ArticleNature communications2014
AmiA is a penicillin target enzyme with dual activity in the intracellular pathogen Chlamydia pneumoniae.
Article in Nature communications, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 39 citations in OpenAlex.
- Characterization of the cell division-associated peptidoglycan amidase AmiA ofJournal of bacteriology · 2026Article
- Article
- The MraY Inhibitor Muraymycin D2 and Its Derivatives Induce Enlarged Cells in Obligate IntracellularAntibiotics (Basel, Switzerland) · 2024Article
- Structure predictions and functional insights into Amidase_3 domain containing N-acetylmuramyl-L-alanine amidases from Deinococcus indicus DR1.BMC microbiology · 2024Article
- Article
- Article
- Persistence Alters the Interaction between Chlamydia trachomatis and Its Host Cell.Infection and immunity · 2021Article
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- Vibrio fischeri Amidase Activity Is Required for Normal Cell Division, Motility, and Symbiotic Competence.Applied and environmental microbiology · 2021Article
- Chlamydia trachomatis Oligopeptide Transporter Performs Dual Functions of Oligopeptide Transport and Peptidoglycan Recycling.Infection and immunity · 2020Article
- Building peptidoglycan inside eukaryotic cells: A view from symbiotic and pathogenic bacteria.Molecular microbiology · 2020Review
- Interactions Screenings Unearth Potential New Divisome Components in theMicroorganisms · 2019Article
- Article
- Amidase activity is essential for medial localization of AmiC in Caulobacter crescentus.Current genetics · 2018Article
- Peptidoglycan in obligate intracellular bacteria.Molecular microbiology · 2018Review
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- AmiD Is a Novel Peptidoglycan Amidase inFrontiers in cellular and infection microbiology · 2017Article
- Chlamydia cell biology and pathogenesis.Nature reviews. Microbiology · 2016Review
- Pathogenic Chlamydia Lack a Classical Sacculus but Synthesize a Narrow, Mid-cell Peptidoglycan Ring, Regulated by MreB, for Cell Division.PLoS pathogens · 2016Article
- Targeted Delivery of Amoxicillin to C. trachomatis by the Transferrin Iron Acquisition Pathway.PloS one · 2016Article
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Authors and funding
11 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
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.
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