Moraes A H, Ackerbauer D, Kostadinova M, Bublin M, Ferreira F, Almeida F C L, Breiteneder H, Valente A P
Centro Nacional de Ressonância Magnética, Instituto de Bioquímica Médica, Universidade Federal do Rio de Janeiro, Rio de Janeiro, Brazil.
Biomol NMR Assign. 2013 Oct;7(2):133-6. doi: 10.1007/s12104-012-9393-y. Epub 2012 May 15.
Gad m 1 is the major allergen from Atlantic cod. It belongs to β-parvalbumin protein family and is characterized by the presence of two calcium-binding sites so called EF-hand motifs. β-Parvalbumins such as Gad m 1 are the most important fish allergens and their high cross-reactivity is the cause of the observed polysensitization to various fish species in allergic patients. Despite extensive efforts, the complete elucidation of β-parvalbumin-IgE complexes has not been achieved yet. Allergen structural studies are essential for the development of novel immunotherapy strategies, including vaccination with hypoallergenic derivatives and chimeric molecules. Here, we report for the first time the NMR study of a β-parvalbumin: Gad m 1. This report includes: (1)H, (13)C and (15)N resonance assignments of Gad m 1 as well as the second structure information based on the (13)C chemical shifts.
Gad m 1是大西洋鳕鱼的主要过敏原。它属于β-原肌球蛋白蛋白家族,其特征是存在两个所谓的EF-手基序的钙结合位点。诸如Gad m 1之类的β-原肌球蛋白是最重要的鱼类过敏原,它们的高交叉反应性是过敏患者对各种鱼类出现多敏化现象的原因。尽管付出了巨大努力,但尚未完全阐明β-原肌球蛋白-IgE复合物。过敏原结构研究对于开发新型免疫治疗策略至关重要,包括用低敏衍生物和嵌合分子进行疫苗接种。在此,我们首次报告了对一种β-原肌球蛋白:Gad m 1的核磁共振研究。本报告包括:Gad m 1的(1)H、(13)C和(15)N共振归属以及基于(13)C化学位移的二级结构信息。