{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["15"],"submitter":["Zhao Q"],"pubmed_abstract":["The foodborne pathogenic bacterium <i>Campylobacter jejuni</i> utilizes chemotaxis to assist in the colonization of host niches. A key to revealing the relationship among chemotaxis and pathogenicity is the discovery of signaling molecules perceived by the chemoreceptors. The <i>C. jejuni</i> chemoreceptor Tlp11 is encoded by the highly infective <i>C. jejuni</i> strains. In the present study, we report that the dCache-type ligand-binding domain (LBD) of <i>C. jejuni</i> ATCC 33560 Tlp11 binds directly to novel ligands methyl pyruvate, toluene, and quinoline using the same pocket. Methyl pyruvate elicits a strong chemoattractant response, while toluene and quinoline function as the antagonists without triggering chemotaxis. The sensory LBD was used to control heterologous proteins by const"],"journal":["Frontiers in microbiology"],"pagination":["1400284"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11111895"],"repository":["biostudies-literature"],"pubmed_title":["Identification of a dCache-type chemoreceptor in <i>Campylobacter jejuni</i> that specifically mediates chemotaxis towards methyl pyruvate."],"pmcid":["PMC11111895"],"pubmed_authors":["Li W","Bi S","Zhao Q","Liu S","Yao F"],"additional_accession":[]},"is_claimable":false,"name":"Identification of a dCache-type chemoreceptor in <i>Campylobacter jejuni</i> that specifically mediates chemotaxis towards methyl pyruvate.","description":"The foodborne pathogenic bacterium <i>Campylobacter jejuni</i> utilizes chemotaxis to assist in the colonization of host niches. A key to revealing the relationship among chemotaxis and pathogenicity is the discovery of signaling molecules perceived by the chemoreceptors. The <i>C. jejuni</i> chemoreceptor Tlp11 is encoded by the highly infective <i>C. jejuni</i> strains. In the present study, we report that the dCache-type ligand-binding domain (LBD) of <i>C. jejuni</i> ATCC 33560 Tlp11 binds directly to novel ligands methyl pyruvate, toluene, and quinoline using the same pocket. Methyl pyruvate elicits a strong chemoattractant response, while toluene and quinoline function as the antagonists without triggering chemotaxis. The sensory LBD was used to control heterologous proteins by const","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024","modification":"2026-04-16T03:23:19.773Z","creation":"2026-04-16T03:13:10.02Z"},"accession":"S-EPMC11111895","cross_references":{"pubmed":["38784811"],"doi":["10.3389/fmicb.2024.1400284"]}}