<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><volume>15</volume><submitter>Zhao Q</submitter><pubmed_abstract>The foodborne pathogenic bacterium &lt;i>Campylobacter jejuni&lt;/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 &lt;i>C. jejuni&lt;/i> chemoreceptor Tlp11 is encoded by the highly infective &lt;i>C. jejuni&lt;/i> strains. In the present study, we report that the dCache-type ligand-binding domain (LBD) of &lt;i>C. jejuni&lt;/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</pubmed_abstract><journal>Frontiers in microbiology</journal><pagination>1400284</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC11111895</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>Identification of a dCache-type chemoreceptor in &lt;i>Campylobacter jejuni&lt;/i> that specifically mediates chemotaxis towards methyl pyruvate.</pubmed_title><pmcid>PMC11111895</pmcid><pubmed_authors>Li W</pubmed_authors><pubmed_authors>Bi S</pubmed_authors><pubmed_authors>Zhao Q</pubmed_authors><pubmed_authors>Liu S</pubmed_authors><pubmed_authors>Yao F</pubmed_authors></additional><is_claimable>false</is_claimable><name>Identification of a dCache-type chemoreceptor in &lt;i>Campylobacter jejuni&lt;/i> that specifically mediates chemotaxis towards methyl pyruvate.</name><description>The foodborne pathogenic bacterium &lt;i>Campylobacter jejuni&lt;/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 &lt;i>C. jejuni&lt;/i> chemoreceptor Tlp11 is encoded by the highly infective &lt;i>C. jejuni&lt;/i> strains. In the present study, we report that the dCache-type ligand-binding domain (LBD) of &lt;i>C. jejuni&lt;/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</description><dates><release>2024-01-01T00:00:00Z</release><publication>2024</publication><modification>2026-04-16T03:23:19.773Z</modification><creation>2026-04-16T03:13:10.02Z</creation></dates><accession>S-EPMC11111895</accession><cross_references><pubmed>38784811</pubmed><doi>10.3389/fmicb.2024.1400284</doi></cross_references></HashMap>