脆弱类杆菌
生物
微生物学
微生物群
泛素
基因组
生物化学
遗传学
基因
抗生素
作者
Kun Jiang,Weixun Li,Ming Tong,Jinghua Xu,Zhe Chen,Yan Yang,Yuanrong Zang,Xuyao Jiao,Chang Liu,Bentley Lim,Xianzhi Jiang,Jiawei Wang,Dalei Wu,Mingyu Wang,Shuang‐Jiang Liu,Feng Shao,Xiang Gao
出处
期刊:Nature microbiology
日期:2023-12-11
卷期号:9 (1): 70-84
被引量:7
标识
DOI:10.1038/s41564-023-01541-5
摘要
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. The Bacteroides fragilis ubiquitin homologue, BfUbb, mediates intraspecies competition and provides a competitive advantage for encoding strains in the gut.
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