Discovery of chlamydial peptidoglycan reveals bacteria with murein sacculi but without FtsZ
Martin Pilhofer,
Karin Aistleitner,
Jacob Biboy,
Joe Gray,
Erkin Kuru,
Edward Hall,
Yves V. Brun,
Michael S. VanNieuwenhze,
Waldemar Vollmer,
Matthias Horn () and
Grant J. Jensen ()
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Martin Pilhofer: California Institute of Technology
Karin Aistleitner: University of Vienna
Jacob Biboy: Institute for Cell and Molecular Biosciences, The Centre for Bacterial Cell Biology, Newcastle University
Joe Gray: Institute for Cell and Molecular Biosciences, Pinnacle Laboratory, Newcastle University
Erkin Kuru: Indiana University
Edward Hall: Indiana University
Yves V. Brun: Indiana University
Michael S. VanNieuwenhze: Indiana University
Waldemar Vollmer: Institute for Cell and Molecular Biosciences, The Centre for Bacterial Cell Biology, Newcastle University
Matthias Horn: University of Vienna
Grant J. Jensen: California Institute of Technology
Nature Communications, 2013, vol. 4, issue 1, 1-7
Abstract:
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.
Date: 2013
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Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:4:y:2013:i:1:d:10.1038_ncomms3856
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DOI: 10.1038/ncomms3856
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