Coronavirus Envelope (E) Protein Remains at the Site of Assembly
Identifieur interne : 000742 ( Pmc/Corpus ); précédent : 000741; suivant : 000743Coronavirus Envelope (E) Protein Remains at the Site of Assembly
Auteurs : Pavithra Venkatagopalan ; Sasha M. Daskalova ; Lisa A. Lopez ; Kelly A. Dolezal ; Brenda G. HogueSource :
- Virology [ 0042-6822 ] ; 2015.
Abstract
Coronaviruses (CoVs) assemble at endoplasmic reticulum Golgi intermediate compartment (ERGIC) membranes and egress from cells in cargo vesicles. Only a few molecules of the envelope (E) protein are assembled into virions. The role of E in morphogenesis is not fully understood. The cellular localization and dynamics of mouse hepatitis CoV A59 (MHV) E protein were investigated to further understanding of its role during infection. E protein localized in the ERGIC and Golgi with the amino and carboxy termini in the lumen and cytoplasm, respectively. E protein does not traffic to the cell surface. MHV was genetically engineered with a tetracysteine tag at the carboxy end of E. Fluorescence recovery after photobleaching (FRAP) showed that E is mobile in ERGIC/Golgi membranes. Correlative light electron microscopy (CLEM) confirmed the presence of E in Golgi cisternae. The results provide strong support that E proteins carry out their function(s) at the site of budding/assembly.
Url:
DOI: 10.1016/j.virol.2015.02.005
PubMed: 25726972
PubMed Central: 4550588
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PMC:4550588Le document en format XML
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<author><name sortKey="Venkatagopalan, Pavithra" sort="Venkatagopalan, Pavithra" uniqKey="Venkatagopalan P" first="Pavithra" last="Venkatagopalan">Pavithra Venkatagopalan</name>
<affiliation><nlm:aff id="A1">The Biodesign Institute, Center for Infectious Diseases and Vaccinology, Arizona State University, Tempe AZ 85287-5401</nlm:aff>
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<affiliation><nlm:aff id="A2">School of Life Sciences, Arizona State University, Tempe AZ 85287-5401</nlm:aff>
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<affiliation><nlm:aff id="A4">Microbiology Graduate Program, Arizona State University, Tempe AZ 85287-5401</nlm:aff>
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<front><div type="abstract" xml:lang="en"><p id="P2">Coronaviruses (CoVs) assemble at endoplasmic reticulum Golgi intermediate compartment (ERGIC) membranes and egress from cells in cargo vesicles. Only a few molecules of the envelope (E) protein are assembled into virions. The role of E in morphogenesis is not fully understood. The cellular localization and dynamics of mouse hepatitis CoV A59 (MHV) E protein were investigated to further understanding of its role during infection. E protein localized in the ERGIC and Golgi with the amino and carboxy termini in the lumen and cytoplasm, respectively. E protein does not traffic to the cell surface. MHV was genetically engineered with a tetracysteine tag at the carboxy end of E. Fluorescence recovery after photobleaching (FRAP) showed that E is mobile in ERGIC/Golgi membranes. Correlative light electron microscopy (CLEM) confirmed the presence of E in Golgi cisternae. The results provide strong support that E proteins carry out their function(s) at the site of budding/assembly.</p>
</div>
</front>
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<pmc article-type="research-article"><pmc-comment>The publisher of this article does not allow downloading of the full text in XML form.</pmc-comment>
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<front><journal-meta><journal-id journal-id-type="nlm-journal-id">0110674</journal-id>
<journal-id journal-id-type="pubmed-jr-id">8015</journal-id>
<journal-id journal-id-type="nlm-ta">Virology</journal-id>
<journal-id journal-id-type="iso-abbrev">Virology</journal-id>
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<article-id pub-id-type="manuscript">NIHMS668555</article-id>
<article-categories><subj-group subj-group-type="heading"><subject>Article</subject>
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<title-group><article-title>Coronavirus Envelope (E) Protein Remains at the Site of Assembly</article-title>
