Helicobacter pylori adhesin HopQ engages in a virulence-enhancing interaction with human CEACAMs

Anahita Javaheri, Tobias Kruse, Kristof Moones, Raquel Mejías-Luque, Ayla Debraekeleer, Isabell Asche, Nicole Tegtmeyer, Behnam Kalali, Nina Bach, Stephan A. Sieber, Darryl Hill, Verena Königer, Christof R. Hauck, Roman Moskalenko, Rainer Haas, Dirk H. Busch, Esther Klaile, Hortense Slevogt, Alexej Schmidt, Steffen BackertHan Remaut, Bernhard B. Singer, Markus Gerhard

Research output: Contribution to journalArticle (Academic Journal)peer-review

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Helicobacter pylori specifically colonizes the human gastric epithelium and is the major causative agent for ulcer disease and gastric cancer development. Here we identified members of the carcinoembryonic antigen-related cell adhesion molecule (CEACAM) family as receptors of H. pylori and show that HopQ is the surface-exposed adhesin that specifically binds human CEACAM1, CEACAM3, CEACAM5 and CEACAM6. HopQ - CEACAM binding is glycan-independent and targeted to the N-domain. H. pylori binding induces CEACAM1 mediated signaling, and the HopQ-CEACAM1 interaction enables translocation of the virulence factor CagA into host cells, and enhances the release of pro-inflammatory mediators such as interleukin-8. Based on the crystal structure of HopQ, we found that a β-hairpin insertion (HopQ-ID) in HopQ’s extracellular 3+4 helix bundle domain is important for CEACAM binding. A peptide derived from this domain competitively inhibits HopQ-mediated activation of the Cag virulence pathway, as genetic or antibody-mediated abrogation of the HopQ function shows. Together, our data imply the HopQ-CEACAM1 interaction as potentially promising novel therapeutic target to combat H. pylori-associated diseases.
Original languageEnglish
Article number16189
JournalNature Microbiology
Publication statusPublished - 17 Oct 2016


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