A Novel System of Cytoskeletal Elements in the Human Pathogen Helicobacter pylori. Waidner, B., Specht, M., Dempwolff, F., Haeberer, K., Schaetzle, S., Speth, V., Kist, M., & Graumann, P. L. PLoS Pathog, 5(11):e1000669, November, 2009. ![A Novel System of Cytoskeletal Elements in the Human Pathogen Helicobacter pylori [link]](https://bibbase.org/img/filetypes/link.svg "link")
Paper doi abstract bibtex Author Summary The human pathogen Helicobacter pylori lives in the hostile environment of the human stomach. H. pylori possesses a spiral shape and high motility that enable the bacterium to swim through the stomach lumen and to come into close contact with epithelial cells. High urease activity in the bacterium counterbalances the low pH within the stomach, in order to persist within the viscous mucus layer. In this work, we analysed the molecular basis of the spiral structure of H. pylori. We demonstrate that the helical cell shape depends on so called coiled coil rich proteins (Ccrp), which form extended filamentous structures in vitro and in vivo, and are differentially required for the maintenance of proper cell morphology. In most bacteria analysed so far, the actin-like protein MreB affects cell morphology. Contrarily, H. pylori MreB is not involved in the maintenance of cell shape, but affects the progression of the cell cycle. Mutant cells were highly elongated, characteristic for a delay in cell division, and contained non-segregated chromosomes. The persistence of H. pylori in the hostile environment of the human stomach depends on the activity of urease. Interestingly, mreB mutant cells displayed significantly reduced urease activity, revealing a novel connection between the cytoskeletal element and an enzyme, and thus with pathogenicity. These experiments show that H. pylori has a novel type of system setting up helical cell shape, which has not yet been described for any bacterium. Our work will allow studying H. pylori cell cycle and pathogenicity at a new visual level.
@article{waidner_novel_2009,
title = {A {Novel} {System} of {Cytoskeletal} {Elements} in the {Human} {Pathogen} {Helicobacter} pylori},
volume = {5},
url = {http://dx.doi.org/10.1371/journal.ppat.1000669},
doi = {10.1371/journal.ppat.1000669},
abstract = {Author Summary
The human pathogen Helicobacter pylori lives in the hostile environment of the human stomach. H. pylori possesses a spiral shape and high motility that enable the bacterium to swim through the stomach lumen and to come into close contact with epithelial cells. High urease activity in the bacterium counterbalances the low pH within the stomach, in order to persist within the viscous mucus layer. In this work, we analysed the molecular basis of the spiral structure of H. pylori. We demonstrate that the helical cell shape depends on so called coiled coil rich proteins (Ccrp), which form extended filamentous structures in vitro and in vivo, and are differentially required for the maintenance of proper cell morphology. In most bacteria analysed so far, the actin-like protein MreB affects cell morphology. Contrarily, H. pylori MreB is not involved in the maintenance of cell shape, but affects the progression of the cell cycle. Mutant cells were highly elongated, characteristic for a delay in cell division, and contained non-segregated chromosomes. The persistence of H. pylori in the hostile environment of the human stomach depends on the activity of urease. Interestingly, mreB mutant cells displayed significantly reduced urease activity, revealing a novel connection between the cytoskeletal element and an enzyme, and thus with pathogenicity. These experiments show that H. pylori has a novel type of system setting up helical cell shape, which has not yet been described for any bacterium. Our work will allow studying H. pylori cell cycle and pathogenicity at a new visual level.},
number = {11},
urldate = {2015-01-19TZ},
journal = {PLoS Pathog},
author = {Waidner, Barbara and Specht, Mara and Dempwolff, Felix and Haeberer, Katharina and Schaetzle, Sarah and Speth, Volker and Kist, Manfred and Graumann, Peter L.},
month = nov,
year = {2009},
pages = {e1000669}
}
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