SwePub
Sök i LIBRIS databas

  Extended search

onr:"swepub:oai:DiVA.org:umu-162887"
 

Search: onr:"swepub:oai:DiVA.org:umu-162887" > A SpoIID Homolog Cl...

  • 1 of 1
  • Previous record
  • Next record
  •    To hitlist

A SpoIID Homolog Cleaves Glycan Strands at the Chlamydial Division Septum

Jacquier, Nicolas (author)
Yadav, Akhilesh K. (author)
Umeå universitet,Institutionen för molekylärbiologi (Medicinska fakulteten),Molekylär Infektionsmedicin, Sverige (MIMS)
Pillonel, Trestan (author)
show more...
Viollier, Patrick H. (author)
Cava, Felipe (author)
Umeå universitet,Molekylär Infektionsmedicin, Sverige (MIMS),Institutionen för molekylärbiologi (Medicinska fakulteten)
Greub, Gilbert (author)
show less...
 (creator_code:org_t)
American Society for Microbiology (ASM), 2019
2019
English.
In: mBio. - : American Society for Microbiology (ASM). - 2161-2129 .- 2150-7511. ; 10:4
  • Journal article (peer-reviewed)
Abstract Subject headings
Close  
  • 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 Chiamydiales. 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. IMPORTANCE Chlamydiales 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.

Subject headings

MEDICIN OCH HÄLSOVETENSKAP  -- Medicinska och farmaceutiska grundvetenskaper -- Mikrobiologi inom det medicinska området (hsv//swe)
MEDICAL AND HEALTH SCIENCES  -- Basic Medicine -- Microbiology in the medical area (hsv//eng)

Keyword

Chlamydiales
Waddlia chondrophila
cell division
peptidoglycan
sporulation

Publication and Content Type

ref (subject category)
art (subject category)

Find in a library

  • mBio (Search for host publication in LIBRIS)

To the university's database

  • 1 of 1
  • Previous record
  • Next record
  •    To hitlist

Find more in SwePub

By the author/editor
Jacquier, Nicola ...
Yadav, Akhilesh ...
Pillonel, Tresta ...
Viollier, Patric ...
Cava, Felipe
Greub, Gilbert
About the subject
MEDICAL AND HEALTH SCIENCES
MEDICAL AND HEAL ...
and Basic Medicine
and Microbiology in ...
Articles in the publication
mBio
By the university
Umeå University

Search outside SwePub

Kungliga biblioteket hanterar dina personuppgifter i enlighet med EU:s dataskyddsförordning (2018), GDPR. Läs mer om hur det funkar här.
Så här hanterar KB dina uppgifter vid användning av denna tjänst.

 
pil uppåt Close

Copy and save the link in order to return to this view