The human bitter taste receptor, hTAS2R16, discriminates slight differences in the configuration of disaccharides

• Published in: Biochemical and biophysical research communications Vol. 402; no. 4; pp. 595 - 601
• Main Authors: Sakurai, Takanobu, Misaka, Takumi, Ueno, Yohei, Ishiguro, Masaji, Matsuo, Shinji, Ishimaru, Yoshiro, Asakura, Tomiko, Abe, Keiko
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 26.11.2010
• Subjects: Benzyl Alcohols - chemistry; Binding site; Binding Sites; Bitter; Calcium imaging; Cell Line; Disaccharides - chemistry; Disaccharides - metabolism; Gentiobiose; Glucosides - chemistry; Humans; Molecular Conformation; Mutation; Receptors, G-Protein-Coupled - genetics; Receptors, G-Protein-Coupled - metabolism; Sweet; Taste; Taste - physiology; Calcium imaging; Bitter; Sweet; Taste; Binding site; Gentiobiose
• ISSN: 0006-291X; 1090-2104
• DOI: 10.1016/j.bbrc.2010.10.059

► The bitterness of gentiobiose is mediated by activation of hTAS2R16. ► Only slight differences in sugar configuration can lead to the activation of different taste receptors, and therefore elicit quite different tastes. ► Mutational analysis of hTAS2R16 also indicated that gentiobiose and β-d-glucopyranosides, such as salicin share a common binding site of hTAS2R16. Sweetness and bitterness are key determinants of food acceptance and rejection, respectively. Sugars, such as sucrose and fructose, are generally recognized as sweet. However, not all sugars are sweet, and even anomers may have quite different tastes. For example, gentiobiose is bitter, whereas its anomer, isomaltose, is sweet. Despite this unique sensory character, the molecular basis of the bitterness of gentiobiose remains to be clarified. In this study, we used calcium imaging analysis of human embryonic kidney 293T cells that heterologously expressed human taste receptors to demonstrate that gentiobiose activated hTAS2R16, a bitter taste receptor, but not hT1R2/hT1R3, a sweet taste receptor. In contrast, isomaltose activated hT1R2/hT1R3. As a result, these anomers elicit different taste sensations. Mutational analysis of hTAS2R16 also indicated that gentiobiose and β-d-glucopyranosides, such as salicin share a common binding site of hTAS2R16.