A shared mechanism for Bacteroidota protein transport and gliding motility

Xiaolong Liu (), Marieta Avramova, Justin C. Deme, Rachel L. Jones, Camilla A. K. Lundgren, Susan M. Lea () and Ben C. Berks ()
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Xiaolong Liu: University of Oxford, Department of Biochemistry
Marieta Avramova: University of Oxford, Department of Biochemistry
Justin C. Deme: National Cancer Institute, Center for Structural Biology, Center for Cancer Research
Rachel L. Jones: University of Oxford, Department of Biochemistry
Camilla A. K. Lundgren: University of Oxford, Department of Biochemistry
Susan M. Lea: National Cancer Institute, Center for Structural Biology, Center for Cancer Research
Ben C. Berks: University of Oxford, Department of Biochemistry

Nature Communications, 2025, vol. 16, issue 1, 1-17

Abstract: Abstract Bacteria of the phylum Bacteroidota are major human commensals and pathogens in addition to being abundant members of the wider biosphere. Bacteroidota move by gliding and they export proteins using the Type 9 Secretion System (T9SS). Here we discover that gliding motility and the T9SS share an unprecedented mechanism of energisation in which outer membrane proteins are covalently attached by disulfide bonds to a moving internal track structure that propels them laterally through the membrane. We determined the structure of an exemplar Bacteroidota mobile track by obtaining the cryoEM structure of a 3 MDa circular mini-track from Porphyromonas gingivalis. Our discoveries identify a mechanistic and evolutionary link between gliding motility and T9SS-dependent protein transport.

Date: 2025
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DOI: 10.1038/s41467-025-65003-8

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