ArticleProtein science : a publication of the Protein Society2022
Identification of 121 variants of honey bee Vitellogenin protein sequences with structural differences at functional sites.
Article in Protein science : a publication of the Protein Society, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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9 citing papers in PubMed, 12 citations in OpenAlex.
- Simulation of CRISPR/Cas9-mediated gene editing for the Vitellogenin gene in Apis mellifera.Scientific reports · 2026Article
- Population Genetic Study ofEcology and evolution · 2026Article
- AI-enhanced marker-assisted selection concept for the multifunctional honey bee (Hymenoptera: Apidea) protein Vitellogenin (Vg).Journal of economic entomology · 2025Article
- Assessing structure-function impacts on Vitellogenin by leveraging allelic variant found in honey bee subspeciesiScience · 2025Article
- Genomic signatures associated with the evolutionary loss of egg yolk in parasitoid wasps.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- A Barcoded ITS Primer-Based Nanopore Sequencing Protocol for Detection ofJournal of fungi (Basel, Switzerland) · 2025Article
- Honey Bee Larval Hemolymph as a Source of Key Nutrients and Proteins Offers a Promising Medium forInternational journal of molecular sciences · 2023Article
- Identification of 121 variants of honey bee Vitellogenin protein sequences with structural differences at functional sites.Protein science : a publication of the Protein Society · 2022Article
- How Honey Bee Vitellogenin Holds Lipid Cargo: A Role for the C-Terminal.Frontiers in molecular biosciences · 2022Article
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Authors and funding
9 authors at 3 institutions in 2 countries.
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Abstract
Proteins are under selection to maintain central functions and to accommodate needs that arise in ever-changing environments. The positive selection and neutral drift that preserve functions result in a diversity of protein variants. The amount of diversity differs between proteins: multifunctional or disease-related proteins tend to have fewer variants than proteins involved in some aspects of immunity. Our work focuses on the extensively studied protein Vitellogenin (Vg), which in honey bees (Apis mellifera) is multifunctional and highly expressed and plays roles in immunity. Yet, almost nothing is known about the natural variation in the coding sequences of this protein or how amino acid-altering variants might impact structure-function relationships. Here, we map out allelic variation in honey bee Vg using biological samples from 15 countries. The successful barcoded amplicon Nanopore sequencing of 543 bees revealed 121 protein variants, indicating a high level of diversity in Vg. We find that the distribution of non-synonymous single nucleotide polymorphisms (nsSNPs) differs between protein regions with different functions; domains involved in DNA and protein-protein interactions contain fewer nsSNPs than the protein's lipid binding cavities. We outline how the central functions of the protein can be maintained in different variants and how the variation pattern may inform about selection from pathogens and nutrition.
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