Journal
BIOCHEMISTRY
Volume 51, Issue 23, Pages 4627-4629Publisher
AMER CHEMICAL SOC
DOI: 10.1021/bi300522s
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Funding
- U.K. Biotechnology and Biological Sciences Research Council (BBSRC)
- Bayer Animal Health
- EU
- BBSRC
- BBSRC [BBS/E/C/00005193, BB/F009143/1] Funding Source: UKRI
- EPSRC [EP/H043888/1] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BBS/E/C/00005193, BB/F009143/1] Funding Source: researchfish
- Engineering and Physical Sciences Research Council [EP/H043888/1] Funding Source: researchfish
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Neonicotinoid insecticides target nicotinic acetylcholine receptors (nAChR) in the nervous system of insects but are largely ineffective against ticks. This study aimed to identify the molecular basis for this insensitivity. A homology model of the nAChR binding domain was generated on the basis of the crystal structure of an acetylcholine-binding protein with the insecticide imidacloprid bound. We hypothesized that tick beta-subunits would differ at a critical residue (Arg81) in their D loops. To test this, we sequenced nAChR genes from five tick species and found that instead of the conserved arginine found in insects, a glutamine was present in all the tick sequences.
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