Peptidoglycan hydrolase of an unusual cross-link cleavage specificity contributes to bacterial cell wall synthesis
Abstract
Bacteria contain peptidoglycan (PG) in their cell envelope to protect them against intracellular osmotic pressure and environmental stress. PG is a large elastic polymer made up of glycan strands interlinked by short peptide chains that form a mesh-like sacculus. In many bacteria, the peptide cross-links are of two types: the predominant D-alanine-meso-diaminopimelic acid (mDAP) and the rare mDAP-mDAP cross-links. Here, we report the importance of mDAP cross-links in PG synthesis during cell growth by identifying a previously unknown hydrolytic enzyme that cleaves such cross-links in the PG sacculi of Escherichia coli. In summary, this study clarifies the role of PG hydrolysis in bacterial cell wall synthesis, thereby rendering it an alternative drug target for development of new antimicrobial agents.
- Publication:
-
Proceedings of the National Academy of Science
- Pub Date:
- April 2019
- DOI:
- 10.1073/pnas.1816893116
- Bibcode:
- 2019PNAS..116.7825C