A novel system of cytoskeletal elements in the human pathogen Helicobacter pylori.

Pathogenicity of the human pathogen Helicobacter pylori relies upon its capacity to adapt to a hostile environment and to escape from the host response. Therefore, cell shape, motility, and pH homeostasis of these bacteria are specifically adapted to the gastric mucus. We have found that the helical...

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Autores principales: Barbara Waidner, Mara Specht, Felix Dempwolff, Katharina Haeberer, Sarah Schaetzle, Volker Speth, Manfred Kist, Peter L Graumann
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Publicado: Public Library of Science (PLoS) 2009
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Acceso en línea:https://doaj.org/article/d136a8dbf2434620a8d128ba15d2e5cf
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spelling oai:doaj.org-article:d136a8dbf2434620a8d128ba15d2e5cf2021-11-25T05:48:29ZA novel system of cytoskeletal elements in the human pathogen Helicobacter pylori.1553-73661553-737410.1371/journal.ppat.1000669https://doaj.org/article/d136a8dbf2434620a8d128ba15d2e5cf2009-11-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/19936218/?tool=EBIhttps://doaj.org/toc/1553-7366https://doaj.org/toc/1553-7374Pathogenicity of the human pathogen Helicobacter pylori relies upon its capacity to adapt to a hostile environment and to escape from the host response. Therefore, cell shape, motility, and pH homeostasis of these bacteria are specifically adapted to the gastric mucus. We have found that the helical shape of H. pylori depends on coiled coil rich proteins (Ccrp), which form extended filamentous structures in vitro and in vivo, and are differentially required for the maintenance of cell morphology. We have developed an in vivo localization system for this pathogen. Consistent with a cytoskeleton-like structure, Ccrp proteins localized in a regular punctuate and static pattern within H. pylori cells. Ccrp genes show a high degree of sequence variation, which could be the reason for the morphological diversity between H. pylori strains. In contrast to other bacteria, the actin-like MreB protein is dispensable for viability in H. pylori, and does not affect cell shape, but cell length and chromosome segregation. In addition, mreB mutant cells displayed significantly reduced urease activity, and thus compromise a major pathogenicity factor of H. pylori. Our findings reveal that Ccrp proteins, but not MreB, affect cell morphology, while both cytoskeletal components affect the development of pathogenicity factors and/or cell cycle progression.Barbara WaidnerMara SpechtFelix DempwolffKatharina HaebererSarah SchaetzleVolker SpethManfred KistPeter L GraumannPublic Library of Science (PLoS)articleImmunologic diseases. AllergyRC581-607Biology (General)QH301-705.5ENPLoS Pathogens, Vol 5, Iss 11, p e1000669 (2009)
institution DOAJ
collection DOAJ
language EN
topic Immunologic diseases. Allergy
RC581-607
Biology (General)
QH301-705.5
spellingShingle Immunologic diseases. Allergy
RC581-607
Biology (General)
QH301-705.5
Barbara Waidner
Mara Specht
Felix Dempwolff
Katharina Haeberer
Sarah Schaetzle
Volker Speth
Manfred Kist
Peter L Graumann
A novel system of cytoskeletal elements in the human pathogen Helicobacter pylori.
description Pathogenicity of the human pathogen Helicobacter pylori relies upon its capacity to adapt to a hostile environment and to escape from the host response. Therefore, cell shape, motility, and pH homeostasis of these bacteria are specifically adapted to the gastric mucus. We have found that the helical shape of H. pylori depends on coiled coil rich proteins (Ccrp), which form extended filamentous structures in vitro and in vivo, and are differentially required for the maintenance of cell morphology. We have developed an in vivo localization system for this pathogen. Consistent with a cytoskeleton-like structure, Ccrp proteins localized in a regular punctuate and static pattern within H. pylori cells. Ccrp genes show a high degree of sequence variation, which could be the reason for the morphological diversity between H. pylori strains. In contrast to other bacteria, the actin-like MreB protein is dispensable for viability in H. pylori, and does not affect cell shape, but cell length and chromosome segregation. In addition, mreB mutant cells displayed significantly reduced urease activity, and thus compromise a major pathogenicity factor of H. pylori. Our findings reveal that Ccrp proteins, but not MreB, affect cell morphology, while both cytoskeletal components affect the development of pathogenicity factors and/or cell cycle progression.
format article
author Barbara Waidner
Mara Specht
Felix Dempwolff
Katharina Haeberer
Sarah Schaetzle
Volker Speth
Manfred Kist
Peter L Graumann
author_facet Barbara Waidner
Mara Specht
Felix Dempwolff
Katharina Haeberer
Sarah Schaetzle
Volker Speth
Manfred Kist
Peter L Graumann
author_sort Barbara Waidner
title A novel system of cytoskeletal elements in the human pathogen Helicobacter pylori.
title_short A novel system of cytoskeletal elements in the human pathogen Helicobacter pylori.
title_full A novel system of cytoskeletal elements in the human pathogen Helicobacter pylori.
title_fullStr A novel system of cytoskeletal elements in the human pathogen Helicobacter pylori.
title_full_unstemmed A novel system of cytoskeletal elements in the human pathogen Helicobacter pylori.
title_sort novel system of cytoskeletal elements in the human pathogen helicobacter pylori.
publisher Public Library of Science (PLoS)
publishDate 2009
url https://doaj.org/article/d136a8dbf2434620a8d128ba15d2e5cf
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