In:
Molecular Nutrition & Food Research, Wiley, Vol. 67, No. 3 ( 2023-02)
Abstract:
Carrot ( Daucus carota ) allergy is caused by the major carrot allergen Dau c 1, which is a mixture of several isoallergens and variants with sequence identities of 〉 67% or 〉 90%, respectively. However, little is known about the qualitative and quantitative composition of natural Dau c 1. Methods and results Mass spectrometry of isolated natural Dau c 1 reveals the existence of several yet unknown Dau c 1‐like proteins. The study expresses four Dau c 1‐like proteins in Escherichia coli . Two of the purified proteins, designated Dau c 1.0501 and 1.0601, exhibit sequence identities to Dau c 1.0101 and 1.0401 between 54% and 87%. They possess allergenic potential and are accepted as new isoallergens. One protein, designated as Dau c 1‐like is 〉 50% identical with the new isoallergens but exhibits no allergenicity. Sequence and structural comparisons of this protein with the known Dau c 1 isoallergens offer relevant clues about putative structural IgE epitopes. Conclusion Identification of new isoallergens and the identification of IgE epitopes may contribute to a more refined component resolved diagnosis and may lay ground for further epitope mapping and personalized targeted treatment approaches of carrot allergy in preclinical and clinical studies.
Type of Medium:
Online Resource
ISSN:
1613-4125
,
1613-4133
DOI:
10.1002/mnfr.202200421
Language:
English
Publisher:
Wiley
Publication Date:
2023
detail.hit.zdb_id:
2160372-8
SSG:
12