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<contrib-group><contrib contrib-type="author"><name><surname>Venkatagopalan</surname>
<given-names>Pavithra</given-names>
</name>
<xref ref-type="aff" rid="A1">1</xref>
<xref ref-type="aff" rid="A2">2</xref>
<xref ref-type="aff" rid="A4">4</xref>
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<contrib contrib-type="author"><name><surname>Daskalova</surname>
<given-names>Sasha M.</given-names>
</name>
<xref ref-type="aff" rid="A1">1</xref>
<xref ref-type="aff" rid="A3">3</xref>
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<contrib contrib-type="author"><name><surname>Lopez</surname>
<given-names>Lisa A.</given-names>
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<xref ref-type="aff" rid="A1">1</xref>
<xref ref-type="aff" rid="A2">2</xref>
<xref ref-type="aff" rid="A5">5</xref>
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<contrib contrib-type="author"><name><surname>Dolezal</surname>
<given-names>Kelly A.</given-names>
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<xref ref-type="aff" rid="A2">2</xref>
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<contrib contrib-type="author"><name><surname>Hogue</surname>
<given-names>Brenda G.</given-names>
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<xref ref-type="aff" rid="A1">1</xref>
<xref ref-type="aff" rid="A2">2</xref>
<xref rid="FN1" ref-type="author-notes">*</xref>
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<aff id="A1"><label>1</label>
The Biodesign Institute, Center for Infectious Diseases and Vaccinology, Arizona State University, Tempe AZ 85287-5401</aff>
<aff id="A2"><label>2</label>
School of Life Sciences, Arizona State University, Tempe AZ 85287-5401</aff>
<aff id="A3"><label>3</label>
Department of Biochemistry and Chemistry, Arizona State University, Tempe AZ 85287-5401</aff>
<aff id="A4"><label>4</label>
Microbiology Graduate Program, Arizona State University, Tempe AZ 85287-5401</aff>
<aff id="A5"><label>5</label>
Molecular and Cellular Biology Graduate Program, Arizona State University, Tempe AZ 85287-5401</aff>
<author-notes><corresp id="FN1"><label>*</label>
Corresponding Author. Mailing address: The Biodesign Institute, PO Box 875401, Arizona State University, Tempe, AZ 85287-5401. Phone: (480) 965-9478. Fax: (480) 727-7615. <email>Brenda.Hogue@asu.edu</email>
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<pub-date pub-type="nihms-submitted"><day>8</day>
<month>8</month>
<year>2015</year>
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<pub-date pub-type="epub"><day>27</day>
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<year>2015</year>
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<pub-date pub-type="ppub"><month>4</month>
<year>2015</year>
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<pub-date pub-type="pmc-release"><day>01</day>
<month>4</month>
<year>2016</year>
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<volume>478</volume>
<fpage>75</fpage>
<lpage>85</lpage>
<pmc-comment>elocation-id from pubmed: 10.1016/j.virol.2015.02.005</pmc-comment>
<abstract><p id="P2">Coronaviruses (CoVs) assemble at endoplasmic reticulum Golgi intermediate compartment (ERGIC) membranes and egress from cells in cargo vesicles. Only a few molecules of the envelope (E) protein are assembled into virions. The role of E in morphogenesis is not fully understood. The cellular localization and dynamics of mouse hepatitis CoV A59 (MHV) E protein were investigated to further understanding of its role during infection. E protein localized in the ERGIC and Golgi with the amino and carboxy termini in the lumen and cytoplasm, respectively. E protein does not traffic to the cell surface. MHV was genetically engineered with a tetracysteine tag at the carboxy end of E. Fluorescence recovery after photobleaching (FRAP) showed that E is mobile in ERGIC/Golgi membranes. Correlative light electron microscopy (CLEM) confirmed the presence of E in Golgi cisternae. The results provide strong support that E proteins carry out their function(s) at the site of budding/assembly.</p>
</abstract>
<kwd-group><kwd>Coronavirus</kwd>
<kwd>Envelope protein</kwd>
<kwd>Protein transport/localization</kwd>
<kwd>Virus assembly</kwd>
<kwd>Live-cell imaging</kwd>
<kwd>FRAP</kwd>
<kwd>CLEM</kwd>
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