Send to

Choose Destination
FEMS Microbiol Rev. 2015 Mar;39(2):262-75. doi: 10.1093/femsre/fuv001. Epub 2015 Feb 10.

The role of peptidoglycan in chlamydial cell division: towards resolving the chlamydial anomaly.

Author information

Institute of Microbiology, University Hospital Center and University of Lausanne, CH-1011 Lausanne, Switzerland.
Department of Microbiology & Molecular Medicine, Institute of Genetics & Genomics in Geneva (iGE3), Faculty of Medicine / CMU, University of Geneva, CH-1211 Geneva 4, Switzerland.
Institute of Microbiology, University Hospital Center and University of Lausanne, CH-1011 Lausanne, Switzerland


Chlamydiales are obligate intracellular bacteria including some important pathogens causing trachoma, genital tract infections and pneumonia, among others. They share an atypical division mechanism, which is independent of an FtsZ homologue. However, they divide by binary fission, in a process inhibited by penicillin derivatives, causing the formation of an aberrant form of the bacteria, which is able to survive in the presence of the antibiotic. The paradox of penicillin sensitivity of chlamydial cells in the absence of detectable peptidoglycan (PG) was dubbed the chlamydial anomaly, since no PG modified by enzymes (Pbps) that are the usual target of penicillin could be detected in Chlamydiales. We review here the recent advances in this field with the first direct and indirect evidences of PG-like material in both Chlamydiaceae and Chlamydia-related bacteria. Moreover, PG biosynthesis is required for proper localization of the newly described septal proteins RodZ and NlpD. Taken together, these new results set the stage for a better understanding of the role of PG and septal proteins in the division mechanism of Chlamydiales and illuminate the long-standing chlamydial anomaly. Moreover, understanding the chlamydial division mechanism is critical for the development of new antibiotics for the treatment of chlamydial chronic infections.


MreB; RodZ; Waddlia chondrophila; cell division; cell wall; contractile ring; peptidoglycan

[Indexed for MEDLINE]

Supplemental Content

Full text links

Icon for Silverchair Information Systems
Loading ...
Support Center