A nicotinic acetylcholine receptor mutation (Y151S) causes reduced agonist potency to a range of neonicotinoid insecticides

A - Papers appearing in refereed journals

Liu, Z., Williamson, M. S., Lansdell, S. J., Han, Z., Denholm, I. and Millar, N. S. 2006. A nicotinic acetylcholine receptor mutation (Y151S) causes reduced agonist potency to a range of neonicotinoid insecticides. Journal of Neurochemistry. 99 (4), pp. 1273-1281.

AuthorsLiu, Z., Williamson, M. S., Lansdell, S. J., Han, Z., Denholm, I. and Millar, N. S.
Abstract

Neonicotinoid insecticides are potent selective agonists of insect nicotinic acetylcholine receptors (nAChRs). Since their introduction in 1991, resistance to neonicotinoids has been slow to develop, but it is now established in some insect field populations such as the planthopper, Nilaparvata lugens, a major rice pest in many parts of Asia. We have reported recently the identification of a target-site mutation (Y151S) within two nAChR subunits (Nl alpha 1 and Nl alpha 3) from a laboratory-selected field population of N. lugens. In the present study, we have examined the influence of this mutation upon the functional properties of recombinant nAChRs expressed in Xenopus oocytes (as hybrid nAChRs, co-expressed with a rat beta 2 subunit). The agonist potency of several nicotinic agonists has been examined, including all of the neonicotinoid insecticides that are currently licensed for either crop protection or animal health applications (acetamiprid, clothianidin, dinotefuran, imidacloprid, nitenpyram, thiacloprid and thiamethoxam). The Y151S mutation was found to have no significant effect on the maximal current (I(max)) observed with the endogenous agonist, acetylcholine. In contrast, a significant reduction in I(max) was observed for all neonicotinoids (the I(max) for mutant nAChRs ranged from 13 to 81% of that observed on wild-type receptors). In addition, nAChRs containing the Y151S mutation caused a significant rightward shift in agonist dose-response curves for all neonicotinoids, but of varying magnitude (shifts in EC(50) values ranged from 1.3 to 3.6-fold). The relationship between neonicotinoid structure and their potency on nAChRs containing the Y151S target-site mutation is discussed.

KeywordsBiochemistry & Molecular Biology; Neurosciences
Year of Publication2006
JournalJournal of Neurochemistry
Journal citation99 (4), pp. 1273-1281
Digital Object Identifier (DOI)doi:10.1111/j.1471-4159.2006.04167.x
PubMed ID16981889
Open accessPublished as non-open access
Funder project or codePDM
ISSN00223042
PublisherWiley

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