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Journal article

A new paradigm for outer membrane protein biogenesis in the Bacteroidota

Abstract:

In Gram-negative bacteria, the outer membrane is the first line of defence against antimicrobial agents and immunological attacks. A key part of outer membrane biogenesis is the insertion of outer membrane proteins by the β-barrel-assembly machinery (BAM). Here we report the cryo-electron microscopy structure of a BAM complex isolated from Flavobacterium johnsoniae, a member of the Bacteroidota, a phylum that includes key human commensals and major anaerobic pathogens. This BAM complex is extensively modified from the canonical Escherichia coli system and includes an extracellular canopy that overhangs the substrate folding site and a subunit that inserts into the BAM pore. The novel BamG and BamH subunits that are involved in forming the extracellular canopy are required for BAM function and are conserved across the Bacteroidota, suggesting that they form an essential extension to the canonical BAM core in this phylum. For BamH, isolation of a suppressor mutation enables the separation of its essential and non-essential functions. The need for a highly remodelled and enhanced BAM complex reflects the unusually complex membrane proteins found in the outer membrane of the Bacteroidota.

Publication status:
Published
Peer review status:
Peer reviewed

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Publisher copy:
10.1038/s41586-025-09532-8

Authors

More by this author
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
More by this author
Institution:
University of Oxford
Division:
MSD
Department:
Biochemistry
Oxford college:
Wadham College
Role:
Author
ORCID:
0000-0001-9685-4067


More from this funder
Funder identifier:
https://ror.org/0472cxd90
Grant:
833713


Publisher:
Springer Nature
Journal:
Nature More from this journal
Volume:
647
Issue:
8089
Pages:
479–487
Publication date:
2025-10-01
Acceptance date:
2025-08-14
DOI:
EISSN:
1476-4687
ISSN:
0028-0836


Language:
English
Pubs id:
2280716
Local pid:
pubs:2280716
Deposit date:
2025-08-14
ARK identifier:

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