Digested Ara h 1 Loses Sensitizing Capacity When Separated into Fractions

被引:27
作者
Bogh, Katrine L. [1 ]
Barkholt, Vibeke [2 ]
Rigby, Neil M. [3 ]
Mills, E. N. Clare [3 ]
Madsen, Charlotte B. [1 ]
机构
[1] Tech Univ Denmark, Natl Food Inst, Div Toxicol & Risk Assessment, DK-2860 Soborg, Denmark
[2] Tech Univ Denmark, Dept Syst Biol Enzyme & Prot Chem, DK-2800 Lyngby, Denmark
[3] Inst Food Res, Norwich NR4 7UA, Norfolk, England
关键词
Ara h 1; digestion; animal model; food allergy; peptides; aggregation; MAJOR PEANUT ALLERGEN; STRUCTURE-IMMUNOGENICITY RELATIONSHIP; IGE-BINDING EPITOPES; B-CELL EPITOPES; FOOD ALLERGENS; GASTROINTESTINAL DIGESTION; SYNTHETIC PEPTIDES; PROTEINS; ANTIBODIES; MELITTIN;
D O I
10.1021/jf2052306
中图分类号
S [农业科学];
学科分类号
082806 [农业信息与电气工程];
摘要
The major peanut allergen Ara h 1 is an easily digestible protein under physiological conditions. The present study revealed that pepsin digestion products of Ara h 1 retained the sensitizing potential in a Brown Norway rat model, while this sensitizing capacity was lost by separating the digest into fractions by gel permeation chromatography. Protein chemical analysis showed that the peptide composition as well as the aggregation profiles of the fractions of Ara h 1 digest differed from that of the whole pool. These results indicate that the sensitizing capacity of digested Ara h 1 is a consequence of the peptides being in an aggregated state resembling the intact molecule or that most peptides of the digests need to be present in the same solution, having a synergistic or adjuvant effect and thereby augmenting the immune response against other peptides.
引用
收藏
页码:2934 / 2942
页数:9
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