clpB, a class III heat-shock gene regulated by CtsR, is involved in thermotolerance and virulence of Enterococcus faecalis

Microbiology (Reading). 2011 Mar;157(Pt 3):656-665. doi: 10.1099/mic.0.041897-0. Epub 2010 Dec 9.

Abstract

Here, we transcriptionally and phenotypically characterized the clpB gene from Enterococcus faecalis. Northern blot analysis identified a monocistronic mRNA strongly induced at 48 and 50 °C. In silico analysis identified that the clpB gene encodes a protein of 868 aa with a predicted molecular mass of approximately 98 kDa, presenting two conserved ATP-binding domains. Sequence analysis also identified a CtsR-binding box upstream of the putative -10 sequence, and inactivation of the ctsR gene resulted in an approximately 2-log increase in clpB mRNA expression, confirming ClpB as a member of the CtsR regulon. While expression of clpB was induced by heat stress, a ΔclpB strain grew relatively well under many different stressful conditions, including elevated temperatures. However, expression of ClpB appears to play a major role in induced thermotolerance and in pathogenesis, as assessed by using the Galleria mellonella virulence model.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism*
  • Base Sequence
  • Disease Models, Animal
  • Enterococcus faecalis / drug effects
  • Enterococcus faecalis / pathogenicity*
  • Enterococcus faecalis / physiology*
  • Gene Expression Regulation, Bacterial*
  • Heat-Shock Proteins / genetics
  • Heat-Shock Proteins / metabolism*
  • Heat-Shock Response
  • Hot Temperature*
  • Humans
  • Molecular Sequence Data
  • Moths / microbiology*
  • Repressor Proteins / genetics
  • Repressor Proteins / metabolism*
  • Reverse Transcriptase Polymerase Chain Reaction
  • Sequence Analysis, DNA
  • Virulence

Substances

  • Bacterial Proteins
  • CtsR protein, bacteria
  • Heat-Shock Proteins
  • Repressor Proteins