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Identification of 121 variants of honey bee Vitellogenin protein sequences with structural differences at functional sites

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...

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Autores principales: Leipart, Vilde, Ludvigsen, Jane, Kent, Matthew, Sandve, Simen, To, Thu‐Hien, Árnyasi, Mariann, Kreibich, Claus D., Dahle, Bjørn, Amdam, Gro V.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley & Sons, Inc. 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9207902/
https://www.ncbi.nlm.nih.gov/pubmed/35762708
http://dx.doi.org/10.1002/pro.4369
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author Leipart, Vilde
Ludvigsen, Jane
Kent, Matthew
Sandve, Simen
To, Thu‐Hien
Árnyasi, Mariann
Kreibich, Claus D.
Dahle, Bjørn
Amdam, Gro V.
author_facet Leipart, Vilde
Ludvigsen, Jane
Kent, Matthew
Sandve, Simen
To, Thu‐Hien
Árnyasi, Mariann
Kreibich, Claus D.
Dahle, Bjørn
Amdam, Gro V.
author_sort Leipart, Vilde
collection PubMed
description 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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spelling pubmed-92079022022-06-27 Identification of 121 variants of honey bee Vitellogenin protein sequences with structural differences at functional sites Leipart, Vilde Ludvigsen, Jane Kent, Matthew Sandve, Simen To, Thu‐Hien Árnyasi, Mariann Kreibich, Claus D. Dahle, Bjørn Amdam, Gro V. Protein Sci Full‐length Papers 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. John Wiley & Sons, Inc. 2022-06-20 2022-07 /pmc/articles/PMC9207902/ /pubmed/35762708 http://dx.doi.org/10.1002/pro.4369 Text en © 2022 The Authors. Protein Science published by Wiley Periodicals LLC on behalf of The Protein Society. https://creativecommons.org/licenses/by-nc-nd/4.0/This is an open access article under the terms of the http://creativecommons.org/licenses/by-nc-nd/4.0/ (https://creativecommons.org/licenses/by-nc-nd/4.0/) License, which permits use and distribution in any medium, provided the original work is properly cited, the use is non‐commercial and no modifications or adaptations are made.
spellingShingle Full‐length Papers
Leipart, Vilde
Ludvigsen, Jane
Kent, Matthew
Sandve, Simen
To, Thu‐Hien
Árnyasi, Mariann
Kreibich, Claus D.
Dahle, Bjørn
Amdam, Gro V.
Identification of 121 variants of honey bee Vitellogenin protein sequences with structural differences at functional sites
title Identification of 121 variants of honey bee Vitellogenin protein sequences with structural differences at functional sites
title_full Identification of 121 variants of honey bee Vitellogenin protein sequences with structural differences at functional sites
title_fullStr Identification of 121 variants of honey bee Vitellogenin protein sequences with structural differences at functional sites
title_full_unstemmed Identification of 121 variants of honey bee Vitellogenin protein sequences with structural differences at functional sites
title_short Identification of 121 variants of honey bee Vitellogenin protein sequences with structural differences at functional sites
title_sort identification of 121 variants of honey bee vitellogenin protein sequences with structural differences at functional sites
topic Full‐length Papers
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9207902/
https://www.ncbi.nlm.nih.gov/pubmed/35762708
http://dx.doi.org/10.1002/pro.4369
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