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Updated: Jun 6, 2026

Analysis of the Lipid Composition of Mycobacteria by Thin Layer Chromatography
Published on: April 16, 2021
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
Abstract:
Few therapeutic alternatives remain for the treatment of infections due to multiresistant Mycobacterium abscessus. Here we show that the peptidoglycans of the "rough" and "smooth" morphotypes contain predominantly 3→3 cross-links generated by l,d-transpeptidases, indicating that these enzymes are attractive targets for the development of efficient drugs.
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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