Coronavirus Envelope (E) Protein Remains at the Site of Assembly
Identifieur interne : 000444 ( Ncbi/Merge ); précédent : 000443; suivant : 000445Coronavirus Envelope (E) Protein Remains at the Site of Assembly
Auteurs : Pavithra Venkatagopalan [États-Unis] ; Sasha M. Daskalova [États-Unis] ; Lisa A. Lopez [États-Unis] ; Kelly A. Dolezal [États-Unis] ; Brenda G. Hogue [États-Unis]Source :
- 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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Lopez</name><affiliation wicri:level="2"><nlm:aff id="A1">The Biodesign Institute, Center for Infectious Diseases and Vaccinology, Arizona State University, Tempe AZ 85287-5401</nlm:aff><country xml:lang="fr">États-Unis</country><placeName><region type="state">Arizona</region></placeName><wicri:cityArea>The Biodesign Institute, Center for Infectious Diseases and Vaccinology, Arizona State University</wicri:cityArea></affiliation><affiliation wicri:level="2"><nlm:aff id="A2">School of Life Sciences, Arizona State University, Tempe AZ 85287-5401</nlm:aff><country xml:lang="fr">États-Unis</country><placeName><region type="state">Arizona</region></placeName><wicri:cityArea>School of Life Sciences, Arizona State University</wicri:cityArea></affiliation><affiliation wicri:level="2"><nlm:aff id="A5">Molecular and Cellular Biology Graduate Program, Arizona State University, Tempe AZ 85287-5401</nlm:aff><country xml:lang="fr">États-Unis</country><placeName><region type="state">Arizona</region></placeName><wicri:cityArea>Molecular and Cellular Biology Graduate Program, Arizona State University</wicri:cityArea></affiliation></author><author><name sortKey="Dolezal, Kelly A" sort="Dolezal, Kelly A" uniqKey="Dolezal K" first="Kelly A." last="Dolezal">Kelly A. Dolezal</name><affiliation wicri:level="2"><nlm:aff id="A1">The Biodesign Institute, Center for Infectious Diseases and Vaccinology, Arizona State University, Tempe AZ 85287-5401</nlm:aff><country xml:lang="fr">États-Unis</country><placeName><region type="state">Arizona</region></placeName><wicri:cityArea>The Biodesign Institute, Center for Infectious Diseases and Vaccinology, Arizona State University</wicri:cityArea></affiliation><affiliation wicri:level="2"><nlm:aff id="A2">School of Life Sciences, Arizona State University, Tempe AZ 85287-5401</nlm:aff><country xml:lang="fr">États-Unis</country><placeName><region type="state">Arizona</region></placeName><wicri:cityArea>School of Life Sciences, Arizona State University</wicri:cityArea></affiliation><affiliation wicri:level="2"><nlm:aff id="A4">Microbiology Graduate Program, Arizona State University, Tempe AZ 85287-5401</nlm:aff><country xml:lang="fr">États-Unis</country><placeName><region type="state">Arizona</region></placeName><wicri:cityArea>Microbiology Graduate Program, Arizona State University</wicri:cityArea></affiliation></author><author><name sortKey="Hogue, Brenda G" sort="Hogue, Brenda G" uniqKey="Hogue B" first="Brenda G." last="Hogue">Brenda G. Hogue</name><affiliation wicri:level="2"><nlm:aff id="A1">The Biodesign Institute, Center for Infectious Diseases and Vaccinology, Arizona State University, Tempe AZ 85287-5401</nlm:aff><country xml:lang="fr">États-Unis</country><placeName><region type="state">Arizona</region></placeName><wicri:cityArea>The Biodesign Institute, Center for Infectious Diseases and Vaccinology, Arizona State University</wicri:cityArea></affiliation><affiliation wicri:level="2"><nlm:aff id="A2">School of Life Sciences, Arizona State University, Tempe AZ 85287-5401</nlm:aff><country xml:lang="fr">États-Unis</country><placeName><region type="state">Arizona</region></placeName><wicri:cityArea>School of Life Sciences, Arizona State University</wicri:cityArea></affiliation></author></analytic><series><title level="j">Virology</title><idno type="ISSN">0042-6822</idno><idno type="eISSN">1096-0341</idno><imprint><date when="2015">2015</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><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></TEI><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>
