ArticleJournal of insect science (Online)2026
Sequence and structure analysis for chemosensory proteins and odorant-binding proteins in Nilaparvata lugens (Hemiptera: Delphacidae).
Article in Journal of insect science (Online), 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
0 citing papers in PubMed.
No citing paper in PubMed yet.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors.
Funding
Abstract
Chemosensation is crucial for insect behavior and physiology, involving several molecules. Chemosensory proteins (CSPs) and odorant-binding proteins (OBPs) transport volatile and lipophilic semiochemicals to activate the chemosensory system. Nilaparvata lugens Stål, is a monophagous pest of rice plants, causing significant economic losses worldwide. To date, 15 CSPs and 13 OBPs have been characterized, but their functions have not been fully investigated especially regarding their binding affinity with various ligands. This study compares the commonalities and differences between the 15 CSPs and 13 OBPs regarding sequence similarity, phylogeny, structural identity, and binding affinity with 3 different ligands. As expected, all 15 CSPs contain 4 conserved cysteine residues and 6 α-helical domains, whereas 13 OBPs have at least 6 cysteine residues and 6 α-helical domains. CSP1, 2, 8, and 14 cluster together in the phylogenetic tree, showing high structural similarity and similar binding affinity to the 3 ligands. OBP9 and 10 form a clade with high structural conservation; however, molecular docking indicates OBP9 exhibits a high binding affinity for the insecticide thiamethoxam. Three OBPs, OBP56d, OBPunknown1, and OBPunknown2 have been characterized and they display no significant preference for the 3 ligands. Overall, our integrated sequence and structural analysis reveals both functional redundancy and specific ligand preferences within the N. lugens chemosensory system. These findings provide a critical foundation for understanding the molecular basis of chemoreception in N. lugens and may inform the development of novel behavioral interference strategies.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.