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• Canals, Mateu Montserrat; Schnelle, Kilian; Leipart, Vilde; Halskau, Øyvind; Amdam, Gro Vang & Moeller, Arne [Vis alle 8 forfattere av denne artikkelen] (2025). Cryo-EM structure of native honey bee vitellogenin. Nature Communications. 16(1). doi: 10.1038/s41467-025-58575-y. Fulltekst i vitenarkiv Vis sammendrag

  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.

• Leipart, Vilde; Canals, Mateu Montserrat; Cunha, Eva Mariana de Sousa; Luecke, Hartmut; Herrero-Galán, Elías & Halskau, Øyvind [Vis alle 7 forfattere av denne artikkelen] (2021). Structure prediction of honey bee vitellogenin: a multi-domain protein important for insect immunity. FEBS Open Bio. 12(1), s. 51–70. doi: 10.1002/2211-5463.13316. Fulltekst i vitenarkiv Vis sammendrag

  Vitellogenin (Vg) has been implicated as a central protein in the immunity of egg-laying animals. Studies on a diverse set of species suggest that Vg supports health and longevity through binding to pathogens. Specific studies of honey bees (Apis mellifera) further indicate that the vitellogenin (vg) gene undergoes selection driven by local pathogen pressures. Determining the complete 3D structure of full-length Vg (flVg) protein will provide insights regarding the structure–function relationships underlying allelic variation. Honey bee Vg has been described in terms of function, and two subdomains have been structurally described, while information about the other domains is lacking. Here, we present a structure prediction, restrained by experimental data, of flVg from honey bees. To achieve this, we performed homology modeling and used AlphaFold before using a negative-stain electron microscopy map to restrict, orient, and validate our 3D model. Our approach identified a highly conserved Ca2+-ion-binding site in a von Willebrand factor domain that might be central to Vg function. Thereafter, we used rigid-body fitting to predict the relative position of high-resolution domains in a flVg model. This mapping represents the first experimentally validated full-length protein model of a Vg protein and is thus relevant for understanding Vg in numerous species. Our results are also specifically relevant to honey bee health, which is a topic of global concern due to rapidly declining pollinator numbers.

• Cunha, Eva; Chen, Xiaorui; Gaitero, Marta Sanz; J, Deryck Mills & Luecke, Hartmut (2021). Cryo-EM structure of Helicobacter pylori urease with an inhibitor in the active site at 2.0 Å resolution. Nature Communications. 12:230, s. 1–8. doi: 10.1038/s41467-020-20485-6. Fulltekst i vitenarkiv

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• Cunha, Eva Mariana de Sousa; Chen, Xiaorui; Gaitero, Marta Sanz; Mills, Deryck J. & Lücke, Hartmut (2023). Author Correction: Cryo-EM structure of Helicobacter pylori urease with an inhibitor in the active site at 2.0 Å resolution (Nature Communications, (2021), 12, 1, (230), 10.1038/s41467-020-20485-6). Nature Communications. 14(1). doi: 10.1038/s41467-023-36404-4. Fulltekst i vitenarkiv
• Canals, Mateu Montserrat; Schnelle, Kilian; Leipart, Vilde; Halskau, Øyvind; Amdam, Gro Vang & Moeller, Arne [Vis alle 8 forfattere av denne artikkelen] (2023). The high-resolution cryo-EM structure of vitellogenin from the hemolymph of the honey bee. Fulltekst i vitenarkiv
• Heim, Joel Benjamin; Kersten, Flore Marie Colette; Cunha, Eva & Luecke, Hartmut (2020). Survival in acidic environments – Structure and mechanism of bacterial urea channels. Fulltekst i vitenarkiv

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