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TitleFlgV forms a flagellar motor ring that is required for optimal motility of Helicobacter pylori.
Journal, issue, pagesPLoS One, Vol. 18, Issue 11, Page e0287514, Year 2023
Publish dateNov 17, 2023
AuthorsJack M Botting / Shoichi Tachiyama / Katherine H Gibson / Jun Liu / Vincent J Starai / Timothy R Hoover /
PubMed AbstractFlagella-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 ...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.
External linksPLoS One / PubMed:37976320 / PubMed Central
MethodsEM (subtomogram averaging)
Resolution31.0 Å
Structure data

EMDB-40219: A subtomogram averaged structure of Helicobacter pylori flagellar motor from a flgV deletion mutant.
Method: EM (subtomogram averaging) / Resolution: 31.0 Å

Source
  • Helicobacter pylori B128 (bacteria)

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