| Title | An Iron-Containing Dodecameric Heptosyltransferase Family Modifies Bacterial Autotransporters in Pathogenesis |
| Authors | Lu, Qiuhe Yao, Qing Xu, Yue Li, Lin Li, Shan Liu, Yanhua Gao, Wenqing Niu, Miao Sharon, Michal Ben-Nissan, Gili Zamyatina, Alla Liu, Xiaoyun Chen, She Shao, Feng |
| Affiliation | Natl Inst Biol Sci, Beijing 102206, Peoples R China. China Agr Univ, Coll Biol Sci, Beijing 100094, Peoples R China. Peking Univ, Coll Chem & Mol Engn, Inst Anal Chem & Synthet, Beijing 100871, Peoples R China. Peking Univ, Coll Chem & Mol Engn, Funct Biomol Ctr, Beijing 100871, Peoples R China. Weizmann Inst Sci, Dept Biol Chem, IL-76100 Rehovot, Israel. Univ Nat Resources & Life Sci, Dept Chem, A-1190 Vienna, Austria. Chinese Acad Sci, Inst Biophys, Natl Lab Biomacromol, Beijing 100101, Peoples R China. Beijing Collaborat Innovat Ctr Canc Med, Natl Inst Biol Sci, Beijing 102206, Peoples R China. |
| Keywords | ENTEROTOXIGENIC ESCHERICHIA-COLI PROTEIN GLYCOSYLATION CRYSTAL-STRUCTURE BIOFILM FORMATION ADHESIN SECRETION PATHWAY SYSTEM ADHERENCE VIRULENCE |
| Issue Date | 2014 |
| Publisher | cell host microbe |
| Citation | CELL HOST & MICROBE.2014,16,(3),351-363. |
| Abstract | Autotransporters 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. |
| URI | http://hdl.handle.net/20.500.11897/209197 |
| ISSN | 1931-3128 |
| DOI | 10.1016/j.chom.2014.08.008 |
| Indexed | SCI(E) |
| Appears in Collections: | å å¦ä¸ å å å·¥ç¨ å¦é ¢ |
