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Identification reveals binding affinity of secretory proteins in Spodoptera exigua, suggesting roles in toxicodynamics.
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.
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Liu et al. (2025) studied this question.
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