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TitleA highly conserved SusCD transporter determines the import and species-specific antagonism of Bacteroides ubiquitin homologues.
Journal, issue, pagesNat Commun, Vol. 15, Issue 1, Page 8794, Year 2024
Publish dateOct 10, 2024
AuthorsMing Tong / Jinghua Xu / Weixun Li / Kun Jiang / Yan Yang / Zhe Chen / Xuyao Jiao / Xiangfeng Meng / Mingyu Wang / Jie Hong / Hongan Long / Shuang-Jiang Liu / Bentley Lim / Xiang Gao /
PubMed AbstractEfficient interbacterial competitions and diverse defensive strategies employed by various bacteria play a crucial role in acquiring a hold within a dense microbial community. The gut symbiont ...Efficient interbacterial competitions and diverse defensive strategies employed by various bacteria play a crucial role in acquiring a hold within a dense microbial community. The gut symbiont Bacteroides fragilis secretes an antimicrobial ubiquitin homologue (BfUbb) that targets an essential periplasmic PPIase to drive intraspecies bacterial competition. However, the mechanisms by which BfUbb enters the periplasm and its potential for interspecies antagonism remain poorly understood. Here, we employ transposon mutagenesis and identify a highly conserved TonB-dependent transporter SusCD (designated as ButCD) in B. fragilis as the BfUbb transporter. As a putative protein-related nutrient utilization system, ButCD is widely distributed across diverse Bacteroides species with varying sequence similarity, resulting in distinct import efficiency of Bacteroides ubiquitin homologues (BUbb) and thereby determining the species-specific toxicity of BUbb. Cryo-EM structural and functional investigations of the BfUbb-ButCD complex uncover distinctive structural features of ButC that are crucial for its targeting by BfUbb. Animal studies further demonstrate the specific and efficient elimination of enterotoxigenic B. fragilis (ETBF) in the murine gut by BfUbb, suggesting its potential as a therapeutic against ETBF-associated inflammatory bowel disease and colorectal cancer. Our findings provide a comprehensive elucidation of the species-specific toxicity exhibited by BUbb and explore its potential applications.
External linksNat Commun / PubMed:39389974 / PubMed Central
MethodsEM (single particle)
Resolution2.97 - 3.05 Å
Structure data

39493

8ypt

EMDB-39493, PDB-8ypt:
Cryo-EM structure of BfUbb-ButCD complex
Method: EM (single particle) / Resolution: 3.05 Å

39494

8ypu

EMDB-39494, PDB-8ypu:
Cryo-EM structure of ButCD complex
Method: EM (single particle) / Resolution: 2.97 Å

Source
  • bacteroides fragilis (bacteria)
KeywordsMEMBRANE PROTEIN / transporter / TonB-dependent

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