ArticleScientific reports2021
A new non-classical fold of varroa odorant-binding proteins reveals a wide open internal cavity.
Article in Scientific reports, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 10 citations in OpenAlex.
- Efficacy and safety of Moroccan and Turkish essential oils against Varroa destructor: varroacidal potency, locomotor activity impact, and mechanistic insights via molecular docking.Experimental & applied acarology · 2026Article
- Integrative Omics and AI-Driven Systems Biology: Multilayer Networks DecodingJournal of proteome research · 2025Review
- Smelly communication between haemaphysalis longicornis and infected hosts with indolic odorants: A case from severe fever with thrombocytopenia syndrome virus.PLoS neglected tropical diseases · 2025Article
- Current status of structural studies of proteins originating from Arachnida.Systematic and applied acarology · 2023Article
- An odorant-binding protein in the elephant's trunk is finely tuned to sex pheromone (Z)-7-dodecenyl acetate.Scientific reports · 2022Article
- The Odorant-Binding Proteins of the Spider MiteInternational journal of molecular sciences · 2021Article
Corrections and comments
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Authors and funding
13 authors at 7 institutions in 4 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Odorant-binding proteins (OBPs), as they occur in insects, form a distinct class of proteins that apparently has no closely related representatives in other animals. However, ticks, mites, spiders and millipedes contain genes encoding proteins with sequence similarity to insect OBPs. In this work, we have explored the structure and function of such non-insect OBPs in the mite Varroa destructor, a major pest of honey bee. Varroa OBPs present six cysteines paired into three disulphide bridges, but with positions in the sequence and connections different from those of their insect counterparts. VdesOBP1 structure was determined in two closely related crystal forms and appears to be a monomer. Its structure assembles five α-helices linked by three disulphide bridges, one of them exhibiting a different connection as compared to their insect counterparts. Comparison with classical OBPs reveals that the second of the six α-helices is lacking in VdesOBP1. Ligand-binding experiments revealed molecules able to bind only specific OBPs with a moderate affinity, suggesting that either optimal ligands have still to be identified, or post-translational modifications present in the native proteins may be essential for modulating binding activity, or else these OBPs might represent a failed attempt in evolution and are not used by the mites.
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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.