A Unique Bacterial Secretion Machinery with Multiple Secretion Centers

Liqiang Song (1) , John Perpich (2) , Chenggang Wu (3) , Thierry Doan (4) , Zuzanna Nowakowska (5) , Jan Potempa (2, 5) , Peter Christie (3) , E. Cascales (4) , Richard Lamont (2) , Bo Hu (3)

1 Department of Microbiology and Molecular Genetics
2 University of Louisville School of Medicine
3 Department of Microbiology & Molecular Genetics
4 LISM - Laboratoire d'ingénierie des systèmes macromoléculaires
5 UJ - Uniwersytet Jagielloński w Krakowie = Jagiellonian University

The Porphyromonas gingivalis type IX secretion system (T9SS) promotes periodontal disease by secreting gingipains and other virulence factors. By in situ cryoelectron tomography, we report that the P. gingivalisT9SS consists of eighteen PorM dimers arranged as a large caged ring in the periplasm. Near the outer membrane, PorM dimers interact with a PorKN ring complex of ~52 nm in diameter. PorMKN translocation complexes of a given T9SS adopt distinct conformations energized by the proton motive force, suggestive of different activation states. At the inner membrane, PorM associates with a cytoplasmic complex that exhibits 12-fold symmetry and requires both PorM and PorL for assembly. Activated motors deliver substrates across the outer membrane via one of eight Sov translocons arranged in a ring. The T9SSs are unique among known secretion systems in bacteria and eukaryotes in their assembly as supramolecular machines composed of apparently independently-functioning translocation motors and export pores.

Mots clés: type IX secretion; protein transport; proton motive force; cryo-electron tomography

Domaines: Microbiologie et Parasitologie

Liqiang Song, John Perpich, Chenggang Wu, Thierry Doan, Zuzanna Nowakowska, et al.. A Unique Bacterial Secretion Machinery with Multiple Secretion Centers. Proceedings of the National Academy of Sciences of the United States of America, 2022, 119 (18), ⟨10.1073/pnas.2119907119⟩. ⟨hal-03655004⟩