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Identification of a polygalacturonase (Cup s 2) as the major CCD ‐bearing allergen in Cupressus sempervirens pollen
Author(s) -
Shahali Y.,
Sutra J.P.,
Hilger C.,
Swiontek K.,
Haddad I.,
Vinh J.,
Guilloux L.,
Charpin D.,
Sénéchal H.,
Poncet P.
Publication year - 2017
Publication title -
allergy
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.363
H-Index - 173
eISSN - 1398-9995
pISSN - 0105-4538
DOI - 10.1111/all.13191
Subject(s) - cypress , allergen , pollen , cupressus , pectinase , immunoglobulin e , epitope , biology , aeroallergen , cross reactivity , botany , microbiology and biotechnology , immunology , allergy , biochemistry , cross reactions , antigen , antibody , enzyme
As IgE glyco‐epitopes, also referred to as cross‐reactive carbohydrate determinants ( CCD s), can share significant structural homologies between different plants, they are prone to extensive cross‐reactivity among allergen pollen extracts. Here, cypress pollen allergens, especially a polygalacturonase ( PG ), were further characterized using double one‐dimensional electrophoresis (D1‐ DE ). The presence of specific IgE directed against CCD s was investigated by bromelain IgE inhibition and concanavalin A binding assays using sera of cypress pollen‐sensitized patients. Our results showed that IgE reactivity to CCD s in Cupressus sempervirens pollen extracts is mainly related to bromelain‐type epitopes of a newly identified cypress PG . This glycoprotein has been further characterized through an immunoproteomic approach and officially indexed as Cup s 2 by the WHO / IUIS allergen nomenclature. Cup s 2 could thus be associated with the increased prevalence of IgE reactivity to cypress pollen extracts because of CCD interference.