Coronavirus Envelope (E) Protein Remains at the Site of Assembly
Identifieur interne : 001101 ( Main/Exploration ); précédent : 001100; suivant : 001102Coronavirus 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
Affiliations:
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Le document en format XML
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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>
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