Identification of 121 variants of honey bee Vitellogenin protein sequences with structural differences at functional sites.
Vitellogenin
honey bee
long-range amplicon sequencing
protein variants
Journal
Protein science : a publication of the Protein Society
ISSN: 1469-896X
Titre abrégé: Protein Sci
Pays: United States
ID NLM: 9211750
Informations de publication
Date de publication:
07 2022
07 2022
Historique:
received:
19
04
2022
accepted:
21
05
2022
entrez:
28
6
2022
pubmed:
29
6
2022
medline:
1
7
2022
Statut:
ppublish
Résumé
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.
Identifiants
pubmed: 35762708
doi: 10.1002/pro.4369
pmc: PMC9207902
doi:
Substances chimiques
Vitellogenins
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
e4369Informations de copyright
© 2022 The Authors. Protein Science published by Wiley Periodicals LLC on behalf of The Protein Society.
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