The Severe Acute Respiratory Syndrome (SARS)-coronavirus 3a protein may function as a modulator of the trafficking properties of the spike protein
Identifieur interne : 000D74 ( Ncbi/Merge ); précédent : 000D73; suivant : 000D75The Severe Acute Respiratory Syndrome (SARS)-coronavirus 3a protein may function as a modulator of the trafficking properties of the spike protein
Auteurs : Yee-Joo TanSource :
- Virology Journal [ 1743-422X ] ; 2005.
Descripteurs français
- KwdFr :
- Glycoprotéine de spicule des coronavirus, Glycoprotéines membranaires (génétique), Glycoprotéines membranaires (métabolisme), Protéines de l'enveloppe virale (génétique), Protéines de l'enveloppe virale (métabolisme), Protéines virales (génétique), Protéines virales (métabolisme), Régulation de l'expression des gènes viraux, Réplication virale, Transport de protéines, Virus du SRAS (génétique), Virus du SRAS (métabolisme).
- MESH :
- génétique : Glycoprotéines membranaires, Protéines de l'enveloppe virale, Protéines virales, Virus du SRAS.
- métabolisme : Glycoprotéines membranaires, Protéines de l'enveloppe virale, Protéines virales, Virus du SRAS.
- Glycoprotéine de spicule des coronavirus, Régulation de l'expression des gènes viraux, Réplication virale, Transport de protéines.
English descriptors
- KwdEn :
- Gene Expression Regulation, Viral, Membrane Glycoproteins (genetics), Membrane Glycoproteins (metabolism), Protein Transport, SARS Virus (genetics), SARS Virus (metabolism), Spike Glycoprotein, Coronavirus, Viral Envelope Proteins (genetics), Viral Envelope Proteins (metabolism), Viral Proteins (genetics), Viral Proteins (metabolism), Virus Replication.
- MESH :
- chemical , genetics : Membrane Glycoproteins, Viral Envelope Proteins, Viral Proteins.
- chemical , metabolism : Membrane Glycoproteins, Viral Envelope Proteins, Viral Proteins.
- genetics : SARS Virus.
- metabolism : SARS Virus.
- Gene Expression Regulation, Viral, Protein Transport, Spike Glycoprotein, Coronavirus, Virus Replication.
Abstract
A recent publication reported that a tyrosine-dependent sorting signal, present in cytoplasmic tail of the spike protein of most coronaviruses, mediates the intracellular retention of the spike protein. This motif is missing from the spike protein of the severe acute respiratory syndrome-coronavirus (SARS-CoV), resulting in high level of surface expression of the spike protein when it is expressed on its own
It has been shown that the severe acute respiratory syndrome-coronavirus genome contains open reading frames that encode for proteins with no homologue in other coronaviruses. One of them is the 3a protein, which is expressed during infection
The effects of 3a on the internalization of cell surface spike protein can be examined biochemically and the significance of the interplay between these two viral proteins during viral infection can be studied using reverse genetics methodology.
If this hypothesis is proven, it will indicate that the severe acute respiratory syndrome-coronavirus modulates the surface expression of the spike protein via a different mechanism from other coronaviruses. The interaction between 3a and S, which are expressed from separate subgenomic RNA, would be important for controlling the trafficking properties of S. The cell surface expression of S in infected cells significantly impacts viral assembly, viral spread and viral pathogenesis. Modulation by this unique pathway could confer certain advantages during the replication of the severe acute respiratory syndrome-coronavirus.
