A conserved odorant binding protein is required for essential amino acid detection in Drosophila

被引:25
作者
Rihani, Karen [1 ]
Fraichard, Stephane [1 ]
Chauvel, Isabelle [1 ]
Poirier, Nicolas [1 ]
Delompre, Thomas [1 ]
Neiers, Fabrice [1 ]
Tanimura, Teiichi [2 ,3 ]
Ferveur, Jean-Francois [1 ]
Briand, Loic [1 ]
机构
[1] Univ Bourgogne Franche Comte, Ctr Sci Gout & Alimentat, INRA, AgroSup Dijon,CNRS, F-21000 Dijon, France
[2] Nagoya Univ, Grad Sch Sci, Div Biol Sci, Chikusa Ku, Furo, Aichi 4648602, Japan
[3] LIN, Dept Genet, Brenneckestr 6, D-39118 Magdeburg, Germany
基金
日本学术振兴会;
关键词
PHEROMONE-BINDING; LIGAND-BINDING; BITTER TASTE; RECEPTOR; NEURONS; FAMILY; MELANOGASTER; ORGANIZATION; PREFERENCE; REVEALS;
D O I
10.1038/s42003-019-0673-2
中图分类号
Q [生物科学];
学科分类号
07 ; 0710 ; 09 ;
摘要
Animals need to detect in the food essential amino acids that they cannot synthesize. We found that the odorant binding protein OBP19b, which is highly expressed in Drosophila melanogaster taste sensilla, is necessary for the detection of several amino acids including the essential L-phenylalanine. The recombinant OBP19b protein was produced and characterized for its binding properties: it stereoselectively binds to several amino acids. Using a feeding-choice assay, we found that OBP19b is necessary for detecting L-phenylalanine and L-glutamine, but not L-alanine or D-phenylalanine. We mapped the cells expressing OBP19b and compared the electrophysiological responses of a single taste sensillum to several amino acids: OBP19b mutant flies showed a reduced response compared to control flies when tested to preferred amino acids, but not to the other ones. OBP19b is well conserved in phylo-genetically distant species suggesting that this protein is necessary for detection of specific amino acids in insects.
引用
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页数:10
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