Inverse correlation of thermal lability and conversion efficiency for five prion protein polymorphic variants

L. Kirby, S. Agarwal, J. F. Graham, W. Goldmann, A. C. Gill

Research output: Contribution to journalArticlepeer-review

Abstract / Description of output

The NSs protein of Bunyamwera virus (Bunyaviridae) is an antiapoptotic interferon antagonist involved in silencing host protein expression by interfering with mRNA synthesis. Here, we show that the ability to inhibit both host transcription and the interferon response is linked to interaction of NSs with the MED8 component of Mediator, a protein complex necessary for mRNA production. The interacting domain on NSs was mapped to the C-terminal region, which contains amino acids conserved among orthobunyavirus NSs proteins. A recombinant virus in which the interacting domain in NSs was deleted had strongly reduced ability to inhibit host protein expression and was unable to inhibit the interferon response. This study provides further information on the mechanisms by which bunyavirus nonstructural proteins are involved in pathogenesis.
Original languageEnglish
Pages (from-to)1448-59
Number of pages12
Issue number7
Publication statusPublished - 2010

Keywords / Materials (for Non-textual outputs)

  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Cell Line
  • Cricetinae
  • DNA-Directed RNA Polymerases/metabolism
  • Humans
  • Immunity, Innate/immunology
  • Interferons/ antagonists & inhibitors/genetics/immunology
  • Mediator Complex
  • Molecular Sequence Data
  • Orthobunyavirus/chemistry/genetics/immunology/ metabolism
  • Protein Binding
  • Saccharomyces cerevisiae/genetics/metabolism
  • Transcription Factors/genetics/ metabolism
  • Two-Hybrid System Techniques
  • Viral Proteins/chemistry/genetics/ metabolism


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