Insect-vertebrate chimeric nicotinic acetylcholine receptors identify a region, loop B to the N-terminus of the Drosophila Dalpha2 subunit, which contributes to neonicotinoid sensitivity
| Autor: | Kazuhiko Matsuda, Makoto Ihara, Maiko Yokota, David B. Sattelle, Masaru Shimomura, Hitoshi Satoh |
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| Rok vydání: | 2005 |
| Předmět: |
Protein subunit
Recombinant Fusion Proteins Amino Acid Motifs Xenopus Cholinergic Agents Drug Resistance Receptors Nicotinic Interleukin 10 receptor alpha subunit chemistry.chemical_compound Neonicotinoids Xenopus laevis Imidacloprid parasitic diseases Animals Amino Acid Sequence Acetylcholine receptor Genetics biology General Neuroscience Neonicotinoid Imidazoles biology.organism_classification Nitro Compounds Cell biology Protein Structure Tertiary Nicotinic acetylcholine receptor Protein Subunits Nicotinic agonist Drosophila melanogaster chemistry Amino Acid Substitution Oocytes sense organs Chickens |
| Zdroj: | Neuroscience letters. 385(2) |
| ISSN: | 0304-3940 |
| Popis: | A chimera based on the chicken alpha4 nicotinic acetylcholine receptor (nAChR) subunit containing an insert from loop B to the N-terminus of the Drosophila melanogaster Dalpha2 (=SAD) subunit was constructed and co-expressed with the chicken beta2 nAChR subunit in Xenopus laevis oocytes. The actions of the neonicotinoid insecticide imidacloprid were examined. Replacement of the region loop B to the N-terminus of the alpha4 subunit by the corresponding region of the Dalpha2 subunit had little effect on the concentration-response curve for imidacloprid. However, replacement of Glu219 by proline in the YXCC motif in loop C of the chimeric alpha4 subunit resulted in a marked displacement to the left of the concentration-response curve for imidacloprid not seen when an equivalent mutation was made in the alpha4beta2 nAChR. The results suggest that the region loop B to the N-terminus in the Dalpha2 subunit contributes to the high imidacloprid sensitivity of the hybrid Dalpha2beta2 nAChR. |
| Databáze: | OpenAIRE |
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