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AmiA is a penicillin target enzyme with dual activity in the intracellular pathogen Chlamydia pneumoniae

Lookup NU author(s): Dr Adeline Derouaux, Professor Waldemar Vollmer


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Intracellular Chlamydiaceae do not need to resist osmotic challenges and a functional cell wall was not detected in these pathogens. Nevertheless, a recent study revealed evidence for circular peptidoglycan-like structures in Chlamydiaceae and penicillin inhibits cytokinesis, a phenomenon known as the chlamydial anomaly. Here, by characterizing a cell wall precursor-processing enzyme, we provide insights into the mechanisms underlying this mystery. We show that AmiA from Chlamydia pneumoniae separates daughter cells in an Escherichia coli amidase mutant. Contrary to homologues from free-living bacteria, chlamydial AmiA uses lipid II as a substrate and has dual activity, acting as an amidase and a carboxypeptidase. The latter function is penicillin sensitive and assigned to a penicillin-binding protein motif. Consistent with the lack of a regulatory domain in AmiA, chlamydial CPn0902, annotated as NlpD, is a carboxypeptidase, rather than an amidase activator, which is the case for E. coli NlpD. Functional conservation of AmiA implicates a role in cytokinesis and host response modulation.

Publication metadata

Author(s): Klöckner A, Otten C, Derouaux A, Vollmer W, Bühl H, De Benedetti S, Münch D, Josten M, Mölleken K, Sahl HG, Henrichfreise B

Publication type: Article

Publication status: Published

Journal: Nature Communications

Year: 2014

Volume: 5

Print publication date: 23/06/2014

ISSN (print): 2041-1723

Publisher: Nature Publishing Group


DOI: 10.1038/ncomms5201


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