en
Scientific article
Open access
English

FtsZ-independent septal recruitment and function of cell wall remodelling enzymes in chlamydial pathogens

Published inNature communications, vol. 5, 4200
Publication date2014
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.

Citation (ISO format)
FRANDI, Antonio et al. FtsZ-independent septal recruitment and function of cell wall remodelling enzymes in chlamydial pathogens. In: Nature communications, 2014, vol. 5, p. 4200. doi: 10.1038/ncomms5200
Main files (1)
Article (Published version)
accessLevelPublic
Identifiers
ISSN of the journal2041-1723
583views
393downloads

Technical informations

Creation06/24/2014 3:09:00 PM
First validation06/24/2014 3:09:00 PM
Update time03/14/2023 9:23:12 PM
Status update03/14/2023 9:23:12 PM
Last indexation01/16/2024 11:08:54 AM
All rights reserved by Archive ouverte UNIGE and the University of GenevaunigeBlack