抗原相互作用和热失活会使人类IgE上暴露新的表位。

Antigen interaction and heat inactivation expose new epitopes on human IgE.

作者信息

Pachlopnik J M, Stämpfli M R, Rudolf M P, Aebischer I, Kricek F, Miescher S, Stadler B M

机构信息

Institute of Immunology and Allergology, University of Bern,

出版信息

Int Arch Allergy Immunol. 1998 Dec;117(4):231-8. doi: 10.1159/000024016.

DOI:10.1159/000024016

PMID:9876224

Abstract

It is well established that heat-denatured IgE is no longer capable of binding to FcepsilonRI. We have found an antibody that interacts with heat-denatured IgE. Interestingly, this antibody can also be used to detect some serum IgE, but not IgE synthesized de novo in vitro. However, native IgE can be transformed into an IgE that is recognized by this antibody, if antigen is added. Our data indicate that physiological mechanisms exist that biologically inactivate IgE which might still be mistaken for 'functional' IgE by assays based on polyclonal antibodies.

摘要

众所周知，热变性的IgE不再能够与FcepsilonRI结合。我们发现了一种与热变性IgE相互作用的抗体。有趣的是，这种抗体也可用于检测一些血清IgE，但不能检测体外重新合成的IgE。然而，如果添加抗原，天然IgE可以转化为能被这种抗体识别的IgE。我们的数据表明，存在生理机制可使IgE发生生物学失活，而基于多克隆抗体的检测方法可能仍会将其误判为“功能性”IgE。