ArticleJournal of insect science (Online)2023
Odorant-binding Protein 10 From Bradysia odoriphaga (Diptera: Sciaridae) Binds Volatile Host Plant Compounds.
Article in Journal of insect science (Online), 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
6 citing papers in PubMed.
- Butterfly brains change in morphology and in gene splicing patterns after brief pheromone exposure.BMC biology · 2026Article
- Neophytadiene, a Plant Specialized Metabolite, Mediates the Virus-Vector-Plant Tripartite Interactions.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Molecular Characterization of Plant Volatile Compound Interactions withPlants (Basel, Switzerland) · 2024Article
- The Sequence Characteristics and Binding Properties of the Odorant-Binding Protein SvelOBP1 fromLife (Basel, Switzerland) · 2024Article
- Characterization of the ligand-binding properties of odorant-binding protein 38 fromFrontiers in physiology · 2024Article
- Roles of insect odorant binding proteins in communication and xenobiotic adaptation.Frontiers in insect science · 2023Review
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
Bradysia odoriphaga (Diptera: Sciaridae) is a major insect pest of seven plant families including 30 commercial crops in Asia. The long-term use of chemical pesticides leads to problems such as insect resistance, environmental issues, and food contamination. Against this background, a novel pest control method should be developed. In insects, odorant-binding proteins (OBPs) transport odor molecules, including pheromones and plant volatiles, to olfactory receptors. Here, we expressed and characterized the recombinant B. odoriphaga OBP BodoOBP10, observing that it could bind the sulfur-containing compounds diallyl disulfide and methyl allyl disulfide with Ki values of 8.01 μM and 7.00 μM, respectively. Homology modeling showed that the BodoOBP10 3D structure was similar to that of a typical OBP. Both diallyl disulfide and methyl allyl disulfide bound to the same site on BodoOBP10, mediated by interactions with six hydrophobic residues Met70, Ile75, Thr89, Met90, Leu93, and Leu94, and one aromatic residue, Phe143. Furthermore, silencing BodoOBP10 expression via RNAi significantly reduced the electroantennogram (EAG) response to diallyl disulfide and methyl allyl disulfide. These findings suggest that BodoOBP10 should be involved in the recognition and localization of host plants.
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Registered trials
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