A coronavirus E protein is present in two distinct pools with different effects on assembly and the secretory pathway

Jason W. Westerbeck, Carolyn E Machamer

Research output: Contribution to journalArticle

Abstract

Coronaviruses (CoVs) assemble by budding into the lumen of the early Golgi complex prior to exocytosis. The small CoV envelope (E) protein plays roles in assembly, virion release, and pathogenesis. CoV E has a single hydrophobic domain (HD), is targeted to Golgi complex membranes, and has cation channel activity in vitro. However, the precise functions of the CoV E protein during infection are still enigmatic. Structural data for the severe acute respiratory syndrome (SARS)-CoV E protein suggest that it assembles into a homopentamer. Specific residues in the HD regulate the ion-conducting pore formed by SARS-CoV E in artificial bilayers and the pathogenicity of the virus during infection. The E protein from the avian infectious bronchitis virus (IBV) has dramatic effects on the secretory system which require residues in the HD. Here, we use the known structural data from SARS-CoV E to infer the residues important for ion channel activity and the oligomerization of IBV E. We present biochemical data for the formation of two distinct oligomeric pools of IBV E in transfected and infected cells and the residues required for their formation. A high-order oligomer of IBV E is required for the production of virus-like particles (VLPs), implicating this form of the protein in virion assembly. Additionally, disruption of the secretory pathway by IBV E correlates with a form that is likely monomeric, suggesting that the effects on the secretory pathway are independent of E ion channel activity.

Original languageEnglish (US)
Pages (from-to)9313-9323
Number of pages11
JournalJournal of Virology
Volume89
Issue number18
DOIs
StatePublished - 2015

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Infectious bronchitis virus
Coronavirus
Coronavirinae
Secretory Pathway
Severe Acute Respiratory Syndrome
Virion
ion channels
Golgi Apparatus
Golgi apparatus
Proteins
Ion Channels
virion
proteins
virus-like particles
exocytosis
Exocytosis
Virus Diseases
infection
Virulence
Cations

ASJC Scopus subject areas

  • Immunology
  • Virology

Cite this

A coronavirus E protein is present in two distinct pools with different effects on assembly and the secretory pathway. / Westerbeck, Jason W.; Machamer, Carolyn E.

In: Journal of Virology, Vol. 89, No. 18, 2015, p. 9313-9323.

Research output: Contribution to journalArticle

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