Insect-vertebrate chimeric nicotinic acetylcholine receptors identify a region, loop B to the N-terminus of the Drosophila Dα2 subunit, which contributes to neonicotinoid sensitivity

Shimomura, Masaru; Satoh, Hitoshi; Yokota, Maiko; Ihara, Makoto; Matsuda, Kazuhiko; Sattelle, David B.

doi:10.1016/j.neulet.2005.05.014

Cited by 37 publications

(24 citation statements)

References 10 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The I max and pEC 50 values of ACh for Dα2β2 nAChR were 1.08±0.03 and 4.60±0.04, respectively. The ACh values of the Dα2β2 nAChR were similar to those in previous reports [16][17][18] (Fig. 3, Table 2).…”

Section: Agonist Activity Of Achsupporting

confidence: 90%

Association between the R81T mutation in the nicotinic acetylcholine receptor β1 subunit of <i>Aphis gossypii</i> and the differential resistance to acetamiprid and imidacloprid

Hirata

Kiyota

Matsuura

et al. 2015

Journal of Pesticide Science

View full text Add to dashboard Cite

The Aphis gossypii clone, Kushima, which was first discovered in Miyazaki Prefecture, Japan, exhibits significant resistance to neonicotinoid insecticides. We investigated the resistance mechanism involved by sequencing the nicotinic acetylcholine receptor (nAChR) gene, by electrophysiological analysis, and by insecticidal tests in the presence or absence of the oxidase inhibitor, piperonyl butoxide. The Kushima clone showed higher resistance to nitro-substituted neonicotinoids, such as imidacloprid, than to cyano-substituted neonicotinoids, such as acetamiprid. Sequencing of the nAChR subunit genes of a susceptible clone and the Kushima clone revealed an R81T mutation in loop D of the β1 subunit in the resistant clone. This mutation led to a significant shift in the pEC 50 value of imidacloprid for the Drosophila melanogaster Dα2-chicken β2 subunit, while it barely affected the concentration-response curves of acetylcholine and acetamiprid.

show abstract

Section: Agonist Activity Of Achsupporting

confidence: 90%

Association between the R81T mutation in the nicotinic acetylcholine receptor β1 subunit of <i>Aphis gossypii</i> and the differential resistance to acetamiprid and imidacloprid

Hirata

Kiyota

Matsuura

et al. 2015

Journal of Pesticide Science

View full text Add to dashboard Cite

show abstract

“…The importance of nAChR subunit domains and of individual amino acids to the selective binding of neonicotinoid insecticides is also starting to be examined by techniques such as site-directed mutagenesis and construction of subunit chimeras (Matsuda et al 2000;Shimomura et al 2002Shimomura et al , 2003Shimomura et al , 2004Shimomura et al , 2005.…”

Section: Neonicotinoid Insecticidesmentioning

confidence: 99%

Nicotinic acetylcholine receptors: targets for commercially important insecticides

2007

View full text Add to dashboard Cite

Nicotinic acetylcholine receptors (nAChRs) are major excitatory neurotransmitter receptors in both vertebrates and invertebrates. In insects, nAChRs are the target site for several naturally occurring and synthetic compounds that exhibit potent insecticidal activity. Several compounds isolated from plants are potent agonists or antagonists of nAChRs, suggesting that these may have evolved as a defence mechanism against insects and other herbivores. Nicotine, isolated from the tobacco plant, has insecticidal activity and has been used extensively as a commercial insecticide. Spinosad, a naturally occurring mixture of two macrocyclic lactones isolated from the microorganism Saccharopolyspora spinosa, acts upon nAChRs and has been developed as a commercial insecticide. Since the early 1990s, one of the most widely used and rapidly growing classes of insecticides has been the neonicotinoids. Neonicotinoid insecticides are potent selective agonists of insect nAChRs and are used extensively in both crop protection and animal health applications. As with other classes of insecticides, there is growing evidence for the evolution of resistance to insecticides that act on nAChRs.

show abstract

“…Another way to examine the pharmacological properties of insect nAChRs is to construct artificial subunit chimeras, although it can't reveal all features of the wildtype receptor (Lansdell and Millar, 2004;Shimomura et al, 2005).…”

Section: Introductionmentioning

confidence: 99%

Amino acids within loops D, E and F of insect nicotinic acetylcholine receptor β subunits influence neonicotinoid selectivity

Yao

Song

Chen

et al. 2008

Insect Biochemistry and Molecular Biology

View full text Add to dashboard Cite

Insect-vertebrate chimeric nicotinic acetylcholine receptors identify a region, loop B to the N-terminus of the Drosophila Dα2 subunit, which contributes to neonicotinoid sensitivity

Cited by 37 publications

References 10 publications

Association between the R81T mutation in the nicotinic acetylcholine receptor β1 subunit of <i>Aphis gossypii</i> and the differential resistance to acetamiprid and imidacloprid

Association between the R81T mutation in the nicotinic acetylcholine receptor β1 subunit of <i>Aphis gossypii</i> and the differential resistance to acetamiprid and imidacloprid

Nicotinic acetylcholine receptors: targets for commercially important insecticides

Amino acids within loops D, E and F of insect nicotinic acetylcholine receptor β subunits influence neonicotinoid selectivity

Contact Info

Product

Resources

About