Sl. Chao et al., WHITEFLY (HEMIPTERA, ALEYRODIDAE) BINDING-SITE FOR IMIDACLOPRID AND RELATED INSECTICIDES - A PUTATIVE NICOTINIC ACETYLCHOLINE-RECEPTOR, Journal of economic entomology, 90(4), 1997, pp. 879-882
Imidacloprid is used extensively to control sweetpotato whiteflies, Be
misia argentifolii Bellows & Perring [also known as B. tabaci (Gennadi
us) biotype B]. As a radlioligand, [H-3]imidacloprid binds rapidly to
a single class of high-affinity sites in membrane preparations from wh
ole adult whiteflies with an apparent dissociation constant of 2 nM an
d maximal binding capacity of 101 fmol/mg protein. Three related compo
unds (the nitromethylene analog of imidacloprid, acetamiprid, and nite
npyram) inhibit [H-3]imidacloprid binding by 50% at 0.40, 2.9, and 57
nM, respectively. The pharmacological profile of the binding site (exa
mined with imidacloprid and the analogs listed above, and nicotine, al
pha-bungarotoxin, carbachol, acetylcholine [with. paraoxon], and atrop
ine) is consistent with that anticipated for a nicotinic acetylcholine
receptor and correlates well with binding results for house fly. Musc
a domestica L., head membranes under the same conditions. Thus, [H-3]i
midacloprid is a suitable radioligand to investigate the putative nico
tinic acetylcholine receptor of Bemisia and the possible modifications
of this target site associated with selection of resistant strains.