ArticleMolecular microbiology2018
The Helicobacter pylori cell shape promoting protein Csd5 interacts with the cell wall, MurF, and the bacterial cytoskeleton.
Article in Molecular microbiology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
18 citing papers in PubMed, 31 citations in OpenAlex.
- Pathogenicity and virulence ofVirulence · 2025Review
- Article
- The Unique N-Terminal Domain of Chlamydial Bactofilin Mediates Its Membrane Localization and Ring-Forming Properties.Journal of bacteriology · 2023Article
- Genetic determinants of Biofilm formation of Helicobacter pylori using whole-genome sequencing.BMC microbiology · 2023Article
- Interacting bactofilins impact cell shape of the MreB-less multicellular Rhodomicrobium vannielii.PLoS genetics · 2023Article
- Distinct regions ofeLife · 2022Article
- Insights Into the Helical Shape Complex ofFrontiers in microbiology · 2022Article
- A Dynamic Network of Proteins Facilitate Cell Envelope Biogenesis in Gram-Negative Bacteria.International journal of molecular sciences · 2021Review
- Morphological change of coiled bacterium Spirosoma linguale with acquisition of β-lactam resistance.Scientific reports · 2021Article
- 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
- Antibiotic susceptibility signatures identify potential antimicrobial targets in the Acinetobacter baumannii cell envelope.Nature communications · 2020Article
- Cell morphology as a virulence determinant: lessons from Helicobacter pylori.Current opinion in microbiology · 2020Review
- Article
- The structure of bactofilin filaments reveals their mode of membrane binding and lack of polarity.Nature microbiology · 2019Article
- A Genome-Wide Helicobacter pylori Morphology Screen Uncovers a Membrane-Spanning Helical Cell Shape Complex.Journal of bacteriology · 2019Article
- Article
- Potential Role of Biofilm Formation in the Development of Digestive Tract Cancer With Special Reference toFrontiers in microbiology · 2019Article
- Peptidoglycan binding by a pocket on the accessory NTF2-domain of Pgp2 directs helical cell shape of Campylobacter jejuni.The Journal of biological chemistryArticle
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 4 institutions in 2 countries.
Funding
Abstract
Chronic infection with Helicobacter pylori can lead to the development of gastric ulcers and stomach cancers. The helical cell shape of H. pylori promotes stomach colonization. Screens for loss of helical shape have identified several periplasmic peptidoglycan (PG) hydrolases and non-enzymatic putative scaffolding proteins, including Csd5. Both over and under expression of the PG hydrolases perturb helical shape, but the mechanism used to coordinate and localize their enzymatic activities is not known. Using immunoprecipitation and mass spectrometry we identified Csd5 interactions with cytosolic proteins CcmA, a bactofilin required for helical shape, and MurF, a PG precursor synthase, as well as the inner membrane spanning ATP synthase. A combination of Csd5 domain deletions, point mutations, and transmembrane domain chimeras revealed that the N-terminal transmembrane domain promotes MurF, CcmA, and ATP synthase interactions, while the C-terminal SH3 domain mediates PG binding. We conclude that Csd5 promotes helical shape as part of a membrane associated, multi-protein shape complex that includes interactions with the periplasmic cell wall, a PG precursor synthesis enzyme, the bacterial cytoskeleton, and ATP synthase.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.