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dc.contributor.authorPang, Siew Siew
dc.contributor.authorStanley, Thai Son Nguyen
dc.contributor.authorPerry, Andrew J
dc.contributor.authorDay, Christopher J
dc.contributor.authorPanjikar, Santosh
dc.contributor.authorTiralongo, Joe
dc.contributor.authorWhisstock, James C
dc.contributor.authorKwok, Terry
dc.date.accessioned2017-05-03T14:16:54Z
dc.date.available2017-05-03T14:16:54Z
dc.date.issued2014
dc.identifier.issn0021-9258
dc.identifier.doi10.1074/jbc.M113.513135
dc.identifier.urihttp://hdl.handle.net/10072/66801
dc.description.abstractThe gastric pathogen Helicobacter pylori is a major cause of acute chronic gastritis and the development of stomach and duodenal ulcers. Chronic infection furthermore predisposes to the development of gastric cancer. Crucial to H. pylori survival within the hostile environment of the digestive system are the adhesins SabA and BabA; these molecules belong to the same protein family and permit the bacteria to bind tightly to sugar moieties LewisB and sialyl-LewisX, respectively, on the surface of epithelial cells lining the stomach and duodenum. To date, no representative SabA/BabA structure has been determined, hampering the development of strategies to eliminate persistent H. pylori infections that fail to respond to conventional therapy. Here, using x-ray crystallography, we show that the soluble extracellular adhesin domain of SabA shares distant similarity to the tetratricopeptide repeat fold family. The molecule broadly resembles a golf putter in shape, with the head region featuring a large cavity surrounded by loops that vary in sequence between different H. pylori strains. The N-terminal and C-terminal helices protrude at right angles from the head domain and together form a shaft that connects to a predicted outer membrane protein-like ߭barrel trans-membrane domain. Using surface plasmon resonance, we were able to detect binding of the SabA adhesin domain to sialyl-LewisX and LewisX but not to LewisA, LewisB, or LewisY. Substitution of the highly conserved glutamine residue 159 in the predicted ligand-binding pocket abrogates the binding of the SabA adhesin domain to sialyl-LewisX and LewisX. Taken together, these data suggest that the adhesin domain of SabA is sufficient in isolation for specific ligand binding.
dc.description.peerreviewedYes
dc.description.publicationstatusYes
dc.languageEnglish
dc.language.isoeng
dc.publisherAmerican Society for Biochemistry and Molecular Biology
dc.publisher.placeUnited States
dc.relation.ispartofstudentpublicationN
dc.relation.ispartofpagefrom6332
dc.relation.ispartofpageto6340
dc.relation.ispartofissue10
dc.relation.ispartofjournalJournal of Biological Chemistry
dc.relation.ispartofvolume289
dc.rights.retentionY
dc.subject.fieldofresearchChemical sciences
dc.subject.fieldofresearchBiological sciences
dc.subject.fieldofresearchReceptors and membrane biology
dc.subject.fieldofresearchStructural biology (incl. macromolecular modelling)
dc.subject.fieldofresearchBacteriology
dc.subject.fieldofresearchBiomedical and clinical sciences
dc.subject.fieldofresearchcode34
dc.subject.fieldofresearchcode31
dc.subject.fieldofresearchcode310110
dc.subject.fieldofresearchcode310112
dc.subject.fieldofresearchcode310701
dc.subject.fieldofresearchcode32
dc.titleThe Three-dimensional Structure of the Extracellular Adhesion Domain of the Sialic Acid-binding Adhesin SabA from Helicobacter pylori
dc.typeJournal article
dc.type.descriptionC1 - Articles
dc.type.codeC - Journal Articles
gro.hasfulltextNo Full Text
gro.griffith.authorDay, Christopher J.
gro.griffith.authorTiralongo, Joe


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