期刊
EMBO JOURNAL
卷 37, 期 13, 页码 -出版社
WILEY
DOI: 10.15252/embj.201798665
关键词
bacterial adhesion; CagA delivery; CEACAM1; Helicobacter pylori; HopQ
资金
- VIB
- Flanders Science Foundation (FWO) through the Odysseus programme
- Hercules Funds [UABR/09/005]
- German Science Foundation [CRC-1181, TE776/3-1]
- DFG [GE 2042/5-1, SI-1558/3-1]
The human gastric pathogen Helicobacter pylori is a major causative agent of gastritis, peptic ulcer disease, and gastric cancer. Aspart of its adhesive lifestyle, the bacterium targets members of the carcinoembryonic antigen-related cell adhesion molecule (CEACAM) family by the conserved outer membrane adhesin HopQ. The HopQ-CEACAM1 interaction is associated with inflammatory responses and enables the intracellular delivery and phosphorylation of the CagA oncoprotein via a yet unknown mechanism. Here, we generated crystal structures of HopQ isotypes I and II bound to the N-terminal domain of human CEACAM1 (C1ND) and elucidated the structural basis of H. pylori specificity toward human CEACAM receptors. Both HopQ alleles target the - strands G, F, and C of C1ND, which form the trans dimerization interface in homo- and heterophilic CEACAM interactions. Using SAXS, we show that the HopQ ectodomain is sufficient to induce C1ND monomerization and thus providing H. pylori a route to influence CEACAM-mediated cell adherence and signaling events.
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