Mapping IgE-binding epitopes of Ric c 1 and Ric c 3, allergens from Ricinus communis, by mast cell degranulation assay

被引：9
|
作者：
Felix, S. P.
Mayerhoffer, R. O.
Damatta, R. A. [1 ]
Vericimo, M. A. [2 ]
Nascimento, V. V.
Machado, O. L. T.
机构：
[1] Univ Estadual Norte Fluminense, Ctr Biociencias & Biotecnol, Lab Biol Celular & Tecidual, Darcy Ribeirao, Brazil
[2] Univ Fed Fluminense, Outeiro Sao Joao Batista Ctr, Ctr Estudos Gerais, Dept Imunobiol, BR-24210150 Niteroi, RJ, Brazil
来源：
PEPTIDES | 2008年 / 29卷 / 04期
关键词：
castor bean; 2S albumin; Ricinus communis; Ric c 1; Ric c 3; CB-1A;
D O I：
10.1016/j.peptides.2007.12.013
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
Ric c 1 and Ric c 3 are the major castor bean allergens. In order to identify continuous IgE-epitopes in Ric c 1 and Ric c 3, pools of sera from rats immunized with a pool of 2S albumin from these seeds, Ric c 1 and Ric c 3 overlapping synthetic peptides, were used to screen for IgE-binding epitopes. The allergenic properties were monitored by mast cell degranulation assays, histamine quantification and human-IgE binding. Large and small chains isolated from these proteins present allergenic properties. Four continuous epitopes were identified in Ric c 3 and two in Ric c 1. This knowledge may allow the induction of protective antibody responses to antagonize the IgE recognition. (C) 2007 Elsevier Inc. All rights reserved.
引用
收藏
页码：497 / 504
页数：8
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