ArticleNature communications2025
Cryo-EM structure of native honey bee vitellogenin.
Article in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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Who cites it
7 citing papers in PubMed.
- Simulation of CRISPR/Cas9-mediated gene editing for the Vitellogenin gene in Apis mellifera.Scientific reports · 2026Article
- Energy's long game: thermogenic adipocytes and the metabolic diseases of modern life.Academia biology · 2026Article
- Cryo-EM Analysis in CASP16.Proteins · 2026Article
- In silico prediction of the binding structure between vitellogenin and vitellogenin receptor of Haemaphysalis longicornis.The Journal of veterinary medical science · 2025Article
- Evidence for vitellogenin DNA-binding in honey bees.Protein science : a publication of the Protein Society · 2025Article
- Assessing structure-function impacts on Vitellogenin by leveraging allelic variant found in honey bee subspeciesiScience · 2025Article
- Ovary Activation Dynamics in the Bean WeevilInsects · 2025Article
Corrections and comments
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Authors and funding
8 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Vitellogenin (Vg) is the main yolk precursor lipoprotein in almost all egg-laying animals. In addition, along its evolutionary history, Vg has developed a range of new functions in different taxa. In the honey bee, Vg has functions related to immunity, antioxidant protection, social behavior and longevity. However, the molecular mechanisms underlying Vg functionalities are still poorly understood. Here, we report the cryo-EM structure of full-length honey bee Vg, one-step purified directly from hemolymph. The structure provides structural insights into the overall domain architecture, including the lipid binding cavity and the previously uncharacterized von Willebrand factor type D domain. A domain of unknown function has been identified as a C-terminal cystine knot domain based on structural homology. Information about post-translational modifications, cleavage products, metal and lipid binding allow an improved understanding of the mechanisms underlying the range of Vg functionalities. The findings have numerous implications for the structure-function relationship of vitellogenins of other species as well as members of the same protein superfamily, which share the same structural elements.
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