Inverse relation between structural flexibility and IgE reactivity of Cor a 1 hazelnut allergens.
Journal
Scientific reports
ISSN: 2045-2322
Titre abrégé: Sci Rep
Pays: England
ID NLM: 101563288
Informations de publication
Date de publication:
18 02 2021
18 02 2021
Historique:
received:
03
12
2020
accepted:
05
02
2021
entrez:
19
2
2021
pubmed:
20
2
2021
medline:
15
12
2021
Statut:
epublish
Résumé
A major proportion of allergic reactions to hazelnuts (Corylus avellana) are caused by immunologic cross-reactivity of IgE antibodies to pathogenesis-related class 10 (PR-10) proteins. Intriguingly, the four known isoforms of the hazelnut PR-10 allergen Cor a 1, denoted as Cor a 1.0401-Cor a 1.0404, share sequence identities exceeding 97% but possess different immunologic properties. In this work we describe the NMR solution structures of these proteins and provide an in-depth study of their biophysical properties. Despite sharing highly similar three-dimensional structures, the four isoforms exhibit remarkable differences regarding structural flexibility, hydrogen bonding and thermal stability. Our experimental data reveal an inverse relation between structural flexibility and IgE-binding in ELISA experiments, with the most flexible isoform having the lowest IgE-binding potential, while the isoform with the most rigid backbone scaffold displays the highest immunologic reactivity. These results point towards a significant entropic contribution to the process of antibody binding.
Identifiants
pubmed: 33603065
doi: 10.1038/s41598-021-83705-z
pii: 10.1038/s41598-021-83705-z
pmc: PMC7892832
doi:
Substances chimiques
Allergens
0
Antigens, Plant
0
Plant Proteins
0
Protein Isoforms
0
Immunoglobulin E
37341-29-0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
4173Subventions
Organisme : Austrian Science Fund FWF
ID : P 30737
Pays : Austria
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