๐ Coronavirus envelope (E) protein remains at the site of assembly
ยฉ 2015 Elsevier Inc. Coronaviruses (Co. Vs) 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.
keywords
๐ endoplasmic reticulum (78)
๐ mouse hepatitis (371)
๐ cell surface (110)
๐ electron microscopy (149)
๐ intermediate compartment (22)
author
๐ค Venkatagopalan, Pavithra
๐ค Daskalova, Sasha M.
๐ค Lopez, Lisa A.
๐ค Dolezal, Kelly A.
๐ค Hogue, Brenda G.
year
โฐ 2015
journal
๐ Virology
issn
๐ 10960341 00426822
volume
478
number
page
75-85
citedbycount
10
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