TY - JOUR
T1 - Odor-specific deactivation defects in a drosophila odorant-binding protein mutant
AU - Scheuermann, Elizabeth A.
AU - Smith, Dean P.
N1 - Funding Information:
We thank Kishor Kunwar for assistance with the QPCR analysis. This work was supported by National Institutes of Health grants R01 DC-015230 to D.P.S. and 5T32 GM-008203 to E.A.S. The authors declare no competing financial interests.
Publisher Copyright:
© 2019 by the Genetics Society of America.
PY - 2019
Y1 - 2019
N2 - Insect odorant-binding proteins (OBPs) are a large, diverse group of low-molecular weight proteins secreted into the fluid bathing olfactory and gustatory neuron dendrites. The best-characterized OBP, LUSH (OBP76a) enhances pheromone sensitivity enabling detection of physiological levels of the male-specific pheromone, 11-cis vaccenyl acetate. The role of the other OBPs encoded in the Drosophila genome is largely unknown. Here, using clustered regularly interspaced short palindromic repeats/Cas9, we generated and characterized the loss-of-function phenotype for two genes encoding homologous OBPs, OS-E (OBP83b) and OS-F (OBP83a). Instead of activation defects, these extracellular proteins are required for normal deactivation of odorant responses to a subset of odorants. Remarkably, odorants detected by the same odorant receptor are differentially affected by the loss of the OBPs, revealing an odorant-specific role in deactivation kinetics. In stark contrast to lush mutants, the OS-E/F mutants have normal activation kinetics to the affected odorants, even at low stimulus concentrations, suggesting that these OBPs are not competing for these ligands with the odorant receptors. We also show that OS-E and OS-F are functionally redundant as either is sufficient to revert the mutant phenotype in transgenic rescue experiments. These findings expand our understanding of the roles of OBPs to include the deactivation of odorant responses.
AB - Insect odorant-binding proteins (OBPs) are a large, diverse group of low-molecular weight proteins secreted into the fluid bathing olfactory and gustatory neuron dendrites. The best-characterized OBP, LUSH (OBP76a) enhances pheromone sensitivity enabling detection of physiological levels of the male-specific pheromone, 11-cis vaccenyl acetate. The role of the other OBPs encoded in the Drosophila genome is largely unknown. Here, using clustered regularly interspaced short palindromic repeats/Cas9, we generated and characterized the loss-of-function phenotype for two genes encoding homologous OBPs, OS-E (OBP83b) and OS-F (OBP83a). Instead of activation defects, these extracellular proteins are required for normal deactivation of odorant responses to a subset of odorants. Remarkably, odorants detected by the same odorant receptor are differentially affected by the loss of the OBPs, revealing an odorant-specific role in deactivation kinetics. In stark contrast to lush mutants, the OS-E/F mutants have normal activation kinetics to the affected odorants, even at low stimulus concentrations, suggesting that these OBPs are not competing for these ligands with the odorant receptors. We also show that OS-E and OS-F are functionally redundant as either is sufficient to revert the mutant phenotype in transgenic rescue experiments. These findings expand our understanding of the roles of OBPs to include the deactivation of odorant responses.
KW - Olfaction
KW - Olfactory
KW - Perireceptor
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U2 - 10.1534/genetics.119.302629
DO - 10.1534/genetics.119.302629
M3 - Article
C2 - 31492805
AN - SCOPUS:85074532177
SN - 0016-6731
VL - 213
SP - 897
EP - 909
JO - Genetics
JF - Genetics
IS - 3
ER -