<pmc-dir>properties manuscript</pmc-dir>
<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><journal-title-group><journal-title>Virology</journal-title></journal-title-group><issn pub-type="ppub">0042-6822</issn><issn pub-type="epub">1096-0341</issn></journal-meta><article-meta><article-id pub-id-type="pmid">25726972</article-id><article-id pub-id-type="pmc">4550588</article-id><article-id pub-id-type="doi">10.1016/j.virol.2015.02.005</article-id><article-id pub-id-type="manuscript">NIHMS668555</article-id><article-categories><subj-group subj-group-type="heading"><subject>Article</subject></subj-group></article-categories><title-group><article-title>Coronavirus Envelope (E) Protein Remains at the Site of Assembly</article-title></title-group><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></contrib><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></contrib><contrib contrib-type="author"><name><surname>Lopez</surname><given-names>Lisa A.</given-names></name><xref ref-type="aff" rid="A1">1</xref><xref ref-type="aff" rid="A2">2</xref><xref ref-type="aff" rid="A5">5</xref></contrib><contrib contrib-type="author"><name><surname>Dolezal</surname><given-names>Kelly A.</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></contrib><contrib contrib-type="author"><name><surname>Hogue</surname><given-names>Brenda G.</given-names></name><xref ref-type="aff" rid="A1">1</xref><xref ref-type="aff" rid="A2">2</xref><xref rid="FN1" ref-type="author-notes">*</xref></contrib></contrib-group><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></corresp></author-notes><pub-date pub-type="nihms-submitted"><day>8</day><month>8</month><year>2015</year></pub-date><pub-date pub-type="epub"><day>27</day><month>2</month><year>2015</year></pub-date><pub-date pub-type="ppub"><month>4</month><year>2015</year></pub-date><pub-date pub-type="pmc-release"><day>01</day><month>4</month><year>2016</year></pub-date><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></kwd-group></article-meta></front></pmc><affiliations><list><country><li>États-Unis</li></country><region><li>Arizona</li></region></list><tree><country name="États-Unis"><region name="Arizona"><name sortKey="Venkatagopalan, Pavithra" sort="Venkatagopalan, Pavithra" uniqKey="Venkatagopalan P" first="Pavithra" last="Venkatagopalan">Pavithra Venkatagopalan</name></region><name sortKey="Daskalova, Sasha M" sort="Daskalova, Sasha M" uniqKey="Daskalova S" first="Sasha M." last="Daskalova">Sasha M. Daskalova</name><name sortKey="Daskalova, Sasha M" sort="Daskalova, Sasha M" uniqKey="Daskalova S" first="Sasha M." last="Daskalova">Sasha M. Daskalova</name><name sortKey="Dolezal, Kelly A" sort="Dolezal, Kelly A" uniqKey="Dolezal K" first="Kelly A." last="Dolezal">Kelly A. Dolezal</name><name sortKey="Dolezal, Kelly A" sort="Dolezal, Kelly A" uniqKey="Dolezal K" first="Kelly A." last="Dolezal">Kelly A. Dolezal</name><name sortKey="Dolezal, Kelly A" sort="Dolezal, Kelly A" uniqKey="Dolezal K" first="Kelly A." last="Dolezal">Kelly A. Dolezal</name><name sortKey="Hogue, Brenda G" sort="Hogue, Brenda G" uniqKey="Hogue B" first="Brenda G." last="Hogue">Brenda G. Hogue</name><name sortKey="Hogue, Brenda G" sort="Hogue, Brenda G" uniqKey="Hogue B" first="Brenda G." last="Hogue">Brenda G. Hogue</name><name sortKey="Lopez, Lisa A" sort="Lopez, Lisa A" uniqKey="Lopez L" first="Lisa A." last="Lopez">Lisa A. Lopez</name><name sortKey="Lopez, Lisa A" sort="Lopez, Lisa A" uniqKey="Lopez L" first="Lisa A." last="Lopez">Lisa A. Lopez</name><name sortKey="Lopez, Lisa A" sort="Lopez, Lisa A" uniqKey="Lopez L" first="Lisa A." last="Lopez">Lisa A. Lopez</name><name sortKey="Venkatagopalan, Pavithra" sort="Venkatagopalan, Pavithra" uniqKey="Venkatagopalan P" first="Pavithra" last="Venkatagopalan">Pavithra Venkatagopalan</name><name sortKey="Venkatagopalan, Pavithra" sort="Venkatagopalan, Pavithra" uniqKey="Venkatagopalan P" first="Pavithra" last="Venkatagopalan">Pavithra Venkatagopalan</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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