Url:
DOI: 10.1186/1743-422X-2-5
PubMed: 15703085
PubMed Central: 549520
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Links to Exploration step
PMC:549520Le document en format XML
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<term>Membrane Glycoproteins (genetics)</term>
<term>Membrane Glycoproteins (metabolism)</term>
<term>Protein Transport</term>
<term>SARS Virus (genetics)</term>
<term>SARS Virus (metabolism)</term>
<term>Spike Glycoprotein, Coronavirus</term>
<term>Viral Envelope Proteins (genetics)</term>
<term>Viral Envelope Proteins (metabolism)</term>
<term>Viral Proteins (genetics)</term>
<term>Viral Proteins (metabolism)</term>
<term>Virus Replication</term>
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<term>Glycoprotéines membranaires (génétique)</term>
<term>Glycoprotéines membranaires (métabolisme)</term>
<term>Protéines de l'enveloppe virale (génétique)</term>
<term>Protéines de l'enveloppe virale (métabolisme)</term>
<term>Protéines virales (génétique)</term>
<term>Protéines virales (métabolisme)</term>
<term>Régulation de l'expression des gènes viraux</term>
<term>Réplication virale</term>
<term>Transport de protéines</term>
<term>Virus du SRAS (génétique)</term>
<term>Virus du SRAS (métabolisme)</term>
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<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Membrane Glycoproteins</term>
<term>Viral Envelope Proteins</term>
<term>Viral Proteins</term>
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<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Membrane Glycoproteins</term>
<term>Viral Envelope Proteins</term>
<term>Viral Proteins</term>
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<keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>SARS Virus</term>
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<keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Glycoprotéines membranaires</term>
<term>Protéines de l'enveloppe virale</term>
<term>Protéines virales</term>
<term>Virus du SRAS</term>
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<term>Protéines de l'enveloppe virale</term>
<term>Protéines virales</term>
<term>Virus du SRAS</term>
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<front><div type="abstract" xml:lang="en"><sec><title>Background</title>
<p>A recent publication reported that a tyrosine-dependent sorting signal, present in cytoplasmic tail of the spike protein of most coronaviruses, mediates the intracellular retention of the spike protein. This motif is missing from the spike protein of the severe acute respiratory syndrome-coronavirus (SARS-CoV), resulting in high level of surface expression of the spike protein when it is expressed on its own <italic>in vitro</italic>
.</p>
</sec>
<sec><title>Presentation of the hypothesis</title>
<p>It has been shown that the severe acute respiratory syndrome-coronavirus genome contains open reading frames that encode for proteins with no homologue in other coronaviruses. One of them is the 3a protein, which is expressed during infection <italic>in vitro</italic>
and <italic>in vivo</italic>
. The 3a protein, which contains a tyrosine-dependent sorting signal in its cytoplasmic domain, is expressed on the cell surface and can undergo internalization. In addition, 3a can bind to the spike protein and through this interaction, it may be able to cause the spike protein to become internalized, resulting in a decrease in its surface expression.</p>
</sec>
<sec><title>Testing the hypothesis</title>
<p>The effects of 3a on the internalization of cell surface spike protein can be examined biochemically and the significance of the interplay between these two viral proteins during viral infection can be studied using reverse genetics methodology.</p>
</sec>
<sec><title>Implication of the hypothesis</title>
<p>If this hypothesis is proven, it will indicate that the severe acute respiratory syndrome-coronavirus modulates the surface expression of the spike protein via a different mechanism from other coronaviruses. The interaction between 3a and S, which are expressed from separate subgenomic RNA, would be important for controlling the trafficking properties of S. The cell surface expression of S in infected cells significantly impacts viral assembly, viral spread and viral pathogenesis. Modulation by this unique pathway could confer certain advantages during the replication of the severe acute respiratory syndrome-coronavirus.</p>
</sec>
</div>
