus (IBV), an avian coronavirus. Surface expression was analyzed by immunofluorescence microscopy, by surface biotinylation, and by syncytium formation by S-expressing cells. By applying these methods, the S protein was found to be retained intracellularly. Tyr1143 in the cytoplasmic tail was shown to be a crucial component of the retention signal. Deletion of a dilysine motif that has previously been suggested to function as a retrieval signal did not abolish intracellular retention. Treatment of the S proteins with endoglycosidases did not reveal any differences between the parental and the mutant proteins. Furthermore, all S proteins analyzed were posttranslationally cleaved into the subunits S1 and S2. In coexpression experiments, the S protein was found to colocalize with a Golgi marker. Taken together, these results indicate that the S protein of IBV is retained at a late Golgi compartment. Therefore, this viral surface protein differs from the S proteins of transmissible gastroenteritis virus and severe acute respiratory syndrome coronavirus, which are retained at a pre-Golgi compartment or transported to the cell surface, respectively. The implications of these differences are discussed.
DOI: 10.1128/JVI.02064-07
PubMed: 18094153
Affiliations:
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Christine.Winter@tiho-hannover.de</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Institut für Virologie, Tierärztliche Hochschule Hannover, Bünteweg 17, 30559 Hannover</wicri:regionArea><placeName><region type="land" nuts="2">Basse-Saxe</region><settlement type="city">Hanovre</settlement></placeName></affiliation></author><author><name sortKey="Schwegmann Wessels, Christel" sort="Schwegmann Wessels, Christel" uniqKey="Schwegmann Wessels C" first="Christel" last="Schwegmann-Wessels">Christel Schwegmann-Wessels</name></author><author><name sortKey="Neumann, Ulrich" sort="Neumann, Ulrich" uniqKey="Neumann U" first="Ulrich" last="Neumann">Ulrich Neumann</name></author><author><name sortKey="Herrler, Georg" sort="Herrler, Georg" uniqKey="Herrler G" first="Georg" last="Herrler">Georg Herrler</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2008">2008</date><idno type="RBID">pubmed:18094153</idno><idno type="pmid">18094153</idno><idno type="doi">10.1128/JVI.02064-07</idno><idno type="wicri:Area/PubMed/Corpus">001C49</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">001C49</idno><idno type="wicri:Area/PubMed/Curation">001C49</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">001C49</idno><idno type="wicri:Area/PubMed/Checkpoint">001985</idno><idno type="wicri:explorRef" wicri:stream="Checkpoint" wicri:step="PubMed">001985</idno><idno type="wicri:Area/Ncbi/Merge">001B46</idno><idno type="wicri:Area/Ncbi/Curation">001B46</idno><idno type="wicri:Area/Ncbi/Checkpoint">001B46</idno><idno type="wicri:Area/Main/Merge">003051</idno><idno type="wicri:Area/Main/Curation">002F85</idno><idno type="wicri:Area/Main/Exploration">002F85</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">The spike protein of infectious bronchitis virus is retained intracellularly by a tyrosine motif.</title><author><name sortKey="Winter, Christine" sort="Winter, Christine" uniqKey="Winter C" first="Christine" last="Winter">Christine Winter</name><affiliation wicri:level="3"><nlm:affiliation>Institut für Virologie, Tierärztliche Hochschule Hannover, Bünteweg 17, 30559 Hannover, Germany. Christine.Winter@tiho-hannover.de</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Institut für Virologie, Tierärztliche Hochschule Hannover, Bünteweg 17, 30559 Hannover</wicri:regionArea><placeName><region type="land" nuts="2">Basse-Saxe</region><settlement type="city">Hanovre</settlement></placeName></affiliation></author><author><name sortKey="Schwegmann Wessels, Christel" sort="Schwegmann Wessels, Christel" uniqKey="Schwegmann Wessels C" first="Christel" last="Schwegmann-Wessels">Christel Schwegmann-Wessels</name></author><author><name sortKey="Neumann, Ulrich" sort="Neumann, Ulrich" uniqKey="Neumann U" first="Ulrich" last="Neumann">Ulrich Neumann</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">Journal of virology</title><idno type="eISSN">1098-5514</idno><imprint><date