Van Regenmortel Marc H V
Ecole Supérieure de Biotechnologie de Strasbourg, Illkirch Cedex, France.
Methods Mol Biol. 2009;524:3-20. doi: 10.1007/978-1-59745-450-6_1.
The antigenicity of proteins resides in different types of antigenic determinants known as continuous and discontinuous epitopes, cryptotopes, neotopes, and mimotopes. All epitopes have fuzzy boundaries and can be identified only by their ability to bind to certain antibodies. Antigenic cross-reactivity is a common phenomenon because antibodies are always able to recognize a considerable number of related epitopes. This places severe limits to the specificity of antibodies. Antigenicity, which is the ability of an epitope to react with an antibody, must be distinguished from its immunogenicity or ability to induce antibodies in a competent vertebrate host. Failure to make this distinction partly explains why no successful peptide-based vaccines have yet been developed. Methods for predicting the epitopes of proteins are discussed and the reasons for the low success rate of epitope prediction are analyzed.
蛋白质的抗原性存在于不同类型的抗原决定簇中，这些抗原决定簇被称为连续和不连续表位、隐蔽表位、新表位和模拟表位。所有表位都具有模糊的边界，并且只能通过它们与某些抗体结合的能力来识别。抗原交叉反应是一种常见现象，因为抗体总是能够识别相当数量的相关表位。这对抗体的特异性造成了严重限制。抗原性是指表位与抗体反应的能力，必须与它的免疫原性或在有能力的脊椎动物宿主中诱导抗体的能力区分开来。未能做出这种区分部分解释了为什么尚未开发出成功的基于肽的疫苗。本文讨论了预测蛋白质表位的方法，并分析了表位预测成功率低的原因。
