ArticleThe Journal of biological chemistry2023
Molecular determinants for differential activation of the bile acid receptor from the pathogen Vibrio parahaemolyticus.
Article in The Journal of biological chemistry, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 17 citations in OpenAlex.
- Bile-mediated ToxS homodimerization provides a model for ToxRS periplasmic interactions.bioRxiv : the preprint server for biology · 2026Article
- Skin androgens regulate Staphylococcus aureus pathogenicity via quorum sensing.Nature microbiology · 2026Article
- The effect of bile salts stress on the biology and transcriptome characteristics of Vibrio parahaemolyticus under low salt environment.Archives of microbiology · 2026Article
- The Diverse Roles of the Histone-Like Nucleoid Structuring (H-NS) Protein inGenetics research · 2026Review
- A critical role forProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Structural and functional diversity of sensor domains in bacterial transmembrane receptors.Trends in microbiology · 2025Review
- Article
- Proteomic Analysis Reveals the Phenotypic Heterogeneity and Tolerance Mechanisms of HalophilicBiomolecules · 2025Article
- Microbially catalyzed conjugation of GABA and tyramine to bile acids.Journal of bacteriology · 2024Article
- The effect of environmental calcium on gene expression, biofilm formation and virulence ofFrontiers in microbiology · 2024Article
- Microbially-catalyzed conjugation of GABA and tyramine to bile acids.bioRxiv : the preprint server for biology · 2023Article
- Article
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Authors and funding
6 authors at 4 institutions in 1 country.
Funding
Abstract
Bile acids are important for digestion of food and antimicrobial activity. Pathogenic Vibrio parahaemolyticus senses bile acids and induce pathogenesis. The bile acid taurodeoxycholate (TDC) was shown to activate the master regulator, VtrB, of this system, whereas other bile acids such as chenodeoxycholate (CDC) do not. Previously, VtrA-VtrC was discovered to be the co-component signal transduction system that binds bile acids and induces pathogenesis. TDC binds to the periplasmic domain of the VtrA-VtrC complex, activating a DNA-binding domain in VtrA that then activates VtrB. Here, we find that CDC and TDC compete for binding to the VtrA-VtrC periplasmic heterodimer. Our crystal structure of the VtrA-VtrC heterodimer bound to CDC revealed CDC binds in the same hydrophobic pocket as TDC but differently. Using isothermal titration calorimetry, we observed that most mutants in the binding pocket of VtrA-VtrC caused a decrease in bile acid binding affinity. Notably, two mutants in VtrC bound bile acids with a similar affinity as the WT protein but were attenuated for TDC-induced type III secretion system 2 activation. Collectively, these studies provide a molecular explanation for the selective pathogenic signaling by V. parahaemolyticus and reveal insight into a host's susceptibility to disease.
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