Restani P, Fiocchi A, Beretta B, Velonà T, Giovannini M, Galli C L
Laboratory of Toxicology, Institute of Pharmacological Sciences, University of Milan, Italy.
Int Arch Allergy Immunol. 1998 Oct;117(2):113-9. doi: 10.1159/000023997.
Bovine serum albumin (BSA) is one of the most widely studied proteins; its structure is well-known and its antigenic characteristics have been described in studies performed in in vitro and animal models. The aim of our work was to evaluate the role of BSA conformation in its antigenicity (recognition by circulating IgEs from allergic children).
This study was performed using electrophoresis associated with the immunoblotting technique, where sera from children sensitized to BSA (as shown by double-blind placebo-controlled food challenge) were used.
Heat treatment and chemical denaturation (SDS treatment) are not able to decrease the BSA capability to bind circulating IgEs. Only by reducing treatment with 2-mercaptoethanol is it possible to modify but not to eliminate the antigenicity of this protein. The reactivity to other serum albumins from different animal species was also investigated and in this study we show a direct correlation between the number of IgE-mediated responses observed in immunoblotting and the percentage of sequence identity (phylogenetic similarity) of serum albumins.
Data obtained in this research indicate that serum albumin antigenicity is only partially correlated to its native three-dimensional structure.
牛血清白蛋白（BSA）是研究最为广泛的蛋白质之一；其结构广为人知，并且在体外和动物模型研究中已对其抗原特性进行了描述。我们研究的目的是评估BSA构象在其抗原性（过敏性儿童循环IgE的识别）中的作用。
本研究采用与免疫印迹技术相关的电泳方法，使用对BSA致敏儿童的血清（通过双盲安慰剂对照食物激发试验证实）。
热处理和化学变性（SDS处理）无法降低BSA与循环IgE结合的能力。只有通过用2-巯基乙醇进行还原处理，才有可能改变但无法消除该蛋白质的抗原性。我们还研究了对来自不同动物物种的其他血清白蛋白的反应性，并且在本研究中我们显示，在免疫印迹中观察到的IgE介导反应的数量与血清白蛋白的序列同一性百分比（系统发育相似性）之间存在直接相关性。
本研究获得的数据表明，血清白蛋白抗原性仅部分与其天然三维结构相关。
