The Severe Acute Respiratory Syndrome (SARS)-coronavirus 3a protein may function as a modulator of the trafficking properties of the spike protein
Identifieur interne : 001210 ( Pmc/Checkpoint ); précédent : 001209; suivant : 001211The 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.
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
Affiliations:
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<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>
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<series><title level="j">Virology Journal</title>
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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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<pmc article-type="research-article"><pmc-dir>properties open_access</pmc-dir>
<front><journal-meta><journal-id journal-id-type="nlm-ta">Virol J</journal-id>
<journal-id journal-id-type="iso-abbrev">Virol. J</journal-id>
<journal-title-group><journal-title>Virology Journal</journal-title>
</journal-title-group>
<issn pub-type="epub">1743-422X</issn>
<publisher><publisher-name>BioMed Central</publisher-name>
<publisher-loc>London</publisher-loc>
</publisher>
</journal-meta>
<article-meta><article-id pub-id-type="pmid">15703085</article-id>
<article-id pub-id-type="pmc">549520</article-id>
<article-id pub-id-type="publisher-id">20</article-id>
<article-id pub-id-type="doi">10.1186/1743-422X-2-5</article-id>
<article-categories><subj-group subj-group-type="heading"><subject>Hypothesis</subject>
</subj-group>
</article-categories>
<title-group><article-title>The Severe Acute Respiratory Syndrome (SARS)-coronavirus 3a protein may function as a modulator of the trafficking properties of the spike protein</article-title>
</title-group>
<contrib-group><contrib contrib-type="author" corresp="yes"><name><surname>Tan</surname>
<given-names>Yee-Joo</given-names>
</name>
<address><email>mcbtanyj@imcb.a-star.edu.sg</email>
</address>
<xref ref-type="aff" rid="Aff1"></xref>
</contrib>
<aff id="Aff1"><institution-wrap><institution-id institution-id-type="GRID">grid.418812.6</institution-id>
<institution>Institute of Molecular and Cell Biology,</institution>
<institution>Institute of Molecular and Cell Biology,</institution>
</institution-wrap>
61 Biopolis Drive, Proteos, 138673 Singapore</aff>
</contrib-group>
<pub-date pub-type="epub"><day>10</day>
<month>2</month>
<year>2005</year>
</pub-date>
<pub-date pub-type="pmc-release"><day>10</day>
<month>2</month>
<year>2005</year>
</pub-date>
<pub-date pub-type="collection"><year>2005</year>
</pub-date>
<volume>2</volume>
<elocation-id>5</elocation-id>
<history><date date-type="received"><day>17</day>
<month>1</month>
<year>2005</year>
</date>
<date date-type="accepted"><day>10</day>
<month>2</month>
<year>2005</year>
</date>
</history>
<permissions><copyright-statement>© Tan; licensee BioMed Central Ltd. 2005</copyright-statement>
<license><license-p>This article is made available via the PMC Open Access Subset for unrestricted research re-use and secondary analysis in any form or by any means with acknowledgement of the original source. These permissions are granted for the duration of the World Health Organization (WHO) declaration of COVID-19 as a global pandemic.</license-p>
</license>
</permissions>
<abstract id="Abs1"><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>
</abstract>
<kwd-group xml:lang="en"><title>Keywords</title>
<kwd>Severe Acute Respiratory Syndrome</kwd>
<kwd>Cell Surface Expression</kwd>
<kwd>Cytoplasmic Tail</kwd>
<kwd>Severe Acute Respiratory Syndrome</kwd>
<kwd>Spike Protein</kwd>
</kwd-group>
<custom-meta-group><custom-meta><meta-name>issue-copyright-statement</meta-name>
<meta-value>© The Author(s) 2005</meta-value>
</custom-meta>
</custom-meta-group>
</article-meta>
</front>
</pmc>
<affiliations><list></list>
<tree><noCountry><name sortKey="Tan, Yee Joo" sort="Tan, Yee Joo" uniqKey="Tan Y" first="Yee-Joo" last="Tan">Yee-Joo Tan</name>
</noCountry>
</tree>
</affiliations>
</record>
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