[3H]imidacloprid labels high- and low-affinity nicotinic acetylcholine receptor-like binding sites in the aphid Myzus persicae (Hemiptera: Aphididae)

• Published in: Pesticide biochemistry and physiology Vol. 62; no. 1; pp. 3 - 14
• Main Authors: Lind, R.J. (University of Bath, Bath, UK.), Clough, M.S, Reynolds, S.E, Earley, F.G.P
• Format: Journal Article
• Language: English
• Published: San Diego, CA Elsevier 01.10.1998
• Subjects: Aphididae; Biological and medical sciences; Chemical control; CHOLINERGIC RECEPTORS; Control; EXPERIMENTACION IN VITRO; EXPERIMENTATION IN VITRO; Fundamental and applied biological sciences. Psychology; Homoptera; IN VITRO EXPERIMENTATION; INSECTA; INSECTICIDAS; INSECTICIDE; INSECTICIDES; MEMBRANES; MYZUS PERSICAE; Phytopathology. Animal pests. Plant and forest protection; Protozoa. Invertebrates; Aphidoidea; Insecticide; Nitroguanidine derivatives; Radiolabelling; Ligand; Affinity labelling; Insecta; Pesticides; Guanidines; Binding site; Myzus persicae; Pest; Homoptera; Pest management; Arthropoda; Chemical control; Aphididae; Acetylcholine; Invertebrata; Nicotinic receptor
• ISSN: 0048-3575; 1095-9939
• DOI: 10.1006/pest.1998.2364

The nitroguanidine insecticide imidacloprid (IMI) is known to act as an agonist at the insect nicotinic acetylcholine receptor (nAChR). Saturable binding of [3H]IMI to membranes of the peach potato aphid Myzus persicae (R1 strain) revealed the presence of both high- and low-affinity [3H]IMI binding sites having dissociation constants and maximal binding capacities of 0.14 nM and 284 fmol/mg and 12.6 nM and 485 fmol/mg, respectively, with a Hill value of 0.61. Displacement of 500 pM [3H]IMI binding to aphid membranes by the nicotinic ligands acetylcholine, (-)-nicotine, alpha-bungarotoxin (alpha-BGTX) (+/-)-epibatidine, methyllycaconitine (MLA) and IMI gave IC50 values (nM) of 2390, 643, 62.4. 21.9, 15.1, and 1.1, respectively. The pharmacology of the aphid high-affinity [3H]IMI binding site thus resembles that of nicotinic acetylcholine receptors. Low Hill values for ACh, alpha-BGTX, and MLA displacement suggest either that high-affinity [3H]IMI binding occurs at multiple sites which have differing affinities for ACh, alpha-BGTX, or MLA or that binding to one high-affinity site is allosterically influenced by binding to another site on the same putative nAChR. Saturable [3H]IMI binding was analyzed in a panel of insects, namely, Nephotettix cincticeps (Hemiptera: Cicadellidae), Periplaneta americana (Dictyoptera: Blattidae), Lucilia sericata (Diptera: Calliphoridae), Drosophila melanogaster (Canton S) (Diptera: Drosophiloidea), Manduca sexta (Lepidoptera: Sphingidae), Heliothis virescens (Lepidoptera: Noctuidae), and Ctenocephalides felis (Siphonaptera: Pulicidae). The results demonstrate that of these, only aphids and green leaf hoppers (both Hemiptera) have very high-affinity binding sites for [3H]IMI in addition to the lower affinity sites that are also seen in insects from other orders, which in these insects have Kd values of about 1 nM and Hill values of approximately 1. The presence of very high-affinity [3H]IMI binding sites only in the hemipteran insects st...