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Helicobacter pylori exploits human CEACAMs via HopQ for adherence and translocation of CagA

Helicobacter pylori exploits human CEACAMs via HopQ for adherence and translocation of CagA

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KÖNIGER, Verena, Alexandra ROTH, Arnaud KENGMO TCHOUPA, Stella I. SMITH, Susanna MUELLER, Eric J. SUNDBERG, Wolfgang ZIMMERMANN, Wolfgang FISCHER, Christof R. HAUCK, Rainer HAAS, 2016. Helicobacter pylori exploits human CEACAMs via HopQ for adherence and translocation of CagA. In: Nature Microbiology. 2, 16188. eISSN 2058-5276. Available under: doi: 10.1038/nmicrobiol.2016.188

@article{Koniger2016Helic-38837, title={Helicobacter pylori exploits human CEACAMs via HopQ for adherence and translocation of CagA}, year={2016}, doi={10.1038/nmicrobiol.2016.188}, volume={2}, journal={Nature Microbiology}, author={Königer, Verena and Roth, Alexandra and Kengmo Tchoupa, Arnaud and Smith, Stella I. and Mueller, Susanna and Sundberg, Eric J. and Zimmermann, Wolfgang and Fischer, Wolfgang and Hauck, Christof R. and Haas, Rainer}, note={Article Number: 16188} }

<rdf:RDF xmlns:dcterms="http://purl.org/dc/terms/" xmlns:dc="http://purl.org/dc/elements/1.1/" xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#" xmlns:bibo="http://purl.org/ontology/bibo/" xmlns:dspace="http://digital-repositories.org/ontologies/dspace/0.1.0#" xmlns:foaf="http://xmlns.com/foaf/0.1/" xmlns:void="http://rdfs.org/ns/void#" xmlns:xsd="http://www.w3.org/2001/XMLSchema#" > <rdf:Description rdf:about="https://kops.uni-konstanz.de/rdf/resource/123456789/38837"> <dc:contributor>Haas, Rainer</dc:contributor> <dcterms:isPartOf rdf:resource="https://kops.uni-konstanz.de/rdf/resource/123456789/28"/> <dc:language>eng</dc:language> <dc:creator>Kengmo Tchoupa, Arnaud</dc:creator> <dc:creator>Smith, Stella I.</dc:creator> <dc:creator>Mueller, Susanna</dc:creator> <dc:contributor>Fischer, Wolfgang</dc:contributor> <dc:creator>Zimmermann, Wolfgang</dc:creator> <bibo:uri rdf:resource="https://kops.uni-konstanz.de/handle/123456789/38837"/> <dc:creator>Hauck, Christof R.</dc:creator> <dc:creator>Haas, Rainer</dc:creator> <dc:creator>Fischer, Wolfgang</dc:creator> <dc:contributor>Roth, Alexandra</dc:contributor> <dc:contributor>Kengmo Tchoupa, Arnaud</dc:contributor> <dc:creator>Königer, Verena</dc:creator> <void:sparqlEndpoint rdf:resource="http://localhost/fuseki/dspace/sparql"/> <dc:contributor>Smith, Stella I.</dc:contributor> <dcterms:issued>2016</dcterms:issued> <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2017-05-11T08:12:43Z</dcterms:available> <dc:contributor>Königer, Verena</dc:contributor> <dc:contributor>Zimmermann, Wolfgang</dc:contributor> <dc:creator>Roth, Alexandra</dc:creator> <dc:creator>Sundberg, Eric J.</dc:creator> <dspace:isPartOfCollection rdf:resource="https://kops.uni-konstanz.de/rdf/resource/123456789/28"/> <dcterms:title>Helicobacter pylori exploits human CEACAMs via HopQ for adherence and translocation of CagA</dcterms:title> <dc:contributor>Hauck, Christof R.</dc:contributor> <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2017-05-11T08:12:43Z</dc:date> <dc:contributor>Sundberg, Eric J.</dc:contributor> <dc:contributor>Mueller, Susanna</dc:contributor> <dcterms:abstract xml:lang="eng">Helicobacter pylori (Hp) strains that carry the cag type IV secretion system (cag-T4SS) to inject the cytotoxin-associated antigen A (CagA) into host cells are associated with peptic ulcer disease and gastric adenocarcinoma. CagA translocation by Hp is mediated by β1 integrin interaction of the cag-T4SS. However, other cellular receptors or bacterial outer membrane adhesins essential for this process are unknown. Here, we identify the HopQ protein as a genuine Hp adhesin, exploiting defined members of the carcinoembryonic antigen-related cell adhesion molecule family (CEACAMs) as host cell receptors. HopQ binds the amino-terminal IgV-like domain of human CEACAM1, CEACAM3, CEACAM5 or CEACAM6 proteins, thereby enabling translocation of the major pathogenicity factor CagA into host cells. The HopQ-CEACAM interaction is characterized by a remarkably high affinity (KD from 23 to 268 nM), which is independent of CEACAM glycosylation, identifying CEACAMs as bona fide protein receptors for Hp. Our data suggest that the HopQ-CEACAM interaction contributes to gastric colonization or Hp-induced pathologies, although the precise role and functional consequences of this interaction in vivo remain to be determined.</dcterms:abstract> <foaf:homepage rdf:resource="http://localhost:8080/jspui"/> </rdf:Description> </rdf:RDF>

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