DevR (DosR) binding peptide inhibits adaptation of Mycobacterium tuberculosis under hypoxia

FEMS Microbiol Lett. 2012 May;330(1):66-71. doi: 10.1111/j.1574-6968.2012.02534.x. Epub 2012 Mar 26.

Abstract

DevR is a key regulator of the dormancy response in Mycobacterium tuberculosis (M. tb). Using DevR as bait to screen a phage display library, a peptide, DevRS1, was obtained. DevRS1 inhibited DevR-regulated transcription and survival of nonreplicating tubercle bacilli in a hypoxia model of dormancy. DevRS1 peptide-mediated inhibition demonstrates the efficacy of intercepting DevR function to block hypoxic adaptation of M. tb.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adaptation, Physiological
  • Anaerobiosis
  • Anti-Bacterial Agents / isolation & purification
  • Anti-Bacterial Agents / metabolism*
  • Bacterial Proteins / antagonists & inhibitors*
  • DNA-Binding Proteins
  • Gene Expression Profiling
  • Gene Expression Regulation, Bacterial
  • Humans
  • Microbial Viability / drug effects
  • Mycobacterium tuberculosis / physiology*
  • Peptide Library
  • Peptides / isolation & purification
  • Peptides / metabolism*
  • Protein Kinases
  • Stress, Physiological*

Substances

  • Anti-Bacterial Agents
  • Bacterial Proteins
  • DNA-Binding Proteins
  • DosR protein, Mycobacterium tuberculosis
  • Peptide Library
  • Peptides
  • Protein Kinases