Search: onr:"swepub:oai:DiVA.org:umu-133381" >
Helicobacter pylori...
Helicobacter pylori adhesin HopQ engages in a virulence-enhancing interaction with human CEACAMs
-
Javaheri, Anahita (author)
-
Kruse, Tobias (author)
-
Moonens, Kristof (author)
-
show more...
-
Mejias-Luque, Raquel (author)
-
Debraekeleer, Ayla (author)
-
Asche, Carmen I. (author)
-
Tegtmeyer, Nicole (author)
-
Kalali, Behnam (author)
-
Bach, Nina C. (author)
-
Sieber, Stephan A. (author)
-
Hill, Darryl J. (author)
-
Koeniger, Verena (author)
-
Hauck, Christof R. (author)
-
Moskalenko, Roman (author)
-
Haas, Rainer (author)
-
Busch, Dirk H. (author)
-
Klaile, Esther (author)
-
Slevogt, Hortense (author)
-
- Schmidt, Alexej (author)
- Umeå universitet,Patologi,Medical Faculty, Institute of Anatomy, University Duisburg-Essen, 45122 Essen, Germany
-
Backert, Steffen (author)
-
Remaut, Han (author)
-
Singer, Bernhard B. (author)
-
Gerhard, Markus (author)
-
show less...
-
(creator_code:org_t)
- 2016-10-17
- 2017
- English.
-
In: Nature Microbiology. - : NATURE PUBLISHING GROUP. - 2058-5276. ; 2:1
- Related links:
-
https://research-inf...
-
show more...
-
https://urn.kb.se/re...
-
https://doi.org/10.1...
-
show less...
Abstract
Subject headings
Close
- Helicobacter pylori specifically colonizes the human gastric epithelium and is the major causative agent for ulcer disease and gastric cancer development. Here, we identify 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 signalling, 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 beta-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 suggest the HopQ-CEACAM1 interaction to be a potentially promising novel therapeutic target to combat H. pylori-associated diseases.
Subject headings
- MEDICIN OCH HÄLSOVETENSKAP -- Medicinska och farmaceutiska grundvetenskaper -- Immunologi inom det medicinska området (hsv//swe)
- MEDICAL AND HEALTH SCIENCES -- Basic Medicine -- Immunology in the medical area (hsv//eng)
- MEDICIN OCH HÄLSOVETENSKAP -- Medicinska och farmaceutiska grundvetenskaper -- Mikrobiologi inom det medicinska området (hsv//swe)
- MEDICAL AND HEALTH SCIENCES -- Basic Medicine -- Microbiology in the medical area (hsv//eng)
Publication and Content Type
- ref (subject category)
- art (subject category)
Find in a library
To the university's database
- By the author/editor
-
Javaheri, Anahit ...
-
Kruse, Tobias
-
Moonens, Kristof
-
Mejias-Luque, Ra ...
-
Debraekeleer, Ay ...
-
Asche, Carmen I.
-
show more...
-
Tegtmeyer, Nicol ...
-
Kalali, Behnam
-
Bach, Nina C.
-
Sieber, Stephan ...
-
Hill, Darryl J.
-
Koeniger, Verena
-
Hauck, Christof ...
-
Moskalenko, Roma ...
-
Haas, Rainer
-
Busch, Dirk H.
-
Klaile, Esther
-
Slevogt, Hortens ...
-
Schmidt, Alexej
-
Backert, Steffen
-
Remaut, Han
-
Singer, Bernhard ...
-
Gerhard, Markus
-
show less...
- About the subject
-
- MEDICAL AND HEALTH SCIENCES
-
MEDICAL AND HEAL ...
-
and Basic Medicine
-
and Immunology in th ...
-
- MEDICAL AND HEALTH SCIENCES
-
MEDICAL AND HEAL ...
-
and Basic Medicine
-
and Microbiology in ...
- Articles in the publication
-
Nature Microbiol ...
- By the university
-
Umeå University