ArticleScientific reports2016
Identification of a Vibrio cholerae chemoreceptor that senses taurine and amino acids as attractants.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed, 65 citations in OpenAlex.
- Chemotaxis and Related Signaling Systems inBiomolecules · 2025Review
- Bacterial sensor evolved by decreasing complexity.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- TheFrontiers in microbiology · 2025Article
- Bacterial amino acid chemotaxis: a widespread strategy with multiple physiological and ecological roles.Journal of bacteriology · 2024Review
- Deciphering Bacterial Chemorepulsion: The Complex Response of Microbes to Environmental Stimuli.Microorganisms · 2024Review
- Taurine, a Component of the Tear Film, Exacerbates the Pathogenic Mechanisms ofPathogens (Basel, Switzerland) · 2023Article
- D-amino acids signal a stress-dependent run-away response in Vibrio cholerae.Nature microbiology · 2023Article
- PAS Domain-Containing Chemoreceptors Influence the Signal Sensing and Intestinal Colonization ofGenes · 2022Article
- Signal binding at both modules of its dCache domain enables the McpA chemoreceptor ofProceedings of the National Academy of Sciences of the United States of America · 2022Article
- Amino acid sensor conserved from bacteria to humans.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- The Signaling Pathway That cGAMP Riboswitches Found: Analysis and Application of Riboswitches to Study cGAMP Signaling inInternational journal of molecular sciences · 2022Article
- Impact of Gene Repression on Biofilm Formation ofFrontiers in microbiology · 2022Article
- Phylogenetic Analysis with Prediction of Cofactor or Ligand Binding for Pseudomonas aeruginosa PAS and Cache Domains.Microbiology spectrum · 2021Article
- Vibrio cholerae Motility in Aquatic and Mucus-Mimicking Environments.Applied and environmental microbiology · 2021Article
- Molecular basis of C-S bond cleavage in the glycyl radical enzyme isethionate sulfite-lyase.Cell chemical biology · 2021Article
- A deep-sea bacterium related to coastal marine pathogens.Environmental microbiology · 2021Article
- Chemotaxis of Beneficial Rhizobacteria to Root Exudates: The First Step towards Root-Microbe Rhizosphere Interactions.International journal of molecular sciences · 2021Review
- Histamine: A Bacterial Signal Molecule.International journal of molecular sciences · 2021Review
- Article
- The chemosensory systems of Vibrio cholerae.Molecular microbiology · 2020Review
Corrections and comments
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Authors and funding
10 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Vibrio cholerae, the etiological agent of cholera, was found to be attracted by taurine (2-aminoethanesulfonic acid), a major constituent of human bile. Mlp37, the closest homolog of the previously identified amino acid chemoreceptor Mlp24, was found to mediate taxis to taurine as well as L-serine, L-alanine, L-arginine, and other amino acids. Methylation of Mlp37 was enhanced upon the addition of taurine and amino acids. Isothermal titration calorimetry demonstrated that a purified periplasmic fragment of Mlp37 binds directly to taurine, L-serine, L-alanine and L-arginine. Crystal structures of the periplamic domain of Mlp37 revealed that L-serine and taurine bind to the membrane-distal PAS domain in essentially in the same way. The structural information was supported by characterising the in vivo properties of alanine-substituted mutant forms of Mlp37. The fact that the ligand-binding domain of the L-serine complex had a small opening, which would accommodate a larger R group, accounts for the broad ligand specificity of Mlp37 and allowed us to visualise ligand binding to Mlp37 with fluorescently labelled L-serine. Taken together, we conclude that Mlp37 serves as the major chemoreceptor for taurine and various amino acids.
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