ArticleProceedings. Biological sciences2019
A natural point mutation in the bitter taste receptor TAS2R16 causes inverse agonism of arbutin in lemur gustation.
Article in Proceedings. Biological sciences, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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9 citing papers in PubMed, 15 citations in OpenAlex.
- Hyper-specialized primates possess a reduced suite of xenobiotic-metabolizing cytochrome P450 genes.Molecular phylogenetics and evolution · 2026Article
- The Remarkable Diversity of Vertebrate Bitter Taste Receptors: Recent Advances in Genomic and Functional Studies.International journal of molecular sciences · 2024Review
- Functional Diversity and Evolution of Bitter Taste Receptors in Egg-Laying Mammals.Molecular biology and evolution · 2022Article
- Pharmacology of T2R Mediated Host-Microbe Interactions.Handbook of experimental pharmacology · 2022Article
- A New World Monkey Resembles Human in Bitter Taste Receptor Evolution and Function via a Single Parallel Amino Acid Substitution.Molecular biology and evolution · 2021Article
- Lowered sensitivity of bitter taste receptors to β-glucosides in bamboo lemurs: an instance of parallel and adaptive functional decline in TAS2R16?Proceedings. Biological sciences · 2021Article
- Detection of Bitter Taste Molecules Based on Odorant-Binding Protein-Modified Screen-Printed Electrodes.ACS omega · 2020Article
- Structure-Function Analyses of Human Bitter Taste Receptors-Where Do We Stand?Molecules (Basel, Switzerland) · 2020Review
- A natural point mutation in the bitter taste receptor TAS2R16 causes inverse agonism of arbutin in lemur gustation.Proceedings. Biological sciences · 2019Article
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4 authors at 4 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Bitter taste enables the detection of potentially harmful substances and is mediated by bitter taste receptors, TAS2Rs, in vertebrates. Few antagonists and inverse agonists of TAS2Rs have been identified, especially natural compounds. TAS2R16s in humans, apes and Old World monkeys (Catarrhini, Anthropoidea) recognize β-glucoside analogues as specific agonists. Here, we investigated responses of TAS2R16 to β-glucosides in non-anthropoid primates, namely lemurs (Lemuriformes, Strepsirrhini). Salicin acted as an agonist on lemur TAS2R16. Arbutin acted as an agonist in the ring-tailed lemur ( Lemur catta) but as an inverse agonist in black lemur ( Eulemur macaco) and black-and-white ruffed lemur ( Varecia variegata). We identified a strepsirrhine-specific amino acid substitution responsible for the inverse agonism of arbutin. In a food preference test, salicin bitterness was inhibited by arbutin in the black lemur. Structural modelling revealed this locus was important for a rearrangement of the intracellular end of transmembrane helix 7 (TM7). Accordingly, arbutin is the first known natural inverse agonist of TAS2Rs, contributing to our understanding of receptor-ligand interactions and the molecular basis of the unique feeding habit diversification in lemurs. Furthermore, the identification of a causal point mutation suggests that TAS2R can acquire functional changes according to feeding habits and environmental conditions.
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