ArticlePloS one2023
FlgV forms a flagellar motor ring that is required for optimal motility of Helicobacter pylori.
Article in PloS one, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Berberine and Berberine-Derived Compounds as Promising Weapons AgainstPharmaceuticals (Basel, Switzerland) · 2026Review
- TheProceedings of the National Academy of Sciences of the United States of America · 2026Article
- Assembly and glycosylation ofPNAS nexus · 2026Article
- Mutations in the Ferric Uptake Regulator Gene (Microorganisms · 2025Article
- Low pH amplifies chemotaxis toward urea in Helicobacter pylori.Biophysical journal · 2025Article
- The impact of the flagellar protein genemSphere · 2025Article
- FlgY, PflA, and PflB form a spoke-ring network in the high-torque flagellar motor ofProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Broadly conserved FlgV controls flagellar assembly and Borrelia burgdorferi dissemination in mice.Nature communications · 2024Article
- Broadly conserved FlgV controls flagellar assembly andbioRxiv : the preprint server for biology · 2024Article
- Control of the flagellation pattern inJournal of bacteriology · 2023Article
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Authors and funding
6 authors.
Funding
Abstract
Flagella-driven motility is essential for Helicobacter pylori to colonize the human stomach, where it causes a variety of diseases, including chronic gastritis, peptic ulcer disease, and gastric cancer. H. pylori has evolved a high-torque-generating flagellar motor that possesses several accessories not found in the archetypical Escherichia coli motor. FlgV was one of the first flagellar accessory proteins identified in Campylobacter jejuni, but its structure and function remain poorly understood. Here, we confirm that deletion of flgV in H. pylori B128 and a highly motile variant of H. pylori G27 (G27M) results in reduced motility in soft agar medium. Comparative analyses of in-situ flagellar motor structures of wild-type, ΔflgV, and a strain expressing FlgV-YFP showed that FlgV forms a ring-like structure closely associated with the junction of two highly conserved flagellar components: the MS and C rings. The results of our studies suggest that the FlgV ring has adapted specifically in Campylobacterota to support the assembly and efficient function of the high-torque-generating motors.
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