Contribution of eukaryotic-type serine/threonine kinase to stress response and virulence of Streptococcus suis

PLoS One. 2014 Mar 17;9(3):e91971. doi: 10.1371/journal.pone.0091971. eCollection 2014.

Abstract

Streptococcus suis serotype 2 (SS2) is an important swine and human pathogen responsible for septicemia and meningitis. The bacterial homologues of eukaryotic-type serine/threonine kinases (ESTKs) have been reported to play critical roles in various cellular processes. To investigate the role of STK in SS2, an isogenic stk mutant strain (Δstk) and a complemented strain (CΔstk) were constructed. The Δstk showed a significant decrease in adherence to HEp-2 cells, compared with the wild-type strain, and a reduced survival ratio in whole blood. In addition, the Δstk exhibited a notable reduced tolerance of environmental stresses including high temperature, acidic pH, oxidative stress, and high osmolarity. More importantly, the Δstk was attenuated in both the CD1 mouse and piglet models of infection. The results of quantitative reverse transcription-PCR (qRT-PCR) analysis indicated that the expressions of a few genes involving in adherence, stress response and virulence were clearly decreased in the Δstk mutant strain. Our data suggest that SsSTK is required for virulence and stress response in SS2.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Bacterial Adhesion / genetics
  • Bacterial Proteins / metabolism
  • Disease Models, Animal
  • Gene Expression Profiling
  • Gene Expression Regulation, Bacterial
  • Genome, Bacterial
  • Mice
  • Mutation
  • Protein Serine-Threonine Kinases / deficiency
  • Protein Serine-Threonine Kinases / genetics
  • Protein Serine-Threonine Kinases / metabolism*
  • Streptococcal Infections / microbiology*
  • Streptococcal Infections / mortality
  • Streptococcus suis / pathogenicity
  • Streptococcus suis / physiology*
  • Streptococcus suis / ultrastructure
  • Stress, Physiological / genetics
  • Swine
  • Virulence / genetics
  • Virulence Factors / genetics

Substances

  • Bacterial Proteins
  • Virulence Factors
  • Protein Serine-Threonine Kinases

Grants and funding

This work was supported by National Natural Science Foundation of China (31302114 and 31072155), China Postdoctoral Science Foundation Grant (2012M521026), Innovation of Agricultural Sciences in Jiangsu province (CX(11)2060), and Special Fund for Public Welfare Industry of Chinese Ministry of Agriculture (201303041). The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.