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Scientific article
English

The double-stranded RNA binding domain of the vaccinia virus E3L protein inhibits both RNA- and DNA-induced activation of interferon beta

Published inThe Journal of biological chemistry, vol. 284, no. 38, p. 25471-25478
Publication date2009
Abstract

Vaccinia virus, a large DNA virus that replicates in the cytoplasm, expresses its E3L protein to inhibit the cellular innate immune response and apoptosis. E3L is a bifunctional protein that contains an N-terminal DNA binding domain (BD) and a C-terminal double-stranded RNA (dsRNA)-BD (residues 100-190), both of which contribute to viral pathogenesis by blocking the activation of cellular genes that respond to the viral infection. We report that expression of the dsRNA-BD alone inhibits not only the dsRNA-induced activation of interferon beta (IFNbeta) but also that of 5'-triphosphate single-stranded RNA and DNA-induced IFNbeta activation even though E3L(100-190) does not bind the latter two pathogen-associated molecular patterns. This inhibition occurs in both human HeLa and A549 cells, where RIG-I appears to be required for dsDNA-induced IFNbeta activation. Unexpectedly, the two residues most important for dsRNA binding are also critical for this domain's ability to inhibit all three nucleic acid-induced cellular responses.

Keywords
  • Animals
  • DEAD-box RNA Helicases/genetics/metabolism
  • DNA, Viral/genetics/metabolism
  • Hela Cells
  • Humans
  • Interferon-beta/genetics/metabolism
  • Mice
  • Protein Binding/genetics
  • Protein Structure, Tertiary
  • RNA, Double-Stranded
  • RNA, Viral/genetics/metabolism
  • RNA-Binding Proteins/genetics/metabolism
  • Vaccinia/genetics/metabolism
  • Vaccinia virus/genetics/metabolism/pathogenicity
  • Viral Proteins/genetics/metabolism
Citation (ISO format)
MARQ, Jean-Baptiste et al. The double-stranded RNA binding domain of the vaccinia virus E3L protein inhibits both RNA- and DNA-induced activation of interferon beta. In: The Journal of biological chemistry, 2009, vol. 284, n° 38, p. 25471–25478. doi: 10.1074/jbc.M109.018895
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Article (Published version)
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Identifiers
ISSN of the journal0021-9258
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