Core–sheath coupling controls flagellar curvature and motility in Leptospira

Abstract

Spirochaete pathogens are among the most invasive bacteria known, causing syphilis, Lyme disease, and leptospirosis. Their tissue penetration depends on periplasmic flagellar filaments that, unlike other bacterial flagella, are encased in a spirochaete-specific multi-protein sheath and deform the cell body into motile waves. How these filaments achieve the mechanical properties needed for invasive motility has remained unclear. Here we determine complete atomic structures of the Leptospira endoflagellar filament, revealing an elaborate sheath of 9 to 12 distinct asymmetrically arranged proteins. We show that the flagellin variant forming the filament core determines sheath composition, producing curvatures ranging from ~3.5 µm −1 to ~5.6 µm −1 . The lower-curvature architecture, employed by pathogenic Leptospira interrogans , proves essential for motility in viscous environments and during infection. Thus, Leptospira achieves environment-specific motility through modular core–sheath coupling, linking atomic-scale structural plasticity to large-scale changes in swimming behaviour. Conservation of key sheath components suggests this mechanism may extend across spirochaetes.

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BibTeX RIS

BibTeX

@article{martin2026coresheath,
  title = {{Core–sheath coupling controls flagellar curvature and motility in Leptospira}},
  author = {Fabiana San Martin and Megan Brady and Lenka Fule and Lucienne Nouchikian and Azalia Rodriguez and Magalie Duchateau and Sonia Mondino and Nicole Larrieux and Elsio Wunder and Albert Ko and Martial Rey and Julia Chamot-Rooke and Rosario Duran and Felipe Trajtenberg and Mathieu Picardeau and Charles Sindelar and Alejandro Buschiazzo},
  journal = {Nature Communications},
  year = {2026},
  month = jul,
  doi = {10.1038/s41467-026-75995-6},
  url = {https://hal.science/hal-05828746v1},
  note = {CC BY 4.0},
}

RIS

TY  - JOUR
TI  - Core–sheath coupling controls flagellar curvature and motility in Leptospira
AU  - Fabiana San Martin
AU  - Megan Brady
AU  - Lenka Fule
AU  - Lucienne Nouchikian
AU  - Azalia Rodriguez
AU  - Magalie Duchateau
AU  - Sonia Mondino
AU  - Nicole Larrieux
AU  - Elsio Wunder
AU  - Albert Ko
AU  - Martial Rey
AU  - Julia Chamot-Rooke
AU  - Rosario Duran
AU  - Felipe Trajtenberg
AU  - Mathieu Picardeau
AU  - Charles Sindelar
AU  - Alejandro Buschiazzo
PY  - 2026
DA  - 2026/07/25
JO  - Nature Communications
DO  - 10.1038/s41467-026-75995-6
UR  - https://hal.science/hal-05828746v1
AB  - Spirochaete pathogens are among the most invasive bacteria known, causing syphilis, Lyme disease, and leptospirosis. Their tissue penetration depends on periplasmic flagellar filaments that, unlike other bacterial flagella, are encased in a spirochaete-specific multi-protein sheath and deform the cell body into motile waves. How these filaments achieve the mechanical properties needed for invasive motility has remained unclear. Here we determine complete atomic structures of the Leptospira endoflagellar filament, revealing an elaborate sheath of 9 to 12 distinct asymmetrically arranged proteins. We show that the flagellin variant forming the filament core determines sheath composition, producing curvatures ranging from ~3.5 µm −1 to ~5.6 µm −1 . The lower-curvature architecture, employed by pathogenic Leptospira interrogans , proves essential for motility in viscous environments and during infection. Thus, Leptospira achieves environment-specific motility through modular core–sheath coupling, linking atomic-scale structural plasticity to large-scale changes in swimming behaviour. Conservation of key sheath components suggests this mechanism may extend across spirochaetes.
SN  - 2041-1723
SN  - 2041-1723
ER  -

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