A SpoIID Homolog Cleaves Glycan Strands at the Chlamydial Division Septum.

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License: CC BY 4.0
Serval ID
serval:BIB_F0458DD5EDF3
Type
Article: article from journal or magazin.
Collection
Publications
Institution
Title
A SpoIID Homolog Cleaves Glycan Strands at the Chlamydial Division Septum.
Journal
mBio
Author(s)
Jacquier N., Yadav A.K., Pillonel T., Viollier P.H., Cava F., Greub G.
ISSN
2150-7511 (Electronic)
Publication state
Published
Issued date
16/07/2019
Peer-reviewed
Oui
Volume
10
Number
4
Language
english
Notes
Publication types: Journal Article ; Research Support, Non-U.S. Gov't
Publication Status: epublish
Abstract
Chlamydiales species are obligate intracellular bacteria lacking a classical peptidoglycan sacculus but relying on peptidoglycan synthesis for cytokinesis. While septal peptidoglycan biosynthesis seems to be regulated by MreB actin and its membrane anchor RodZ rather than FtsZ tubulin in Chlamydiales, the mechanism of peptidoglycan remodeling is poorly understood. An amidase conserved in Chlamydiales is able to cleave peptide stems in peptidoglycan, but it is not clear how peptidoglycan glycan strands are cleaved since no classical lytic transglycosylase is encoded in chlamydial genomes. However, a protein containing a SpoIID domain, known to possess transglycosylase activity in Bacillus subtilis, is conserved in Chlamydiales We show here that the SpoIID homologue of the Chlamydia-related pathogen Waddlia chondrophila is a septal peptidoglycan-binding protein. Moreover, we demonstrate that SpoIID acts as a lytic transglycosylase on peptidoglycan and as a muramidase on denuded glycan strands in vitro As SpoIID-like proteins are widespread in nonsporulating bacteria, SpoIID might commonly be a septal peptidoglycan remodeling protein in bacteria, including obligate intracellular pathogens, and thus might represent a promising drug target.IMPORTANCEChlamydiales species are obligate intracellular bacteria and important human pathogens that have a minimal division machinery lacking the proteins that are essential for bacterial division in other species, such as FtsZ. Chlamydial division requires synthesis of peptidoglycan, which forms a ring at the division septum and is rapidly turned over. However, little is known of peptidoglycan degradation, because many peptidoglycan-degrading enzymes are not encoded by chlamydial genomes. Here we show that an homologue of SpoIID, a peptidoglycan-degrading enzyme involved in sporulation of bacteria such as Bacillus subtilis, is expressed in Chlamydiales, localizes at the division septum, and degrades peptidoglycan in vitro, indicating that SpoIID is not only involved in sporulation but also likely implicated in division of some bacteria.
Keywords
Amino Acid Sequence, Bacterial Proteins/chemistry, Bacterial Proteins/metabolism, Cell Division, Chlamydia/genetics, Chlamydia/metabolism, Chlamydia Infections/microbiology, Chromatography, High Pressure Liquid, Gene Expression, Humans, Peptidoglycan/chemistry, Peptidoglycan/metabolism, Protein Binding, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, Spores, Bacterial, Chlamydiales, Waddlia chondrophila, cell division, peptidoglycan, sporulation
Pubmed
Web of science
Open Access
Yes
Create date
18/07/2019 9:07
Last modification date
03/05/2020 7:02
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