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

Naoto Ito, Tetsuo Mita, Kenta Shimizu, Yuki Ito, Tatsunori Masatani, Keisuke Nakagawa, Satoko Yamaoka, Masako Abe, Kota Okadera, Nobuyuki Minamoto, Makoto Sugiyama

Research output: Contribution to journalArticlepeer-review

7 Scopus citations

Abstract

We previously reported that rabies virus strain CE(NiM), but not the parental Ni-CE strain, killed mice after intracerebral inoculation. CE(NiM) and Ni-CE are genetically identical except for two amino acids at positions 29 and 95 in the M protein. In this study, to identify which residue determines the pathogenicity, we examined pathogenicities of two Ni-CE mutants, CE(NiM29) and CE(NiM95), which were established by replacement of an amino acid residue at position 29 or 95 in the Ni-CE M protein with the corresponding residue of CE(NiM), respectively. We found that CE(NiM95), but not CE(NiM29), killed mice, indicating that the amino acid at position 95 in the M protein is the pathogenic determinant.

Original languageEnglish (US)
Pages (from-to)1363-1366
Number of pages4
JournalJournal of Veterinary Medical Science
Volume73
Issue number10
DOIs
StatePublished - Oct 2011
Externally publishedYes

Keywords

  • Matrix protein
  • Pathogenicity
  • Rabies virus

ASJC Scopus subject areas

  • General Veterinary

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