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dc.contributor.authorHartley-Tassell, Laurenen_US
dc.contributor.authorShewell, Lucyen_US
dc.contributor.authorDay, Christopheren_US
dc.contributor.authorWilson, Jennyen_US
dc.contributor.authorSandhu, Randeepen_US
dc.contributor.authorM. Ketley, Julianen_US
dc.contributor.authorKorolik, Victoriaen_US
dc.date.accessioned2017-04-24T08:37:27Z
dc.date.available2017-04-24T08:37:27Z
dc.date.issued2010en_US
dc.date.modified2012-02-10T02:38:17Z
dc.identifier.issn0950382Xen_US
dc.identifier.doi10.1111/j.1365-2958.2009.07010.xen_US
dc.identifier.urihttp://hdl.handle.net/10072/33172
dc.description.abstractCampylobacter jejuni is a highly motile bacterium that responds via chemotaxis to environmental stimuli to migrate towards favourable conditions. Previous in silico analysis of the C. jejuni strain NCTC11168 genome sequence identified 10 open reading frames, tlp1-10, that encode putative chemosensory receptors. We describe the characterization of the role and specificity of the Tlp1 chemoreceptor (Cj1506c). In vitro and in vivo models were used to determine if Tlp1 had a role in host colonization. The tlp1 - isogenic mutant was more adherent in cell culture, however, showed reduced colonization ability in chickens. Specific interactions between the purified sensory domain of Tlp1 and L-aspartate were identified using an amino acid array and saturation transfer difference nuclear magnetic resonance spectroscopy. Chemotaxis assays showed differences between migration of wild-type C. jejuni cells and that of a tlp1 - isogenic mutant, specifically towards aspartate. Furthermore, using yeast twohybrid and three-hybrid systems for analysis of protein-protein interactions, the cytoplasmic signalling domain of Tlp1 was found to preferentially interact with CheV, rather than the CheW homologue of the chemotaxis signalling pathway; this interaction was confirmed using immune precipitation assays. This is the first identification of an aspartate receptor in bacteria other than Escherichia coli and Salmonella enterica serovar Typhimurium.en_US
dc.description.peerreviewedYesen_US
dc.description.publicationstatusYesen_US
dc.languageEnglishen_US
dc.language.isoen_US
dc.publisherWiley-Blackwell Publishingen_US
dc.publisher.placeUnited Kingdomen_US
dc.relation.ispartofstudentpublicationYen_US
dc.relation.ispartofpagefrom710en_US
dc.relation.ispartofpageto730en_US
dc.relation.ispartofissue3en_US
dc.relation.ispartofjournalMolecular Microbiologyen_US
dc.relation.ispartofvolume75en_US
dc.rights.retentionNen_US
dc.subject.fieldofresearchBacteriologyen_US
dc.subject.fieldofresearchcode060501en_US
dc.titleIdentification and characterization of the aspartate chemosensory receptor of Campylobacter jejunien_US
dc.typeJournal articleen_US
dc.type.descriptionC1 - Peer Reviewed (HERDC)en_US
dc.type.codeC - Journal Articlesen_US
gro.facultyOffice of the Snr Dep Vice Chancellor, Institute for Glycomicsen_US
gro.date.issued2010
gro.hasfulltextNo Full Text


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