A Novel Role for Odorant Binding Proteins in Deactivation of Drosophila Olfactory Neurons
| dc.contributor.advisor | Meeks, Julian P. | en |
| dc.contributor.committeeMember | Smith, Dean P. | en |
| dc.contributor.committeeMember | Krämer, Helmut | en |
| dc.contributor.committeeMember | Terman, Jonathan R. | en |
| dc.creator | Scheuermann, Elizabeth Anne | en |
| dc.creator.orcid | 0000-0002-7498-7130 | |
| dc.date.accessioned | 2021-09-17T17:59:48Z | |
| dc.date.available | 2021-09-17T17:59:48Z | |
| dc.date.created | 2019-08 | |
| dc.date.issued | 2019-07-29 | |
| dc.date.submitted | August 2019 | |
| dc.date.updated | 2021-09-17T17:59:48Z | |
| dc.description.abstract | In insects, odorant binding proteins are a large and diverse group of low molecular weight proteins secreted into the fluid bathing olfactory and gustatory dendrites. The best-characterized OBP, known as LUSH, is required in Drosophila melanogaster for the detection of physiological levels of the male-specific pheromone cVA. While LUSH acts as a sensitizing factor for pheromone detection, the role of other OBPs encoded in the Drosophila genome is largely unknown. In an effort to characterize members of this family, I used CRISPR-Cas9 to generate and characterize a deletion of two genes encoding the homologous OBPs OS-E and OS-F. These OBPs are nearly 70% identical and their expression is restricted to a small set of antennal chemosensory sensilla. Electrophysiological analysis of the olfactory neurons within these sensilla revealed no major difference in odorant sensitivity or specificity in the mutants but did reveal a striking deactivation defect to a subset of odorants. Surprisingly, other odorants detected by the same receptor are differentially affected by the absence of OS-E and OS-F, revealing an odorant-specific role for these OBPs in deactivation kinetics. Activation kinetics remain normal for the affected odorants in mutants. Genomic rescue experiments revealed that OS-E and OS-F are also functionally redundant, as either OBP is sufficient to revert the mutant phenotype. My findings reveal a new role for OBPs in deactivation of olfactory neurons and expand our understanding of the range of OBP functions. | en |
| dc.format.mimetype | application/pdf | en |
| dc.identifier.oclc | 1268338265 | |
| dc.identifier.uri | https://hdl.handle.net/2152.5/9626 | |
| dc.language.iso | en | en |
| dc.subject | Carrier Proteins | en |
| dc.subject | Drosophila Proteins | en |
| dc.subject | Loss of Function Mutation | en |
| dc.subject | Phenotype | en |
| dc.title | A Novel Role for Odorant Binding Proteins in Deactivation of Drosophila Olfactory Neurons | en |
| dc.type | Thesis | en |
| dc.type.material | text | en |
| thesis.degree.department | Graduate School of Biomedical Sciences | en |
| thesis.degree.discipline | Neuroscience | en |
| thesis.degree.grantor | UT Southwestern Medical Center | en |
| thesis.degree.level | Doctoral | en |
| thesis.degree.name | Doctor of Philosophy | en |