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

Anna Klöckner, Christian Otten, Adeline Derouaux, Waldemar Vollmer, Henrike Bühl, Stefania De Benedetti, Daniela Münch, Michaele Josten, Katja Mölleken, Hans-Georg Sahl and Beate Henrichfreise ()
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Anna Klöckner: Institute for Medical Microbiology, Immunology and Parasitology (IMMIP), Pharmaceutical Microbiology, University of Bonn
Christian Otten: Institute for Medical Microbiology, Immunology and Parasitology (IMMIP), Pharmaceutical Microbiology, University of Bonn
Adeline Derouaux: The Centre for Bacterial Cell Biology, Institute for Cell and Molecular Biosciences, Newcastle University
Waldemar Vollmer: The Centre for Bacterial Cell Biology, Institute for Cell and Molecular Biosciences, Newcastle University
Henrike Bühl: Institute for Medical Microbiology, Immunology and Parasitology (IMMIP), Pharmaceutical Microbiology, University of Bonn
Stefania De Benedetti: Institute for Medical Microbiology, Immunology and Parasitology (IMMIP), Pharmaceutical Microbiology, University of Bonn
Daniela Münch: Institute for Medical Microbiology, Immunology and Parasitology (IMMIP), Pharmaceutical Microbiology, University of Bonn
Michaele Josten: Institute for Medical Microbiology, Immunology and Parasitology (IMMIP), Pharmaceutical Microbiology, University of Bonn
Katja Mölleken: Institute of Functional Microbial Genomics, University of Düsseldorf
Hans-Georg Sahl: Institute for Medical Microbiology, Immunology and Parasitology (IMMIP), Pharmaceutical Microbiology, University of Bonn
Beate Henrichfreise: Institute for Medical Microbiology, Immunology and Parasitology (IMMIP), Pharmaceutical Microbiology, University of Bonn

Nature Communications, 2014, vol. 5, issue 1, 1-10

Abstract: Abstract 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.

Date: 2014
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DOI: 10.1038/ncomms5201

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