</front>
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<double pmid="15703085"><pmc><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">The Severe Acute Respiratory Syndrome (SARS)-coronavirus 3a protein may function as a modulator of the trafficking properties of the spike protein</title>
<author><name sortKey="Tan, Yee Joo" sort="Tan, Yee Joo" uniqKey="Tan Y" first="Yee-Joo" last="Tan">Yee-Joo Tan</name>
<affiliation><nlm:aff id="Aff1"></nlm:aff>
</affiliation>
</author>
</titleStmt>
<publicationStmt><idno type="wicri:source">PMC</idno>
<idno type="pmid">15703085</idno>
<idno type="pmc">549520</idno>
<idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC549520</idno>
<idno type="RBID">PMC:549520</idno>
<idno type="doi">10.1186/1743-422X-2-5</idno>
<date when="2005">2005</date>
<idno type="wicri:Area/Pmc/Corpus">000490</idno>
<idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">000490</idno>
<idno type="wicri:Area/Pmc/Curation">000490</idno>
<idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Curation">000490</idno>
<idno type="wicri:Area/Pmc/Checkpoint">001210</idno>
<idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Checkpoint">001210</idno>
</publicationStmt>
<sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">The Severe Acute Respiratory Syndrome (SARS)-coronavirus 3a protein may function as a modulator of the trafficking properties of the spike protein</title>
<author><name sortKey="Tan, Yee Joo" sort="Tan, Yee Joo" uniqKey="Tan Y" first="Yee-Joo" last="Tan">Yee-Joo Tan</name>
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<series><title level="j">Virology Journal</title>
<idno type="eISSN">1743-422X</idno>
<imprint><date when="2005">2005</date>
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<front><div type="abstract" xml:lang="en"><sec><title>Background</title>
<p>A recent publication reported that a tyrosine-dependent sorting signal, present in cytoplasmic tail of the spike protein of most coronaviruses, mediates the intracellular retention of the spike protein. This motif is missing from the spike protein of the severe acute respiratory syndrome-coronavirus (SARS-CoV), resulting in high level of surface expression of the spike protein when it is expressed on its own <italic>in vitro</italic>
.</p>
</sec>
<sec><title>Presentation of the hypothesis</title>
<p>It has been shown that the severe acute respiratory syndrome-coronavirus genome contains open reading frames that encode for proteins with no homologue in other coronaviruses. One of them is the 3a protein, which is expressed during infection <italic>in vitro</italic>
and <italic>in vivo</italic>
. The 3a protein, which contains a tyrosine-dependent sorting signal in its cytoplasmic domain, is expressed on the cell surface and can undergo internalization. In addition, 3a can bind to the spike protein and through this interaction, it may be able to cause the spike protein to become internalized, resulting in a decrease in its surface expression.</p>
</sec>
<sec><title>Testing the hypothesis</title>
<p>The effects of 3a on the internalization of cell surface spike protein can be examined biochemically and the significance of the interplay between these two viral proteins during viral infection can be studied using reverse genetics methodology.</p>
</sec>
<sec><title>Implication of the hypothesis</title>
<p>If this hypothesis is proven, it will indicate that the severe acute respiratory syndrome-coronavirus modulates the surface expression of the spike protein via a different mechanism from other coronaviruses. The interaction between 3a and S, which are expressed from separate subgenomic RNA, would be important for controlling the trafficking properties of S. The cell surface expression of S in infected cells significantly impacts viral assembly, viral spread and viral pathogenesis. Modulation by this unique pathway could confer certain advantages during the replication of the severe acute respiratory syndrome-coronavirus.</p>
</sec>
</div>
</front>
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<pubmed><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">The Severe Acute Respiratory Syndrome (SARS)-coronavirus 3a protein may function as a modulator of the trafficking properties of the spike protein.</title>
<author><name sortKey="Tan, Yee Joo" sort="Tan, Yee Joo" uniqKey="Tan Y" first="Yee-Joo" last="Tan">Yee-Joo Tan</name>
