Multiple moonlighting functions of mycobacterial molecular chaperones

Tuberculosis (Edinb). 2010 Mar;90(2):119-24. doi: 10.1016/ Epub 2010 Mar 24.


Molecular chaperones and protein folding catalysts are normally thought of as intracellular proteins involved in protein folding quality control. However, in the mycobacteria there is increasing evidence to support the hypothesis that molecular chaperones are also secreted intercellular signalling molecules or can control actions at the cell wall or indeed control the composition of the cell wall. The most recent evidence for protein moonlighting in the mycobacteria is the report that chaperonin 60.2 of Mycobacterium tuberculosis is important in the key event in tuberculosis - the entry of the bacterium into the macrophage. This brief overview highlights the potential importance of the moonlighting functions of molecular chaperones in the biology and pathobiology of the mycobacteria.

Publication types

  • Review

MeSH terms

  • Bacterial Proteins / genetics
  • Bacterial Proteins / immunology
  • Bacterial Proteins / metabolism*
  • Cell Communication* / genetics
  • Humans
  • Molecular Chaperones / genetics
  • Molecular Chaperones / immunology
  • Molecular Chaperones / metabolism*
  • Mycobacterium tuberculosis / genetics
  • Mycobacterium tuberculosis / immunology
  • Mycobacterium tuberculosis / metabolism*
  • Signal Transduction* / genetics
  • Tuberculosis / genetics
  • Tuberculosis / immunology
  • Tuberculosis / metabolism*


  • Bacterial Proteins
  • Molecular Chaperones