6gbh
Helicobacter pylori adhesin HopQ type II bound to the N-terminal domain of human CEACAM1Helicobacter pylori adhesin HopQ type II bound to the N-terminal domain of human CEACAM1
Structural highlights
FunctionPublication Abstract from PubMedThe 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 beta-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. Helicobacter pylori adhesin HopQ disrupts trans dimerization in human CEACAMs.,Moonens K, Hamway Y, Neddermann M, Reschke M, Tegtmeyer N, Kruse T, Kammerer R, Mejias-Luque R, Singer BB, Backert S, Gerhard M, Remaut H EMBO J. 2018 Jun 1. pii: embj.201798665. doi: 10.15252/embj.201798665. PMID:29858229[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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