Nodamura virus B2 amino terminal domain sensitivity to small interfering RNA

Ali PS 1 , John J 2 , Selvaraj M 3 , Kek TL 3 , Salleh MZ 3

Affiliations 

  • 1 Institute of Biophysical Chemistry, Goethe University, Max-von-Laue-Str. 9, Frankfurt 60438, Germany
  • 2 Institute of General Microbiology and Microbe Genetics, Friedrich-Schiller University Jena, Neugasse 24, D-07743 Jena, Germany
  • 3 Integrative Pharmacogenomics Institute (iPROMISE), Universiti Teknologi, MARA, 42300 Puncak Alam, Selangor, Malaysia
Microbiol. Immunol., 2015 May;59(5):299-304.
PMID: 25753649 DOI: 10.1111/1348-0421.12253

Abstract

Nodamura virus (NoV) B2, a suppressor of RNA interference, binds double stranded RNAs (dsRNAs) and small interfering RNAs (siRNAs) corresponding to Dicer substrates and products. Here, we report that the amino terminal domain of NoV B2 (NoV B2 79) specifically binds siRNAs but not dsRNAs. NoV B2 79 oligomerizes on binding to 27 nucleotide siRNA. Mutation of the residues phenylalanine49 and alanine60 to cysteine and methionine, respectively enhances the RNA binding affinity of NoV B2 79. Circular dichroism spectra demonstrated that the wild type and mutant NoV B2 79 have similar secondary structure conformations.

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