ArticleNature communications2014
FtsZ-independent septal recruitment and function of cell wall remodelling enzymes in chlamydial pathogens.
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 15 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
15 citing papers in PubMed, 23 citations in OpenAlex.
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- Amidase activity is essential for medial localization of AmiC in Caulobacter crescentus.Current genetics · 2018Article
- Peptidoglycan in obligate intracellular bacteria.Molecular microbiology · 2018Review
- Simkania negevensis, an Example of the Diversity of the Antimicrobial Susceptibility Pattern among Chlamydiales.Antimicrobial agents and chemotherapy · 2017Article
- Redefining the roles of the FtsZ-ring in bacterial cytokinesis.Current opinion in microbiology · 2016Review
- Chlamydia cell biology and pathogenesis.Nature reviews. Microbiology · 2016Review
- Evolutionary Cell Biology of Division Mode in the BacterialFrontiers in microbiology · 2016Review
- Regulated proteolysis of a cross-link-specific peptidoglycan hydrolase contributes to bacterial morphogenesis.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Bacterial actin and tubulin homologs in cell growth and division.Current biology : CB · 2015Review
- Molecular mechanisms for the evolution of bacterial morphologies and growth modes.Frontiers in microbiology · 2015Review
- AmiA is a penicillin target enzyme with dual activity in the intracellular pathogen Chlamydia pneumoniae.Nature communications · 2014Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The nature and assembly of the chlamydial division septum is poorly defined due to the paucity of a detectable peptidoglycan (PG)-based cell wall, the inhibition of constriction by penicillin and the presence of coding sequences for cell wall precursor and remodelling enzymes in the reduced chlamydial (pan-)genome. Here we show that the chlamydial amidase (AmiA) is active and remodels PG in Escherichia coli. Moreover, forward genetics using an E. coli amidase mutant as entry point reveals that the chlamydial LysM-domain protein NlpD is active in an E. coli reporter strain for PG endopeptidase activity (ΔnlpI). Immunolocalization unveils NlpD as the first septal (cell-wall-binding) protein in Chlamydiae and we show that its septal sequestration depends on prior cell wall synthesis. Since AmiA assembles into peripheral clusters, trimming of a PG-like polymer or precursors occurs throughout the chlamydial envelope, while NlpD targets PG-like peptide crosslinks at the chlamydial septum during constriction.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.