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Where Honey Bee Vitellogenin may Bind Zn2+-Ions

View ORCID ProfileVilde Leipart, Øyvind Enger, Diana Cornelia Turcu, Olena Dobrovolska, Finn Drabløs, Øyvind Halskau, Gro V. Amdam
doi: https://doi.org/10.1101/2022.01.28.478200
Vilde Leipart
1Faculty of Environmental Sciences and Natural Resource Management, Norwegian University of Life Sciences, Aas, Norway
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  • For correspondence: vilde.leipart@nmbu.no
Øyvind Enger
1Faculty of Environmental Sciences and Natural Resource Management, Norwegian University of Life Sciences, Aas, Norway
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Diana Cornelia Turcu
2Department of Biological Sciences, University of Bergen, Bergen, Norway
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Olena Dobrovolska
3Helse Bergen, Bergen, Norway
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Finn Drabløs
4Department of Clinical and Molecular Medicine, Faculty of Medicine and Health Sciences, NTNU – Norwegian University of Science and Technology, Trondheim, Norway
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Øyvind Halskau
2Department of Biological Sciences, University of Bergen, Bergen, Norway
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Gro V. Amdam
1Faculty of Environmental Sciences and Natural Resource Management, Norwegian University of Life Sciences, Aas, Norway
5School of Life Sciences, Arizona State University, Tempe, AZ, United States
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Abstract

The protein Vitellogenin (Vg) plays a central role in lipid transportation in most egg-laying animals. High Vg levels correlate with stress resistance and lifespan potential in honey bees (Apis mellifera). Vg is the primary circulating zinc-carrying protein in honey bees. Zinc is an essential metal ion in numerous biological processes, including the function and structure of many proteins. Measurements of Zn2+ suggest a variable number of ions per Vg molecule in different animal species, but the molecular implications of zinc-binding by this protein are not well understood. We used inductively coupled plasma mass spectrometry (ICP-MS) to determine that, on average, each honey bee Vg molecule binds 3 Zn2+-ions. Our full-length protein structure and sequence analysis revealed seven potential zinc-binding sites. These are located in the β-barrel and α-helical subdomains of the N-terminal domain, the lipid binding site, and the cysteine-rich C-terminal region of unknown function. Interestingly, two potential zinc-binding sites in the β-barrel can support a proposed role for this structure in DNA-binding. Overall, our findings illustrate the capacity of honey bee Vg to bind zinc at several functional regions, indicating that Zn2+-ions are important for many of the activities of this protein. In addition to being potentially relevant for other egg-laying species, these insights provide a platform for studies of metal ions in bee health, which is of global interest due to recent declines in pollinator numbers.

Competing Interest Statement

The authors have declared no competing interest.

  • Abbreviations

    (DUF1943)
    Domain of unknown function
    (ICP-MS)
    Inductively coupled plasma mass spectrometry
    (MSA)
    multiple sequence alignment
    (Vg)
    Vitellogenin
    (vWF)
    von Willebrand factor
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    Posted January 28, 2022.
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    Where Honey Bee Vitellogenin may Bind Zn2+-Ions
    Vilde Leipart, Øyvind Enger, Diana Cornelia Turcu, Olena Dobrovolska, Finn Drabløs, Øyvind Halskau, Gro V. Amdam
    bioRxiv 2022.01.28.478200; doi: https://doi.org/10.1101/2022.01.28.478200
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    Where Honey Bee Vitellogenin may Bind Zn2+-Ions
    Vilde Leipart, Øyvind Enger, Diana Cornelia Turcu, Olena Dobrovolska, Finn Drabløs, Øyvind Halskau, Gro V. Amdam
    bioRxiv 2022.01.28.478200; doi: https://doi.org/10.1101/2022.01.28.478200

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