when="2008" type="published">2008</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term><term>Cells, Cultured</term><term>Cricetinae</term><term>Endocytosis</term><term>Fluorescent Antibody Technique</term><term>Immunoprecipitation</term><term>Infectious bronchitis virus (metabolism)</term><term>Membrane Glycoproteins (chemistry)</term><term>Membrane Glycoproteins (metabolism)</term><term>Spike Glycoprotein, Coronavirus</term><term>Tyrosine (metabolism)</term><term>Viral Envelope Proteins (chemistry)</term><term>Viral Envelope Proteins (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux</term><term>Cellules cultivées</term><term>Cricetinae</term><term>Endocytose</term><term>Glycoprotéine de spicule des coronavirus</term><term>Glycoprotéines membranaires ()</term><term>Glycoprotéines membranaires (métabolisme)</term><term>Immunoprécipitation</term><term>Protéines de l'enveloppe virale ()</term><term>Protéines de l'enveloppe virale (métabolisme)</term><term>Technique d'immunofluorescence</term><term>Tyrosine (métabolisme)</term><term>Virus de la bronchite infectieuse (métabolisme)</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" qualifier="metabolism" xml:lang="en"><term>Infectious bronchitis virus</term><term>Membrane Glycoproteins</term><term>Tyrosine</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Glycoprotéines membranaires</term><term>Protéines de l'enveloppe virale</term><term>Tyrosine</term><term>Virus de la bronchite infectieuse</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Cells, Cultured</term><term>Cricetinae</term><term>Endocytosis</term><term>Fluorescent Antibody Technique</term><term>Immunoprecipitation</term><term>Spike Glycoprotein, Coronavirus</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Cellules cultivées</term><term>Cricetinae</term><term>Endocytose</term><term>Glycoprotéine de spicule des coronavirus</term><term>Glycoprotéines membranaires</term><term>Immunoprécipitation</term><term>Protéines de l'enveloppe virale</term><term>Technique d'immunofluorescence</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">We have analyzed the intracellular transport of the spike (S) protein of infectious bronchitis virus (IBV), an avian coronavirus. Surface expression was analyzed by immunofluorescence microscopy, by surface biotinylation, and by syncytium formation by S-expressing cells. By applying these methods, the S protein was found to be retained intracellularly. Tyr1143 in the cytoplasmic tail was shown to be a crucial component of the retention signal. Deletion of a dilysine motif that has previously been suggested to function as a retrieval signal did not abolish intracellular retention. Treatment of the S proteins with endoglycosidases did not reveal any differences between the parental and the mutant proteins. Furthermore, all S proteins analyzed were posttranslationally cleaved into the subunits S1 and S2. In coexpression experiments, the S protein was found to colocalize with a Golgi marker. Taken together, these results indicate that the S protein of IBV is retained at a late Golgi compartment. Therefore, this viral surface protein differs from the S proteins of transmissible gastroenteritis virus and severe acute respiratory syndrome coronavirus, which are retained at a pre-Golgi compartment or transported to the cell surface, respectively. The implications of these differences are discussed.</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="Herrler, Georg" sort="Herrler, Georg" uniqKey="Herrler G" first="Georg" last="Herrler">Georg Herrler</name><name sortKey="Neumann, Ulrich" sort="Neumann, Ulrich" uniqKey="Neumann U" first="Ulrich" last="Neumann">Ulrich Neumann</name><name sortKey="Schwegmann Wessels, Christel" sort="Schwegmann Wessels, Christel" uniqKey="Schwegmann Wessels C" first="Christel" last="Schwegmann-Wessels">Christel Schwegmann-Wessels</name></noCountry><country name="Allemagne"><region name="Basse-Saxe"><name sortKey="Winter, Christine" sort="Winter, Christine" uniqKey="Winter C" first="Christine" last="Winter">Christine Winter</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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