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

Antonio Frandi, Nicolas Jacquier, Laurence Théraulaz, Gilbert Greub and Patrick H. Viollier ()
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Antonio Frandi: Institute of Genetics and Genomics in Geneva (iGE3), Faculty of Medicine/CMU, University of Geneva
Nicolas Jacquier: Center for Research on Intracellular Bacteria (CRIB), Institute of Microbiology, University Hospital Center and University of Lausanne
Laurence Théraulaz: Institute of Genetics and Genomics in Geneva (iGE3), Faculty of Medicine/CMU, University of Geneva
Gilbert Greub: Center for Research on Intracellular Bacteria (CRIB), Institute of Microbiology, University Hospital Center and University of Lausanne
Patrick H. Viollier: Institute of Genetics and Genomics in Geneva (iGE3), Faculty of Medicine/CMU, University of Geneva

Nature Communications, 2014, vol. 5, issue 1, 1-11

Abstract: 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.

Date: 2014
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DOI: 10.1038/ncomms5200

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