The Crystal Structure of the Spodoptera litura Chemosensory Protein CSP8

Abstract

Spodoptera litura F. is a generalist herbivore and one of the most important economic pests feeding on about 300 host plants in many Asian countries. Specific insect behaviors can be stimulated after recognizing chemicals in the external environment through conserved chemosensory proteins (CSPs) in chemoreceptive organs, which are critical components of the olfactory systems. To explore its structural basis for ligand-recognizing capability, we solved the 2.3 Å crystal structure of the apoprotein of S. litura CSP8 (SlCSP8). The SlCSP8 protein displays a conserved spherical shape with a negatively charged surface. Our binding assays showed that SlCSP8 bound several candidate ligands with differential affinities, with rhodojaponin III being the most tightly bound ligand. Our crystallographic and biochemical studies provide important insight into the molecular recognition mechanism of the sensory protein SlCSP8 and the CSP family in general, and they suggest that CSP8 is critical for insects to identify rhodojaponin III, which may aid in the CSP-based rational drug design in the future.

Quantitative Study on Anti-Pest Activity of Natural Products Based on Visualization Framework of Knowledge Graph

“…However, the chemical transformation and structure-activity relationship of lauryl alcohol needs further study. The main active constituents of the insecticide obtained from Rhododendron molle is tetracyclic diterpenes with rhodojaponin-III one of the more active components [114,115] . A pot experiment testing the efficacy of rhodojaponin-III against Spodoptera litura larvae showed that after treatment with a concentration of 500 g• mL −1 rhodojaponin-III, the population reduction rate of S. litura was 53.2%, 64.1%, and 79.7% at 1, 3 and 7 days after treatment, respectively.…”

Renaming ‘Chemosensory’ Proteins (CSPs): ‘Lipoid-Binding Proteins’ — Molecular Nomenclature, Structure, Expression, Evolution, and Intracellular Functions

“…According to Lartigue et al [7], CSPs are composed of six -helices with an appropriate molecular weight of 10-12 kDa (or 110-120 amino acid residues), four cysteines that form two tiny loops, two nearby disulfide bridges, and a globular "prism-like" functional structure. Four CSP structures have so far been identified in locusts (Schistocerca gregaria) and moths (Mamestra brassicae, Bombyx mori, and Spodoptera litura) [7][8][9][10][11]. These structures can breathe' or modify their conformation in certain ways in response to ligand binding [12,13].…”

Comparison and Functional Analysis of Odorant-Binding Proteins and Chemosensory Proteins in Two Closely Related Thrips Species, Frankliniella occidentalis and Frankliniella intonsa (Thysanoptera: Thripidae) Based on Antennal Transcriptome Analysis

“…To date, the structures of more than 20 OBPs have been reported in insects [25,26]. By contrast, the structures of very few CSPs are currently available [22][23][24]27]. The three-dimensional structure-based action mechanism of OBPs has been reported in insect species in Lepidoptera, Diptera, and Hemiptera, etc.…”