The peptidoglycan of Mycobacterium abscessus is predominantly cross-linked by L,D-transpeptidases

Marie Lavollay1, Martine Fourgeaud, Jean-Louis Herrmann

  • 1LRMA, Equipe 12, Centre de Recherches des Cordeliers, 15 rue de l'Ecole de Médecine, 75270 Paris Cedex 06, France. jean-luc.mainardi@crc.jussieu.fr

Journal of Bacteriology
|November 25, 2010
PubMed

Insights

Multiresistant Mycobacterium abscessus infections have limited treatment options. This study reveals that l,d-transpeptidases, which generate peptidoglycan cross-links, are promising drug targets for new therapies.

Area of Science:

  • Microbiology
  • Drug Discovery
  • Biochemistry

Background:

  • Multiresistant Mycobacterium abscessus infections pose a significant clinical challenge.
  • Existing therapeutic options for these infections are severely limited.

Purpose of the Study:

  • To identify novel drug targets for treating multiresistant Mycobacterium abscessus.
  • To investigate the peptidoglycan cross-linking mechanisms in Mycobacterium abscessus.

Main Methods:

  • Analysis of peptidoglycans from rough and smooth morphotypes of Mycobacterium abscessus.
  • Characterization of peptidoglycan cross-linking enzymes, specifically l,d-transpeptidases.

Main Results:

  • Peptidoglycans from both morphotypes predominantly feature 3→3 cross-links.
  • These 3→3 cross-links are generated by l,d-transpeptidases.

Conclusions:

  • L,d-transpeptidases are crucial for peptidoglycan integrity in Mycobacterium abscessus.
  • L,d-transpeptidases represent attractive targets for developing new antimicrobial drugs against resistant strains.

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