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A shared mechanism for Bacteroidota protein transport and gliding motility

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.
Publication status:
Published
Peer review status:
Peer reviewed

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Publisher copy:
10.1038/s41467-025-65003-8

Authors

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Institution:
University of Oxford
Division:
MSD
Department:
Biochemistry
Role:
Author
ORCID:
0000-0002-3448-7406
More by this author
Institution:
University of Oxford
Division:
MSD
Department:
Biochemistry
Role:
Author
ORCID:
0009-0002-5126-4252
More by this author
Role:
Author
ORCID:
0000-0001-8811-9871
More by this author
Institution:
University of Oxford
Division:
MSD
Department:
Biochemistry
Role:
Author
ORCID:
0009-0006-0510-4644
More by this author
Institution:
University of Oxford
Division:
MSD
Department:
Biochemistry
Role:
Author
ORCID:
0000-0001-8854-6937


More from this funder
Funder identifier:
https://ror.org/0472cxd90
Grant:
833713
More from this funder
Funder identifier:
https://ror.org/00cwqg982
Grant:
BB/S007474/1


Publisher:
Springer Nature
Journal:
Nature Communications More from this journal
Volume:
16
Issue:
1
Article number:
10217
Publication date:
2025-11-20
Acceptance date:
2025-09-29
DOI:
EISSN:
2041-1723


Language:
English
Pubs id:
2295214
Local pid:
pubs:2295214
Deposit date:
2025-09-29
ARK identifier:

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