Cryo-EM structure of native honey bee vitellogenin
Mateu Montserrat-Canals,
Kilian Schnelle,
Vilde Leipart,
Øyvind Halskau,
Gro V. Amdam,
Arne Moeller,
Eva S. Cunha and
Hartmut Luecke ()
Additional contact information
Mateu Montserrat-Canals: University of Oslo
Kilian Schnelle: University of Osnabrück
Vilde Leipart: Norwegian University of Life Sciences
Øyvind Halskau: University of Bergen
Gro V. Amdam: Norwegian University of Life Sciences
Arne Moeller: University of Osnabrück
Eva S. Cunha: Proteros biostructures GmbH
Hartmut Luecke: Nova University School of Science and Technology
Nature Communications, 2025, vol. 16, issue 1, 1-13
Abstract:
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.
Date: 2025
References: Add references at CitEc
Citations:
Downloads: (external link)
https://www.nature.com/articles/s41467-025-58575-y Abstract (text/html)
Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.
Export reference: BibTeX
RIS (EndNote, ProCite, RefMan)
HTML/Text
Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:16:y:2025:i:1:d:10.1038_s41467-025-58575-y
Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/
DOI: 10.1038/s41467-025-58575-y
Access Statistics for this article
Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie
More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().