ArticleMolecular microbiology2018
A tetratricopeptide repeat domain protein has profound effects on assembly of periplasmic flagella, morphology and motility of the lyme disease spirochete Borrelia burgdorferi.
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 15 papers.
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Who cites it
15 citing papers in PubMed, 38 citations in OpenAlex.
- Structural insights into the assembly and evolution of a complex bacterial flagellar motor.Nature microbiology · 2026Article
- The ancient E-ring in bacterial flagellar motors.FEMS microbiology reviews · 2026Review
- Secreted LysM proteins are required for niche competition and full virulence in Pseudomonas savastanoi during host plant infection.PLoS pathogens · 2025Article
- Tetrameric PilZ protein stabilizes stator ring in complex flagellar motor and is required for motility inProceedings of the National Academy of Sciences of the United States of America · 2025Article
- FlbB forms a distinctive ring essential for periplasmic flagellar assembly and motility in Borrelia burgdorferi.PLoS pathogens · 2025Article
- Viscosity-dependent determinants ofmBio · 2024Article
- FliL ring enhances the function of periplasmic flagella.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- The Bacterial Flagellar Motor: Insights Into Torque Generation, Rotational Switching, and Mechanosensing.Frontiers in microbiology · 2022Review
- Article
- The Structure, Composition, and Role of Periplasmic Stator Scaffolds in Polar Bacterial Flagellar Motors.Frontiers in microbiology · 2021Review
- BB0259 Encompasses a Peptidoglycan Lytic Enzyme Function for Proper Assembly of Periplasmic Flagella inFrontiers in microbiology · 2021Article
- Structural Conservation and Adaptation of the Bacterial Flagella Motor.Biomolecules · 2020Review
- BB0326 is responsible for the formation of periplasmic flagellar collar and assembly of the stator complex in Borrelia burgdorferi.Molecular microbiology · 2020Article
- Article
- Architecture and Assembly of Periplasmic Flagellum.Microbiology spectrum · 2019Review
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Spirochetes possess a unique periplasmic flagellar motor component called the collar. However, little is known about the composition or function of the flagellar collar proteins. To identify a collar protein, we have inactivated almost all genes annotated as motility-related in the Borrelia burgdorferi genome and identified only FlbB, which comprises the base of the collar. Since the major components of the collar complex remained unidentified, we took advantage of a protein-protein interaction map developed in another spirochete, Treponema pallidum to identify proteins of unknown function that could be collar proteins. Subsequently, using various comprehensive approaches, we identified a tetratricopeptide repeat protein BB0236 as a potential candidate for the collar. Biochemical assays indicated that FlbB interacts with BB0236. Furthermore, ∆bb0236 mutant analyses indicated that BB0236 is crucial for collar structure assembly, cellular morphology, motility, orientation of periplasmic flagella and assembly of other flagellar structures. Moreover, using comparative motor analyses, we propose how the collar structure is assembled in B. burgdorferi. Together, our studies provide new insights into the organization and the complex assembly inherent to the unique spirochetal collar structure.
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Registered trials
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