Comparative analysis of neonicotinoid binding to insect membranes: II. An unusual high affinity site for [3H]thiamethoxam in Myzus persicae and Aphis craccivora

✍ Scribed by Henning Wellmann; Marilyne Gomes; Connie Lee; Dr Hartmut Kayser

• Publisher: John Wiley and Sons
• Year: 2004
• Tongue: English
• Weight: 215 KB
• Volume: 60
• Category: Article
• ISSN: 1526-498X
• DOI: 10.1002/ps.920

✦ Synopsis

Abstract

Neonicotinoids represent a class of insect‐selective ligands of nicotinic acetylcholine receptors. Imidacloprid, the first commercially used neonicotinoid insecticide, has been studied on neuronal preparations from many insects to date. Here we report first intrinsic binding data of thiamethoxam, using membranes from Myzus persicae Sulzer and Aphis craccivora Koch. In both aphids, specific binding of [^3^H]thiamethoxam was sensitive to temperature, while the absolute level of non‐specific binding was not affected. In M persicae, binding capacity (B~max~) for [^3^H]thiamethoxam was ca 450 fmol mg^−1^ of protein at 22 °C and ca 700 fmol mg^−1^ of protein at 2 °C. The negative effect of increased temperature was reversible and hence not due to some destructive process. The affinity for [^3^H]thiamethoxam was less affected by temperature: K~d~ was ca 11 nM at 2 °C and ca 15 nM at 22 °C. The membranes also lost binding sites for [^3^H]thiamethoxam during prolonged storage at room temperature, and upon freezing and thawing. In A craccivora, [^3^H]thiamethoxam was bound with a capacity of ca 1000 fmol mg^−1^ protein and an affinity of ca 90 nM, as measured at 2 °C. Overall, the in vitro temperature sensitivity of [^3^H]thiamethoxam binding was in obvious contrast to the behaviour of [^3^H]imidacloprid studied in parallel. Moreover, the binding of [^3^H]thiamethoxam was inhibited by imidacloprid in a non‐competitive mode, as shown with M persicae. In our view, these differences demonstrate that thiamethoxam and imidacloprid, which represent different structural sub‐classes of neonicotinoids, do not share the same binding site or mode. This holds also for other neonicotinoids, as we report in a companion article. Copyright © 2004 Society of Chemical Industry