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A novel role for poly(C) binding proteins in programmed ribosomal frameshifting

Sawsan Napthine1, Emmely E Treffers2, Susanne Bell1

  • 1Department of Pathology, University of Cambridge, Cambridge, CB2 1QP, UK.

Nucleic Acids Research
|June 4, 2016
PubMed

Insights

This study reveals a novel viral mechanism where a protein complex, including a cellular poly(C) binding protein (PCBP), activates programmed ribosomal frameshifting (PRF) in viruses. This interaction highlights a new virus-host interaction pathway.

Area of Science:

  • Molecular Biology
  • Virology
  • Genetics

Background:

  • Programmed ribosomal frameshifting (PRF) regulates gene expression in viruses and cellular genes.
  • PRF is typically induced by mRNA secondary structures that affect ribosome fidelity at slippery sequences.

Purpose of the Study:

  • To investigate the mechanism of nsp2 programmed ribosomal frameshifting (PRF) in porcine reproductive and respiratory syndrome virus (PRRSV).
  • To identify the trans-acting protein factors involved in nsp2 PRF activation.

Main Methods:

  • In vitro translation assays to study ribosomal frameshifting.
  • Electrophoretic mobility shift assays (EMSAs) to analyze protein-RNA interactions.

Main Results:

  • A protein complex comprising viral nsp1β and cellular poly(C) binding protein (PCBP) was identified.
  • This PCBP/nsp1β complex binds to a C-rich region downstream of the PRRSV nsp2 slippery sequence.
  • The complex was shown to stimulate PRF, mimicking structured mRNA stimulators.

Conclusions:

  • This is the first demonstration of a cellular trans-acting protein's role in viral PRF.
  • The findings expand the known functions of poly(C) binding proteins.
  • A new class of virus-host interactions involving PCBP and viral proteins is proposed.

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