SrasV1, PubMed, Checkpoint, bibRecord, 001985

The spike protein of infectious bronchitis virus is retained intracellularly by a tyrosine motif.

Identifieur interne : 001985 ( PubMed/Checkpoint ); précédent : 001984; suivant : 001986

The spike protein of infectious bronchitis virus is retained intracellularly by a tyrosine motif.

Auteurs : Christine Winter [Allemagne] ; Christel Schwegmann-Wessels ; Ulrich Neumann ; Georg Herrler

Source :

Journal of virology [ 1098-5514 ] ; 2008.

RBID : pubmed:18094153

Descripteurs français

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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Le document en format XML

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<term>Immunoprecipitation</term>
<term>Infectious bronchitis virus (metabolism)</term>
<term>Membrane Glycoproteins (chemistry)</term>
<term>Membrane Glycoproteins (metabolism)</term>
<term>Spike Glycoprotein, Coronavirus</term>
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<term>Viral Envelope Proteins (metabolism)</term>
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<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>
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<term>Viral Envelope Proteins</term>
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<term>Viral Envelope Proteins</term>
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<term>Immunoprecipitation</term>
<term>Spike Glycoprotein, Coronavirus</term>
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<term>Glycoprotéines membranaires</term>
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<term>Protéines de l'enveloppe virale</term>
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<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>
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The spike protein of infectious bronchitis virus is retained intracellularly by a tyrosine motif.

The spike protein of infectious bronchitis virus is retained intracellularly by a tyrosine motif.

Source :

Descripteurs français

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Abstract

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Links to Exploration step

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Pour manipuler ce document sous Unix (Dilib)

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