ArticleMolecular microbiology2016
A novel flagellar sheath protein, FcpA, determines filament coiling, translational motility and virulence for the Leptospira spirochete.
Article in Molecular microbiology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.
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Who cites it
60 citing papers in PubMed, 89 citations in OpenAlex.
- Core-sheath coupling controls flagellar curvature and motility in Leptospira.Nature communications · 2026Article
- Asymmetric architecture and adaptation of Treponema flagella.Nature communications · 2026Article
- Asymmetric sheath coordination controls flagellar architecture and function in Leptospira spirochete.The EMBO journal · 2026Article
- Core-sheath coupling controls flagellar curvature and motility inbioRxiv : the preprint server for biology · 2026Article
- An ELISA for discovering protein-protein interaction inhibitors: Blocking lysinoalanine crosslinking between subunits of the spirochete flagellar hook as a test case.SLAS discovery : advancing life sciences R & D · 2026Article
- The ancient E-ring in bacterial flagellar motors.FEMS microbiology reviews · 2026Review
- Machine Learning-Based Quantification of Motility Parameters in Individual Leptospira Cells.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Measurement of the Cell-Body Rotation of Leptospira.Methods in molecular biology (Clifton, N.J.) · 2026Article
- In Situ Structural Analysis of Leptospira spp. by Electron Cryotomography.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Cell Monolayer Translocation Assay.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Leptospira spp. Toolbox for Chemotaxis Assay.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Inhibitors of Lysinoalanine Cross-Linking in the Flagella Hook as Antimicrobials against Spirochetes.ACS chemical biology · 2025Article
- Induced protein expression in Leptospira spp. and its application to CRISPR/Cas9 mutant generation.Scientific reports · 2025Article
- FlbB forms a distinctive ring essential for periplasmic flagellar assembly and motility in Borrelia burgdorferi.PLoS pathogens · 2025Article
- Leptospira Leptolysin Contributes to Serum Resistance but Is Not Essential for Acute Infection.Molecular microbiology · 2024Article
- Leptospira interrogans biofilm transcriptome highlights adaption to starvation and general stress while maintaining virulence.NPJ biofilms and microbiomes · 2024Article
- Machine learning-based motion tracking reveals an inverse correlation between adhesivity and surface motility of the leptospirosis spirochete.Nature communications · 2023Article
- Lysinoalanine cross-linking is a conserved post-translational modification in the spirochete flagellar hook.PNAS nexus · 2023Article
- MPL36, a major plasminogen (PLG) receptor in pathogenic Leptospira, has an essential role during infection.PLoS pathogens · 2023Article
- Force Measurement of Bacterial Swimming Using Optical Tweezers.Methods in molecular biology (Clifton, N.J.) · 2023Article
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Authors and funding
12 authors at 6 institutions in 4 countries.
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Abstract
Leptospira are unique among bacteria based on their helical cell morphology with hook-shaped ends and the presence of periplasmic flagella (PF) with pronounced spontaneous supercoiling. The factors that provoke such supercoiling, as well as the role that PF coiling plays in generating the characteristic hook-end cell morphology and motility, have not been elucidated. We have now identified an abundant protein from the pathogen L. interrogans, exposed on the PF surface, and named it Flagellar-coiling protein A (FcpA). The gene encoding FcpA is highly conserved among Leptospira and was not found in other bacteria. fcpA(-) mutants, obtained from clinical isolates or by allelic exchange, had relatively straight, smaller-diameter PF, and were not able to produce translational motility. These mutants lost their ability to cause disease in the standard hamster model of leptospirosis. Complementation of fcpA restored the wild-type morphology, motility and virulence phenotypes. In summary, we identified a novel Leptospira 36-kDa protein, the main component of the spirochete's PF sheath, and a key determinant of the flagella's coiled structure. FcpA is essential for bacterial translational motility and to enable the spirochete to penetrate the host, traverse tissue barriers, disseminate to cause systemic infection and reach target organs.
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