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Open AccessArticle

Cysteine Residues in Helicobacter pylori Adhesin HopQ Are Required for CEACAM–HopQ Interaction and Subsequent CagA Translocation

1
Institute for Medical Microbiology, Immunology and Hygiene, Technical University Munich, 81675 Munich, Germany
2
Structural and Molecular Microbiology, VIB-VUB Center for Structural Biology, VIB, 1050 Brussels, Belgium
3
Department for Bioengineering Sciences, Structural Biology Brussels, Vrije Universiteit Brussel, 1050 Brussels, Belgium
4
Med. Mikrobiology and KH-Hygiene, Max von Pettenkofer-Institute, Ludwig-Maximilians-Universität, 80336 Munich, Germany
5
Institute of Anatomy, Medical Faculty, University of Duisburg-Essen, 45147 Essen, Germany
6
German Center for Infection Research (DZIF), partner site Munich, 81675 Munich, Germany
*
Author to whom correspondence should be addressed.
Microorganisms 2020, 8(4), 465; https://doi.org/10.3390/microorganisms8040465
Received: 12 February 2020 / Revised: 20 March 2020 / Accepted: 24 March 2020 / Published: 25 March 2020
(This article belongs to the Special Issue Helicobacter pylori Infection and Host Defense Mechanism)
Attachment to the host gastric mucosa is a key step in Helicobacter pylori infection. Recently, a novel adhesin, HopQ, was shown to bind distinct host CEACAM proteins—an interaction that was found to be essential for the translocation of CagA, a key virulence factor of H. pylori. The HopQ–CEACAM1 co-crystal structure revealed a binding mode dependent on loops in HopQ that are clasped by disulfide bonds. In this study, we investigated the importance of these cysteine residues for CEACAM1 engagement by H. pylori. We observed a loss of CEACAM1 binding and CagA translocation upon disruption of the disulfide bond in loop CL1 (connecting C103 to C132 in HopQ). Deletion of the Dsb-like oxidoreductase HP0231 did not affect cell surface expression of HopQ or alter the interaction of H. pylori with target cells. Although HP0231 deletion was previously described to impede CagA translocation, our results indicate that this occurs through a HopQ-independent mechanism. Together, our results open up new avenues to therapeutically target the HopQ–CEACAM1 interaction and reduce the burden of pathogenic H. pylori. View Full-Text
Keywords: bacterial adhesion; CagA delivery; CEACAM1; Helicobacter pylori; HopQ; host-pathogen interactions; Dsb-like proteins bacterial adhesion; CagA delivery; CEACAM1; Helicobacter pylori; HopQ; host-pathogen interactions; Dsb-like proteins
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MDPI and ACS Style

Hamway, Y.; Taxauer, K.; Moonens, K.; Neumeyer, V.; Fischer, W.; Schmitt, V.; Singer, B.B.; Remaut, H.; Gerhard, M.; Mejías-Luque, R. Cysteine Residues in Helicobacter pylori Adhesin HopQ Are Required for CEACAM–HopQ Interaction and Subsequent CagA Translocation. Microorganisms 2020, 8, 465. https://doi.org/10.3390/microorganisms8040465

AMA Style

Hamway Y, Taxauer K, Moonens K, Neumeyer V, Fischer W, Schmitt V, Singer BB, Remaut H, Gerhard M, Mejías-Luque R. Cysteine Residues in Helicobacter pylori Adhesin HopQ Are Required for CEACAM–HopQ Interaction and Subsequent CagA Translocation. Microorganisms. 2020; 8(4):465. https://doi.org/10.3390/microorganisms8040465

Chicago/Turabian Style

Hamway, Youssef; Taxauer, Karin; Moonens, Kristof; Neumeyer, Victoria; Fischer, Wolfgang; Schmitt, Verena; Singer, Bernhard B.; Remaut, Han; Gerhard, Markus; Mejías-Luque, Raquel. 2020. "Cysteine Residues in Helicobacter pylori Adhesin HopQ Are Required for CEACAM–HopQ Interaction and Subsequent CagA Translocation" Microorganisms 8, no. 4: 465. https://doi.org/10.3390/microorganisms8040465

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