<affiliation wicri:level="1"><nlm:affiliation>Institute of Molecular and Cell Biology, 61 Biopolis Drive, Proteos, 138673 Singapore. mcbtanyj@imcb.a-star.edu.sg</nlm:affiliation>
<country xml:lang="fr">Singapour</country>
<wicri:regionArea>Institute of Molecular and Cell Biology, 61 Biopolis Drive, Proteos</wicri:regionArea>
<wicri:noRegion>Proteos</wicri:noRegion>
</affiliation>
</author>
</titleStmt>
<publicationStmt><idno type="wicri:source">PubMed</idno>
<date when="2005">2005</date>
<idno type="RBID">pubmed:15703085</idno>
<idno type="pmid">15703085</idno>
<idno type="doi">10.1186/1743-422X-2-5</idno>
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<sourceDesc><biblStruct><analytic><title xml:lang="en">The Severe Acute Respiratory Syndrome (SARS)-coronavirus 3a protein may function as a modulator of the trafficking properties of the spike protein.</title>
<author><name sortKey="Tan, Yee Joo" sort="Tan, Yee Joo" uniqKey="Tan Y" first="Yee-Joo" last="Tan">Yee-Joo Tan</name>
<affiliation wicri:level="1"><nlm:affiliation>Institute of Molecular and Cell Biology, 61 Biopolis Drive, Proteos, 138673 Singapore. mcbtanyj@imcb.a-star.edu.sg</nlm:affiliation>
<country xml:lang="fr">Singapour</country>
<wicri:regionArea>Institute of Molecular and Cell Biology, 61 Biopolis Drive, Proteos</wicri:regionArea>
<wicri:noRegion>Proteos</wicri:noRegion>
</affiliation>
</author>
</analytic>
<series><title level="j">Virology journal</title>
<idno type="eISSN">1743-422X</idno>
<imprint><date when="2005" type="published">2005</date>
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Gene Expression Regulation, Viral</term>
<term>Membrane Glycoproteins (genetics)</term>
<term>Membrane Glycoproteins (metabolism)</term>
<term>Protein Transport</term>
<term>SARS Virus (genetics)</term>
<term>SARS Virus (metabolism)</term>
<term>Spike Glycoprotein, Coronavirus</term>
<term>Viral Envelope Proteins (genetics)</term>
<term>Viral Envelope Proteins (metabolism)</term>
<term>Viral Proteins (genetics)</term>
<term>Viral Proteins (metabolism)</term>
<term>Virus Replication</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Glycoprotéine de spicule des coronavirus</term>
<term>Glycoprotéines membranaires (génétique)</term>
<term>Glycoprotéines membranaires (métabolisme)</term>
<term>Protéines de l'enveloppe virale (génétique)</term>
<term>Protéines de l'enveloppe virale (métabolisme)</term>
<term>Protéines virales (génétique)</term>
<term>Protéines virales (métabolisme)</term>
<term>Régulation de l'expression des gènes viraux</term>
<term>Réplication virale</term>
<term>Transport de protéines</term>
<term>Virus du SRAS (génétique)</term>
<term>Virus du SRAS (métabolisme)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Membrane Glycoproteins</term>
<term>Viral Envelope Proteins</term>
<term>Viral Proteins</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Membrane Glycoproteins</term>
<term>Viral Envelope Proteins</term>
<term>Viral Proteins</term>
</keywords>
<keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>SARS Virus</term>
</keywords>
<keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Glycoprotéines membranaires</term>
<term>Protéines de l'enveloppe virale</term>
<term>Protéines virales</term>
<term>Virus du SRAS</term>
</keywords>
<keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>SARS Virus</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Glycoprotéines membranaires</term>
<term>Protéines de l'enveloppe virale</term>
<term>Protéines virales</term>
<term>Virus du SRAS</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Gene Expression Regulation, Viral</term>
<term>Protein Transport</term>
<term>Spike Glycoprotein, Coronavirus</term>
<term>Virus Replication</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Glycoprotéine de spicule des coronavirus</term>
<term>Régulation de l'expression des gènes viraux</term>
<term>Réplication virale</term>
<term>Transport de protéines</term>
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<front><div type="abstract" xml:lang="en">A recent publication reported that a tyrosine-dependent sorting signal, present in cytoplasmic tail of the spike protein of most coronaviruses, mediates the intracellular retention of the spike protein. This motif is missing from the spike protein of the severe acute respiratory syndrome-coronavirus (SARS-CoV), resulting in high level of surface expression of the spike protein when it is expressed on its own in vitro.</div>
</front>
</TEI>
</pubmed>
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