ArticlePLoS pathogens2009
A novel system of cytoskeletal elements in the human pathogen Helicobacter pylori.
Article in PLoS pathogens, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.
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Who cites it
51 citing papers in PubMed, 76 citations in OpenAlex.
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- Assembly properties of bacterial actin MreB involved in Spiroplasma swimming motility.The Journal of biological chemistry · 2023Article
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- Insights Into the Helical Shape Complex ofFrontiers in microbiology · 2022Article
- Structural Determinants and Their Role in Cyanobacterial Morphogenesis.Life (Basel, Switzerland) · 2020Review
- A bacterial cytolinker couples positioning of magnetic organelles to cell shape control.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Cell morphology as a virulence determinant: lessons from Helicobacter pylori.Current opinion in microbiology · 2020Review
- Identification and characterization of novel filament-forming proteins in cyanobacteria.Scientific reports · 2020Article
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- Cultivation and functional characterization of 79 planctomycetes uncovers their unique biology.Nature microbiology · 2020Article
- Role of Bacterial Cytoskeleton and Other Apparatuses in Cell Communication.Frontiers in molecular biosciences · 2020Review
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- The Diverse Functional Roles of Elongation Factor Tu (EF-Tu) in Microbial Pathogenesis.Frontiers in microbiology · 2019Review
- Affinity to cellulose is a shared property among coiled-coil domains of intermediate filaments and prokaryotic intermediate filament-like proteins.Scientific reports · 2018Article
- Prokaryotic cytoskeletons: protein filaments organizing small cells.Nature reviews. Microbiology · 2018Review
- Review
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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.
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