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The severe acute respiratory syndrome coronavirus 3a is a novel structural protein

Identifieur interne : 000E26 ( Pmc/Curation ); précédent : 000E25; suivant : 000E27

The severe acute respiratory syndrome coronavirus 3a is a novel structural protein

Auteurs : Shuo Shen [Singapour] ; Pi-Shiu Lin [République populaire de Chine] ; Yu-Chan Chao [République populaire de Chine] ; Aihua Zhang [République populaire de Chine] ; Xiaoming Yang [République populaire de Chine] ; Seng Gee Lim [Singapour] ; Wanjin Hong [Singapour] ; Yee-Joo Tan [Singapour]

Source :

RBID : PMC:7092867

Abstract

The severe acute respiratory syndrome coronavirus (SARS-CoV) 3a protein is one of the opening reading frames in the viral genome with no homologue in other known coronaviruses. Expression of the 3a protein has been demonstrated during both in vitro and in vivo infection. Here we present biochemical data to show that 3a is a novel coronavirus structural protein. 3a was detected in virions purified from SARS-CoV infected Vero E6 cells although two truncated products were present predominantly instead of the full-length protein. In Vero E6 cells transiently transfected with a cDNA construct for expressing 3a, a similar cleavage was observed. Furthermore, co-expression of 3a, membrane and envelope proteins using the baculovirus system showed that both full-length and truncated 3a can be assembled into virus-like particles. This is the first report that demonstrated the incorporation of 3a into virion and showed that the SARS-CoV encodes a novel coronavirus structural protein.


