Bacteroides fragilis ubiquitin homologue drives intraspecies bacterial competition in the gut microbiome.
Autor: | Jiang K; State Key Laboratory of Microbial Technology, Shandong University, Qingdao, China., Li W; State Key Laboratory of Microbial Technology, Shandong University, Qingdao, China., Tong M; State Key Laboratory of Microbial Technology, Shandong University, Qingdao, China., Xu J; State Key Laboratory of Microbial Technology, Shandong University, Qingdao, China., Chen Z; State Key Laboratory of Microbial Technology, Shandong University, Qingdao, China., Yang Y; State Key Laboratory of Microbial Technology, Shandong University, Qingdao, China., Zang Y; State Key Laboratory of Microbial Technology, Shandong University, Qingdao, China., Jiao X; State Key Laboratory of Microbial Technology, Shandong University, Qingdao, China., Liu C; State Key Laboratory of Microbial Technology, Shandong University, Qingdao, China., Lim B; Department of Microbial Pathogenesis and Microbial Sciences Institute, Yale University School of Medicine, New Haven, CT, USA., Jiang X; Microbiome Research Center, Moon (Guangzhou) Biotech Co. Ltd., Guangzhou, China., Wang J; State Key Laboratory of Membrane Biology, Beijing Advanced Innovation Center for Structural Biology, School of Life Sciences, Tsinghua University, Beijing, China., Wu D; State Key Laboratory of Microbial Technology, Shandong University, Qingdao, China., Wang M; State Key Laboratory of Microbial Technology, Shandong University, Qingdao, China., Liu SJ; State Key Laboratory of Microbial Technology, Shandong University, Qingdao, China.; State Key Laboratory of Microbial Resources, Institute of Microbiology, Chinese Academy of Sciences, Beijing, China., Shao F; National Institute of Biological Sciences, Beijing, China., Gao X; State Key Laboratory of Microbial Technology, Shandong University, Qingdao, China. xgao@email.sdu.edu.cn. |
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Jazyk: | angličtina |
Zdroj: | Nature microbiology [Nat Microbiol] 2024 Jan; Vol. 9 (1), pp. 70-84. Date of Electronic Publication: 2023 Dec 11. |
DOI: | 10.1038/s41564-023-01541-5 |
Abstrakt: | Interbacterial antagonism and associated defensive strategies are both essential during bacterial competition. The human gut symbiont Bacteroides fragilis secretes a ubiquitin homologue (BfUbb) that is toxic to a subset of B. fragilis strains in vitro. In the present study, we demonstrate that BfUbb lyses certain B. fragilis strains by non-covalently binding and inactivating an essential peptidyl-prolyl isomerase (PPIase). BfUbb-sensitivity profiling of B. fragilis strains revealed a key tyrosine residue (Tyr119) in the PPIase and strains that encode a glutamic acid residue at Tyr119 are resistant to BfUbb. Crystal structural analysis and functional studies of BfUbb and the BfUbb-PPIase complex uncover a unique disulfide bond at the carboxy terminus of BfUbb to mediate the interaction with Tyr119 of the PPIase. In vitro coculture assays and mouse studies show that BfUbb confers a competitive advantage for encoding strains and this is further supported by human gut metagenome analyses. Our findings reveal a previously undescribed mechanism of bacterial intraspecies competition. (© 2023. The Author(s), under exclusive licence to Springer Nature Limited.) |
Databáze: | MEDLINE |
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