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dc.contributor.authorElgamoudi, Bassam A
dc.contributor.authorAndrianova, Ekaterina P
dc.contributor.authorShewell, Lucy K
dc.contributor.authorDay, Christopher J
dc.contributor.authorKing, Rebecca M
dc.contributor.authorTaha
dc.contributor.authorRahman, Hossinur
dc.contributor.authorHartley-Tassell, Lauren E
dc.contributor.authorZhulin, Igor B
dc.contributor.authorKorolik, Victoria
dc.date.accessioned2021-01-13T05:34:30Z
dc.date.available2021-01-13T05:34:30Z
dc.date.issued2021
dc.identifier.issn1945-0877
dc.identifier.doi10.1126/scisignal.abc8521
dc.identifier.urihttp://hdl.handle.net/10072/401004
dc.description.abstractCampylobacter jejuni is a bacterial pathogen that is a common cause of enteritis in humans. We identified a previously uncharacterized type of sensory domain in the periplasmic region of the C. jejuni chemoreceptor Tlp10, termed the DAHL domain, that is predicted to have a bimodular helical architecture. Through two independent ligand-binding sites in this domain, Tlp10 responded to molecular aspartate, isoleucine, fumarate, malate, fucose, and mannose as attractants and to arginine, galactose, and thiamine as repellents. Tlp10 also recognized glycan ligands when present as terminal and intermediate residues of complex structures, such as the fucosylated human ganglioside GM1 and Lewisa antigen. A tlp10 mutant strain lacking the ligand-binding sites was attenuated in its ability to colonize avian caeca and to adhere to cultured human intestinal cells, indicating the potential involvement of the DAHL domain in host colonization and disease. The Tlp10 intracellular signaling domain interacted with the scaffolding proteins CheV and CheW, which couple chemoreceptors to intracellular signaling machinery, and with the signaling domains of other chemoreceptors, suggesting a key role for Tlp10 in signal transduction and incorporation into sensory arrays. We identified the DAHL domain in other bacterial signal transduction proteins, including the essential virulence induction protein VirA from the plant pathogen Agrobacterium tumefaciens. Together, these results suggest a potential link between Tlp10 and C. jejuni virulence.
dc.description.peerreviewedYes
dc.languageen
dc.publisherAmerican Association for the Advancement of Science (AAAS)
dc.relation.ispartofpagefromeabc8521
dc.relation.ispartofissue664
dc.relation.ispartofjournalScience Signaling
dc.relation.ispartofvolume14
dc.subject.fieldofresearchBiochemistry and Cell Biology
dc.subject.fieldofresearchcode0601
dc.titleThe Campylobacter jejuni chemoreceptor Tlp10 has a bimodal ligand-binding domain and specificity for multiple classes of chemoeffectors
dc.typeJournal article
dc.type.descriptionC1 - Articles
dcterms.bibliographicCitationElgamoudi, BA; Andrianova, EP; Shewell, LK; Day, CJ; King, RM; Taha, ; Rahman, H; Hartley-Tassell, LE; Zhulin, IB; Korolik, V, The Campylobacter jejuni chemoreceptor Tlp10 has a bimodal ligand-binding domain and specificity for multiple classes of chemoeffectors, Science Signaling, 2021, 14 (664), pp. eabc8521
dc.date.updated2021-01-13T05:13:01Z
gro.hasfulltextNo Full Text
gro.griffith.authorTaha, .
gro.griffith.authorElgamoudi, Bassam A.
gro.griffith.authorDay, Christopher J.
gro.griffith.authorShewell, Lucy K.
gro.griffith.authorKorolik, Victoria
gro.griffith.authorKing, Bec M.
gro.griffith.authorRahman, Hossinur
gro.griffith.authorHartley-Tassell, Lauren E.


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