Heat-shock protein ClpL/HSP100 increases penicillin tolerance in Streptococcus pneumoniae

Adv Otorhinolaryngol. 2011:72:126-8. doi: 10.1159/000324658. Epub 2011 Aug 18.

Abstract

Penicillin resistance and tolerance has been an increasing threat to the treatment of pneumococcal pneumoniae. However, no penicillin tolerance-related genes have been claimed. Here we show that a major heat shock protein ClpL/HSP100 could modulate the expression of a cell wall synthesis enzyme PBP2x, and subsequently increase cell wall thickness and penicillin tolerance in Streptococus pneumoniae.

MeSH terms

  • Bacterial Proteins / drug effects
  • Bacterial Proteins / metabolism*
  • Heat-Shock Proteins / metabolism*
  • Humans
  • Penicillin Resistance*
  • Penicillin-Binding Proteins / metabolism*
  • Penicillins / pharmacology*
  • Pneumococcal Infections / drug therapy*
  • Pneumococcal Infections / metabolism
  • Pneumococcal Infections / microbiology
  • Streptococcus pneumoniae / drug effects*

Substances

  • Bacterial Proteins
  • Heat-Shock Proteins
  • Penicillin-Binding Proteins
  • Penicillins
  • PBP 2x protein, Streptococcus