0000000001275296

AUTHOR

Wolfgang Meyerhof

showing 4 related works from this author

A binary genetic approach to characterize TRPM5 cells in mice

2015

International audience; Transient receptor potential channel subfamily M member 5 (TRPM5) is an important downstream signaling component in a subset of taste receptor cells making it a potential target for taste modulation. Interestingly, TRPM5 has been detected in extra-oral tissues; however, the function of extra-gustatory TRPM5-expressing cells is less well understood. To facilitate visualization and manipulation of TRPM5-expressing cells in mice, we generated a Cre knock-in TRPM5 allele by homologous recombination. We then used the novel TRPM5-IRES-Cre mouse strain to report TRPM5 expression by activating a tau GFP transgene. To confirm faithful coexpression of tau GFP and TRPM5 we gene…

MalePhysiologytaste papillaegene targetingBehavioral NeuroscienceMice0302 clinical medicineTaste receptor[SDV.IDA]Life Sciences [q-bio]/Food engineeringGene Knock-In TechniquesIn Situ Hybridization Fluorescence0303 health sciencestaste budsiresGene targetingrosa26ImmunohistochemistrySensory SystemsCell biologyknock inmedicine.anatomical_structuretrpm5taste receptor cellsFemaleGenotypeTransgeneCre recombinaseTRPM Cation ChannelsMice TransgenicBiologyAntibodiestgfpseptal organ of masera03 medical and health sciencesOlfactory MucosaTonguemicrovillar cellsPhysiology (medical)Gene knockinmedicineAnimals[SPI.GPROC]Engineering Sciences [physics]/Chemical and Process EngineeringTRPM5cre recombinaseAlleles030304 developmental biologyPalateMice Inbred C57BLvomeronasal organolfactory epitheliumgastrointestinal tractHomologous recombinationOlfactory epithelium030217 neurology & neurosurgery
researchProduct

Resolution of the X-ray structure of gurmarin: new insights into the molecular mechanism of sweet taste receptor inhibition

2019

International audience

[SDV.AEN] Life Sciences [q-bio]/Food and Nutrition[SDV.NEU.PC]Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC]/Psychology and behavior[SDV.IDA]Life Sciences [q-bio]/Food engineering[SDV.NEU.PC] Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC]/Psychology and behavior[SDV.NEU]Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC][SDV.NEU] Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC][SDV.IDA] Life Sciences [q-bio]/Food engineering[SDV.AEN]Life Sciences [q-bio]/Food and NutritionComputingMilieux_MISCELLANEOUS
researchProduct

The Crystal Structure of Gurmarin, a Sweet Taste–Suppressing Protein: Identification of the Amino Acid Residues Essential for Inhibition

2018

International audience; Gurmarin is a highly specific sweet-taste suppressing protein in rodents that is isolated from the Indian plant Gymnemasylvestre. Gurmarin consists of 35 amino acid residues containing three intramolecular disulfide bridges that form a cystine knot. Here, we report the crystal structure of gurmarin at a 1.45 Å resolution and compare it with previously reported NMR solution structures. The atomic structure at this resolution allowed us to identify a very flexible region consisting of hydrophobic residues. Some of these amino acid residues had been identified as a putative binding site for the rat sweet taste receptor in a previous study. By combining alanine-scanning …

0301 basic medicineProtein ConformationPhysiologyCrystal structureCrystallography X-Ray03 medical and health sciencesBehavioral NeuroscienceGPCRsweet tastetaste receptorPhysiology (medical)goût sucréAnimalsHumansG protein-coupled receptorAmino AcidsBinding siteReceptorNuclear Magnetic Resonance BiomolecularPlant ProteinsGurmarininhibiteur030102 biochemistry & molecular biologybiologyChemistryMutagenesisCystine knotGymnema sylvestreSweet tastebiology.organism_classificationRecombinant ProteinsSensory SystemsRats3. Good healthinhibitorHEK293 Cells030104 developmental biologyBiochemistryGymnema sylvestreknottin[SDV.AEN]Life Sciences [q-bio]/Food and NutritionHydrophobic and Hydrophilic InteractionsChemical Senses
researchProduct

The X-ray structure of gurmarin provide new insights into amino acid residues essential for inhibition of the rat sweet taste receptor

2018

International audience; Gurmarin is a polypeptide isolated from the Indian plant Gymnema sylvestre, which specifically suppresses sweet taste in rodents without affecting responses to other basic taste stimuli, such as HCl, NaCl, and quinine. Although the exact mechanism of gurmarin inhibition is not known, it has been shown that gurmarin acts via the T1R2/T1R3 sweet taste receptor. The gurmarin molecule is made of 35 amino-acid residues and three intramolecular disulfide bridges. We report herein the 1.45 Å X-ray structure of gurmarin heterologously produced using the yeast Pichia pastoris. The structure revealed a typical knottin fold, which is compared with previously reported NMR soluti…

[SDV.AEN] Life Sciences [q-bio]/Food and Nutritionfood and beverages[SDV.AEN]Life Sciences [q-bio]/Food and Nutrition
researchProduct