Helicobacter pylori adhesin HopQ disrupts trans dimerization in human CEACAMs.

ABSTRACT: The human gastric pathogen Helicobacter pylori is a major causative agent of gastritis, peptic ulcer disease, and gastric cancer. As part 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 β-strands G, F, and C of C1ND, which form t

SUBMITTER: Moonens K 

PROVIDER: S-EPMC6028033 | biostudies-literature | 2018 Jul

REPOSITORIES: biostudies-literature