Allergenicity and IgE Recognition of New Dau c 1 Allergens from Carrot

被引:2
|
作者
Hendrich, Julian M. [1 ]
Wangorsch, Andrea [2 ]
Roedel, Katharina [1 ]
Jacob, Thessa [1 ]
Mahler, Vera [3 ]
Woehrl, Birgitta M. [1 ]
机构
[1] Univ Bayreuth, Lehrstuhl Biochem Biophys Chem 4, Univ Str 30, D-95447 Bayreuth, Germany
[2] Paul Ehrlich Inst, Mol Allergol, D-63225 Langen, Germany
[3] Paul Ehrlich Inst, Div Allergol, D-63225 Langen, Germany
关键词
allergenicity; Dau c 1 isoallergen; IgE cross reactivity; IgE epitopes; mediator release assay; BET V 1; BIRCH POLLEN; NORCOCLAURINE SYNTHASE; IDENTIFICATION; ENZYME; REACTIVITY; MECHANISM; SEARCH;
D O I
10.1002/mnfr.202200421
中图分类号
TS2 [食品工业];
学科分类号
0832 ;
摘要
ScopeCarrot (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 resultsMass 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. ConclusionIdentification 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.
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页数:9
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