Url:
DOI: 10.1016/j.bbrc.2005.02.153
PubMed: 15781262
PubMed Central: 7092867

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PMC:7092867

Le document en format XML

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<p>The severe acute respiratory syndrome coronavirus (SARS-CoV) 3a protein is one of the opening reading frames in the viral genome with no homologue in other known coronaviruses. Expression of the 3a protein has been demonstrated during both in vitro and in vivo infection. Here we present biochemical data to show that 3a is a novel coronavirus structural protein. 3a was detected in virions purified from SARS-CoV infected Vero E6 cells although two truncated products were present predominantly instead of the full-length protein. In Vero E6 cells transiently transfected with a cDNA construct for expressing 3a, a similar cleavage was observed. Furthermore, co-expression of 3a, membrane and envelope proteins using the baculovirus system showed that both full-length and truncated 3a can be assembled into virus-like particles. This is the first report that demonstrated the incorporation of 3a into virion and showed that the SARS-CoV encodes a novel coronavirus structural protein.</p>
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</back>
</TEI>
<pmc article-type="research-article">
<pmc-dir>properties open_access</pmc-dir>
<front>
<journal-meta>
<journal-id journal-id-type="nlm-ta">Biochem Biophys Res Commun</journal-id>
<journal-id journal-id-type="iso-abbrev">Biochem. Biophys. Res. Commun</journal-id>
<journal-title-group>
<journal-title>Biochemical and Biophysical Research Communications</journal-title>
</journal-title-group>
<issn pub-type="ppub">0006-291X</issn>
<issn pub-type="epub">1090-2104</issn>
<publisher>
<publisher-name>Elsevier Inc.</publisher-name>
</publisher>
</journal-meta>
<article-meta>
<article-id pub-id-type="pmid">15781262</article-id>
<article-id pub-id-type="pmc">7092867</article-id>
<article-id pub-id-type="publisher-id">S0006-291X(05)00402-X</article-id>
<article-id pub-id-type="doi">10.1016/j.bbrc.2005.02.153</article-id>
<article-categories>
<subj-group subj-group-type="heading">
<subject>Article</subject>
</subj-group>
</article-categories>
<title-group>
<article-title>The severe acute respiratory syndrome coronavirus 3a is a novel structural protein</article-title>
</title-group>
<contrib-group>
<contrib contrib-type="author">
<name>
<surname>Shen</surname>
<given-names>Shuo</given-names>
</name>
<xref rid="aff1" ref-type="aff">a</xref>
<xref rid="fn1" ref-type="fn">1</xref>
</contrib>
<contrib contrib-type="author">
<name>
<surname>Lin</surname>
<given-names>Pi-Shiu</given-names>
</name>
<xref rid="aff2" ref-type="aff">b</xref>
<xref rid="fn1" ref-type="fn">1</xref>
</contrib>
<contrib contrib-type="author">
<name>
<surname>Chao</surname>
<given-names>Yu-Chan</given-names>
</name>
<xref rid="aff2" ref-type="aff">b</xref>
</contrib>
<contrib contrib-type="author">
<name>
<surname>Zhang</surname>
<given-names>Aihua</given-names>
</name>
<xref rid="aff3" ref-type="aff">c</xref>
</contrib>
<contrib contrib-type="author">
<name>
<surname>Yang</surname>
<given-names>Xiaoming</given-names>
</name>
<xref rid="aff3" ref-type="aff">c</xref>
</contrib>
<contrib contrib-type="author">
<name>
<surname>Lim</surname>
<given-names>Seng Gee</given-names>
</name>
<xref rid="aff1" ref-type="aff">a</xref>
</contrib>
<contrib contrib-type="author">
<name>
<surname>Hong</surname>
<given-names>Wanjin</given-names>
</name>
<xref rid="aff1" ref-type="aff">a</xref>
</contrib>
<contrib contrib-type="author">
<name>
<surname>Tan</surname>
<given-names>Yee-Joo</given-names>
</name>
<email>mcbtanyj@imcb.a-star.edu.sg</email>
<xref rid="aff1" ref-type="aff">a</xref>
<xref rid="cor1" ref-type="corresp"></xref>
</contrib>
</contrib-group>
<aff id="aff1">
<label>a</label>
Institute of Molecular and Cell Biology, 61 Biopolis Drive, Proteos, Singapore 138673, Singapore</aff>
<aff id="aff2">
<label>b</label>
Institute of Molecular Biology, Academia Sinica, Nankang, Taipei 115, Taiwan, ROC</aff>
<aff id="aff3">
<label>c</label>
Wuhan Institute of Biological Products, Wuhan 430060, PR China</aff>
<author-notes>
<corresp id="cor1">
<label></label>
Corresponding author. Fax: + 65 67791117
<email>mcbtanyj@imcb.a-star.edu.sg</email>
</corresp>
<fn id="fn1">
<label>1</label>
<p>These authors contributed equally to this work.</p>
</fn>
</author-notes>
<pub-date pub-type="pmc-release">
<day>5</day>
<month>3</month>
<year>2005</year>
</pub-date>
<pmc-comment> PMC Release delay is 0 months and 0 days and was based on .</pmc-comment>
<pub-date pub-type="ppub">
<day>29</day>
<month>4</month>
<year>2005</year>
</pub-date>
<pub-date pub-type="epub">
<day>5</day>
<month>3</month>
<year>2005</year>
</pub-date>
<volume>330</volume>
<issue>1</issue>
<fpage>286</fpage>
<lpage>292</lpage>
<history>
<date date-type="received">
<day>18</day>
<month>2</month>
<year>2005</year>
</date>
</history>
<permissions>
<copyright-statement>Copyright © 2005 Elsevier Inc. All rights reserved.</copyright-statement>
<copyright-year>2005</copyright-year>
<copyright-holder>Elsevier Inc.</copyright-holder>
<license>
<license-p>Since January 2020 Elsevier has created a COVID-19 resource centre with free information in English and Mandarin on the novel coronavirus COVID-19. The COVID-19 resource centre is hosted on Elsevier Connect, the company's public news and information website. Elsevier hereby grants permission to make all its COVID-19-related research that is available on the COVID-19 resource centre - including this research content - immediately available in PubMed Central and other publicly funded repositories, such as the WHO COVID database with rights for unrestricted research re-use and analyses in any form or by any means with acknowledgement of the original source. These permissions are granted for free by Elsevier for as long as the COVID-19 resource centre remains active.</license-p>
</license>
</permissions>
<abstract>
<p>The severe acute respiratory syndrome coronavirus (SARS-CoV) 3a protein is one of the opening reading frames in the viral genome with no homologue in other known coronaviruses. Expression of the 3a protein has been demonstrated during both in vitro and in vivo infection. Here we present biochemical data to show that 3a is a novel coronavirus structural protein. 3a was detected in virions purified from SARS-CoV infected Vero E6 cells although two truncated products were present predominantly instead of the full-length protein. In Vero E6 cells transiently transfected with a cDNA construct for expressing 3a, a similar cleavage was observed. Furthermore, co-expression of 3a, membrane and envelope proteins using the baculovirus system showed that both full-length and truncated 3a can be assembled into virus-like particles. This is the first report that demonstrated the incorporation of 3a into virion and showed that the SARS-CoV encodes a novel coronavirus structural protein.</p>
</abstract>
<kwd-group>
<title>Keywords</title>
<kwd>Severe acute respiratory syndrome</kwd>
<kwd>SARS coronavirus</kwd>
<kwd>3a viral protein</kwd>
<kwd>Structural protein</kwd>
<kwd>Baculovirus</kwd>
<kwd>Virus-like particles</kwd>
</kwd-group>
</article-meta>
</front>
</pmc>
</record>

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