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Amino acid substitution at position 95 in rabies virus matrix protein affects viral pathogenicity

Naoto Ito1, Tetsuo Mita, Kenta Shimizu

  • 1Laboratory of Zoonotic Diseases, Faculty of Applied Biological Sciences, Gifu University, Gifu, Japan.

The Journal of Veterinary Medical Science
|June 8, 2011
PubMed

Insights

The M protein

Area of Science:

  • Virology
  • Molecular Biology
  • Pathogenesis studies

Background:

  • Rabies virus strain CE(NiM) exhibits pathogenicity in mice after intracerebral inoculation, unlike its parental Ni-CE strain.
  • Genetic analysis reveals CE(NiM) and Ni-CE are identical except for two amino acid residues in the M protein at positions 29 and 95.

Purpose of the Study:

  • To pinpoint the specific amino acid residue within the M protein responsible for the observed pathogenicity of the CE(NiM) rabies virus strain.

Main Methods:

  • Construction of two mutant rabies virus strains, CE(NiM29) and CE(NiM95), by site-directed mutagenesis.
  • Introduction of specific amino acid substitutions at positions 29 and 95 of the Ni-CE M protein, mimicking the CE(NiM) strain.
  • Intracerebral inoculation of mice with the wild-type strains and the generated mutants to assess pathogenicity.

Main Results:

  • The CE(NiM95) mutant, possessing the CE(NiM) amino acid at position 95, demonstrated pathogenicity and killed mice.
  • The CE(NiM29) mutant, with the CE(NiM) amino acid at position 29, did not exhibit pathogenicity in the mouse model.
  • This indicates that the amino acid at position 95 is the critical determinant of pathogenicity.

Conclusions:

  • The amino acid residue at position 95 in the rabies virus M protein is the key determinant of pathogenicity.
  • Understanding these molecular determinants can inform future rabies virus research and control strategies.

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