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Updated: Jan 11, 2026
Functional Characterization of Carboxylesterases in Insecticide Resistant House Flies, Musca Domestica
Published on: August 23, 2018
Identification and Structural Analysis of Apolipoprotein D with High Insecticide-Binding Affinity in Spodoptera
Kuitun Liu1, Hailiang Guo1, Wenlin Jiang1
1State Key Laboratory of Agricultural and Forestry Biosecurity, College of Plant Protection, Nanjing Agricultural University, Nanjing 210095, China.
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The insecticide transport mechanisms in insects remain unclear. In Spodoptera exigua, we identified four secretory ApoD proteins. Structural modeling indicated that SeApoD1, SeApoD3, and SeApoD4 contain a conserved ligand-binding pocket accommodating lambda-cyhalothrin and chlorpyrifos with high affinity, while SeApoD2 exhibited a distorted cavity and negligible binding. The results of MicroScale Thermophoresis (MST) indicated that SeApoD3/4 had a high affinity for the two insecticides. Upregulation of three SeApoDs in a resistant strain implies a possible role in resistance, such as xenobiotic sequestration or tissue delivery. Our findings support a "molecular ferry" model for insecticide transport, broadening the functional scope of insect apolipoproteins and offering new insights into toxicodynamics and resistance evolution.
