Investigation into the role of the serine protease HtrA in Yersinia pestis pathogenesis

FEMS Microbiol Lett. 2000 May 15;186(2):281-6. doi: 10.1111/j.1574-6968.2000.tb09118.x.

Abstract

The HtrA stress response protein has been shown to play a role in the virulence of a number of pathogens. For some organisms, htrA mutants are attenuated in the animal model and can be used as live vaccines. A Yersinia pestis htrA orthologue was identified, cloned and sequenced, showing 86% and 87% similarity to Escherichia coli and Salmonella typhimurium HtrAs. An isogenic Y. pestis htrA mutant was constructed using a reverse genetics approach. In contrast to the wild-type strain, the mutant failed to grow at an elevated temperature of 39 degrees C, but showed only a small increase in sensitivity to oxidative stress and was only partially attenuated in the animal model. However, the mutant exhibited a different protein expression profile to that of the wild-type strain when grown at 28 degrees C to simulate growth in the flea.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Bacterial Proteins / isolation & purification
  • Bacterial Proteins / metabolism
  • Bacterial Vaccines
  • Heat-Shock Proteins*
  • Mice
  • Mice, Inbred BALB C
  • Periplasmic Proteins*
  • Plague / immunology
  • Plague / physiopathology
  • Polymerase Chain Reaction
  • Serine Endopeptidases / genetics
  • Serine Endopeptidases / metabolism*
  • Virulence
  • Yersinia pestis / genetics
  • Yersinia pestis / immunology
  • Yersinia pestis / pathogenicity*

Substances

  • Bacterial Proteins
  • Bacterial Vaccines
  • Heat-Shock Proteins
  • Periplasmic Proteins
  • DegP protease
  • Serine Endopeptidases