title: Discovery of chlamydial peptidoglycan reveals bacteria with murein sacculi but without FtsZ.
abstract: Chlamydiae are important pathogens and symbionts with unique cell biological features. They lack the cell-division protein FtsZ, and the existence of peptidoglycan (PG) in their cell wall has been highly controversial. FtsZ and PG together function in orchestrating cell division and maintaining cell shape in almost all other bacteria. Using electron cryotomography, mass spectrometry and fluorescent labelling dyes, here we show that some environmental chlamydiae have cell wall sacculi consisting of a novel PG type. Treatment with fosfomycin (a PG synthesis inhibitor) leads to lower infection rates and aberrant cell shapes, suggesting that PG synthesis is crucial for the chlamydial life cycle. Our findings demonstrate for the first time the presence of PG in a member of the Chlamydiae. They also present a unique example of a bacterium with a PG sacculus but without FtsZ, challenging the current hypothesis that it is the absence of a cell wall that renders FtsZ non-essential.
authors.affiliation: Division of Biology, California Institute of Technology, Pasadena, CA 91125, USA.|Howard Hughes Medical Institute.
authors.forename: Martin
authors.initials: M
authors.lastname: Pilhofer
authors.affiliation: Division of Microbial Ecology, University of Vienna, Vienna, A-1090, Austria.
authors.forename: Karin
authors.initials: K
authors.lastname: Aistleitner
authors.affiliation: Institute for Cell and Molecular Biosciences, The Centre for Bacterial Cell Biology, Newcastle University, Newcastle upon Tyne, NE2 4AX, United Kingdom.
authors.forename: Jacob
authors.initials: J
authors.lastname: Biboy
authors.affiliation: Institute for Cell and Molecular Biosciences, Pinnacle Laboratory, Newcastle University, Newcastle upon Tyne, NE2 4AX, United Kingdom.
authors.forename: Joe
authors.initials: J
authors.lastname: Gray
authors.affiliation: Indiana University, Bloomington, IN, 47405, USA.
authors.forename: Erkin
authors.initials: E
authors.lastname: Kuru
authors.affiliation: Indiana University, Bloomington, IN, 47405, USA.
authors.forename: Edward
authors.initials: E
authors.lastname: Hall
authors.affiliation: Indiana University, Bloomington, IN, 47405, USA.
authors.forename: Yves V
authors.initials: YV
authors.lastname: Brun
authors.affiliation: Indiana University, Bloomington, IN, 47405, USA.
authors.forename: Michael S
authors.initials: MS
authors.lastname: VanNieuwenhze
authors.affiliation: Institute for Cell and Molecular Biosciences, The Centre for Bacterial Cell Biology, Newcastle University, Newcastle upon Tyne, NE2 4AX, United Kingdom.
authors.forename: Waldemar
authors.initials: W
authors.lastname: Vollmer
authors.affiliation: Division of Microbial Ecology, University of Vienna, Vienna, A-1090, Austria.
authors.forename: Matthias
authors.initials: M
authors.lastname: Horn
authors.affiliation: Division of Biology, California Institute of Technology, Pasadena, CA 91125, USA.|Howard Hughes Medical Institute.
authors.forename: Grant J
authors.initials: GJ
authors.lastname: Jensen
mesh_terms: D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism*; D002473:Cell Wall / Q000737:chemistry / Q000378:metabolism / Q000648:ultrastructure; D002695:Chlamydiales / Q000737:chemistry / Q000145:classification / Q000378:metabolism* / Q000648:ultrastructure; D003598:Cytoskeletal Proteins / Q000235:genetics / Q000378:metabolism*; D010457:Peptidoglycan / Q000737:chemistry / Q000378:metabolism*
chemical_list: D001426:Bacterial Proteins; D003598:Cytoskeletal Proteins; C071525:FtsZ protein, Bacteria; D010457:Peptidoglycan