n Iron-Containing Dodecameric Heptosyltransferase Family Modifies Bacterial Autotransporters in Pathogenesis
utotransporters deliver virulence factors to the bacterial surface by translocating an effector passenger domain through a membrane-anchored barrel structure. Although passenger domains are diverse, those found in enteric bacteria autotransporters, including AIDA-I in diffusely adhering Escherichia coli (DAEC) and TibA in enterotoxigenic E. coli, are commonly glycosylated. We show that AIDA-I is heptosylated within the bacterial cytoplasm by autotransporter adhesin heptosyltransferase (AAH) and its paralogue AAH2. AIDA-I heptosylation determines DAEC adhesion to host cells. AAH/AAH2 define a bacterial autotransporter heptosyltransferase (BAHT) family that contains ferric ion and adopts a dodecamer assembly. Structural analyses of the heptosylated TibA passenger domain reveal 35 heptose conjugates forming patterned and solenoid-like arrays on the surface of a beta helix. Additionally, CARC, the AIDA-like autotransporter from Citrobacter rodentium, is essential for colonization in mice and requires heptosylation by its cognate BAHT. Our study establishes a bacterial glycosylation system that regulates virulence and is essential for pathogenesis.
utotransporters deliver virulence factors to the bacterial surface by translocating an effector passenger domain through a membrane-anchored barrel structure. Although passenger domains are diverse, those found in enteric bacteria autotransporters, including AIDA-I in diffusely adhering Escherichia coli (DAEC) and TibA in enterotoxigenic E. coli, are commonly glycosylated. We show that AIDA-I is heptosylated within the bacterial cytoplasm by autotransporter adhesin heptosyltransferase (AAH) and its paralogue AAH2. AIDA-I heptosylation determines DAEC adhesion to host cells. AAH/AAH2 define a bacterial autotransporter heptosyltransferase (BAHT) family that contains ferric ion and adopts a dodecamer assembly. Structural analyses of the heptosylated TibA passenger domain reveal 35 heptose conjugates forming patterned and solenoid-like arrays on the surface of a beta helix. Additionally, CARC, the AIDA-like autotransporter from Citrobacter rodentium, is essential for colonization in mice and requires heptosylation by its cognate BAHT. Our study establishes a bacterial glycosylation system that regulates virulence and is essential for pathogenesis.
Liu, Xiaoyun、Niu, Miao、Ben-Nissan, Gili、Lu, Qiuhe、Gao, Wenqing、Li, Shan、Li, Lin、Shao, Feng、Xu, Yue、Chen, She、Liu, Xiaoyun、Zamyatina, Alla、Sharon, Michal、Liu, Yanhua、Liu, Yanhua、Shao, Feng、Yao, Qing、Shao, Feng、Xu, Yue
微生物学分子生物学生物化学
ENTEROTOXIGENIC ESCHERICHIA-COLIPROTEIN GLYCOSYLATIONRYSTAL-STRUCTUREBIOFILM FORMATIONHESINSECRETIONPATHWAYSYSTEMHERENCEVIRULENCE
Liu, Xiaoyun,Niu, Miao,Ben-Nissan, Gili,Lu, Qiuhe,Gao, Wenqing,Li, Shan,Li, Lin,Shao, Feng,Xu, Yue,Chen, She,Liu, Xiaoyun,Zamyatina, Alla,Sharon, Michal,Liu, Yanhua,Liu, Yanhua,Shao, Feng,Yao, Qing,Shao, Feng,Xu, Yue.n Iron-Containing Dodecameric Heptosyltransferase Family Modifies Bacterial Autotransporters in Pathogenesis[EB/OL].(2016-05-18)[2025-04-25].https://chinaxiv.org/abs/201605.01804.点此复制
评论