Coronavirus envelope (E) protein remains at the site of assembly

Pavithra Venkatagopalan, Sasha M. Daskalova, Lisa A. Lopez, Kelly A. Dolezal, Brenda Hogue

Research output: Contribution to journalArticlepeer-review

156 Scopus citations


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.

Original languageEnglish (US)
Pages (from-to)75-85
Number of pages11
StatePublished - Apr 1 2015


  • CLEM
  • Coronavirus
  • Envelope protein
  • FRAP
  • Live-cell imaging
  • Protein transport/localization
  • Virus assembly

ASJC Scopus subject areas

  • Virology


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