Inhibition of PKR by vaccinia virus

Role of the N- and C-terminal domains of E3L

Research output: Contribution to journalArticle

72 Citations (Scopus)

Abstract

The process of eukaryotic translation initiation can be regulated by a highly conserved mechanism involving the phosphorylation of the translation initiation factor eIF2 on the α subunit. This mechanism is recognized as an efficient step in the host antiviral response. Vaccinia virus (VV), like many other viruses, encodes proteins to overcome this inhibitory process. The C-terminus of the vaccinia virus E3L is known to bind to double-stranded RNA (dsRNA) thereby sequestering the activator of this antiviral response. In this report, the N-terminus of E3L was found to be required for the additional regulation of eIF2α phosphorylation. This phosphorylation event did not lead to a global shutdown in protein synthesis. Because the N-terminus of E3L is required for full viral pathogenesis in mice, these results suggest an alternative role of eIF2α phosphorylation in regulating viral replication.

Original languageEnglish (US)
Pages (from-to)419-429
Number of pages11
JournalVirology
Volume324
Issue number2
DOIs
StatePublished - Jul 1 2004

Fingerprint

Vaccinia virus
Phosphorylation
Antiviral Agents
Peptide Initiation Factors
Double-Stranded RNA
Proteins
Viruses

Keywords

  • C-terminal domain
  • PKR
  • Vaccinia virus

ASJC Scopus subject areas

  • Virology
  • Infectious Diseases

Cite this

Inhibition of PKR by vaccinia virus : Role of the N- and C-terminal domains of E3L. / Langland, Jeffrey; Jacobs, Bertram.

In: Virology, Vol. 324, No. 2, 01.07.2004, p. 419-429.

Research output: Contribution to journalArticle

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