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A new internal ribosomal entry site 5' boundary is required for poliovirus translation initiation in a mouse system

T Ishii1, K Shiroki, D H Hong

  • 1Department of Microbiology, Institute of Medical Science, The University of Tokyo, Japan.

Journal of Virology
|March 14, 1998
PubMed

Insights

Poliovirus mutations in the internal ribosomal entry site (IRES) stem-loop II (SLII) reduced viral replication in mouse cells and neurovirulence. Revertants restored these functions, indicating nucleotide 107 is crucial for IRES activity in mouse cells.

Area of Science:

  • Virology
  • Molecular Biology
  • Genetics

Background:

  • The internal ribosomal entry site (IRES) is critical for cap-independent translation initiation of poliovirus.
  • The stem-loop II (SLII) structure within the IRES is essential for viral replication and pathogenesis.

Purpose of the Study:

  • To investigate the role of SLII structure mutations in poliovirus replication and neurovirulence.
  • To identify genetic determinants of IRES activity in different cell types.

Main Methods:

  • Generation of poliovirus mutants with alterations in the SLII region.
  • Assessment of viral replication in human (HeLa) and mouse (TgSVA) cells.
  • Evaluation of neurovirulence in a mouse model.
  • Isolation and characterization of naturally occurring revertants.
  • Analysis of IRES activity using a cell-free translation system.

Main Results:

  • SLII mutants replicated efficiently in HeLa cells but poorly in TgSVA cells, with attenuated neurovirulence.
  • Revertants regained efficient replication in TgSVA cells and restored neurovirulence.
  • Revertants exhibited enhanced IRES activity in TgSVA cell extracts.
  • Mutations at nucleotide (nt) 107 and within nt 120-161 were identified as key revertant sites.

Conclusions:

  • Nucleotide 107 of poliovirus RNA plays a critical role in IRES-mediated translation in mouse cells.
  • Specific mutations within the SLII structure modulate IRES activity and affect poliovirus host range and virulence.
  • The findings provide insights into the structural requirements for IRES function and poliovirus adaptation.

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