Lipolytic enzymes in Mycobacterium tuberculosis

Appl Microbiol Biotechnol. 2008 Apr;78(5):741-9. doi: 10.1007/s00253-008-1397-2. Epub 2008 Feb 29.

Abstract

Mycobacterium tuberculosis is a bacterial pathogen that can persist for decades in an infected patient without causing a disease. In vivo, the tubercle bacillus present in the lungs store triacylglycerols in inclusion bodies. The same process can be observed in vitro when the bacteria infect adipose tissues. Indeed, before entering in the dormant state, bacteria accumulate lipids originating from the host cell membrane degradation and from de novo synthesis. During the reactivation phase, these lipids are hydrolysed and the infection process occurs. The degradation of both extra and intracellular lipids can be directly related to the presence of lipolytic enzymes in mycobacteria, which have been ignored during a long period particularly due to the difficulties to obtain a high expression level of these enzymes in M. tuberculosis. The completion of the M. tuberculosis genome offered new opportunity to this kind of study. The aim of this review is to focus on the recent results obtained in the field of mycobacterium lipolytic enzymes and although no experimental proof has been shown in vivo, it is tempting to speculate that these enzymes could be involved in the virulence and pathogenicity processes.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Amino Acid Sequence
  • Bacterial Proteins / chemistry
  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism
  • Humans
  • Lipase / chemistry
  • Lipase / genetics
  • Lipase / metabolism*
  • Lipid Metabolism*
  • Molecular Sequence Data
  • Mycobacterium / enzymology
  • Mycobacterium tuberculosis / enzymology*
  • Mycobacterium tuberculosis / genetics
  • Mycobacterium tuberculosis / metabolism
  • Phospholipases / chemistry
  • Phospholipases / genetics
  • Phospholipases / metabolism*
  • Sequence Alignment
  • Tuberculosis / enzymology
  • Tuberculosis / microbiology*

Substances

  • Bacterial Proteins
  • Phospholipases
  • Lipase