Chipinda Itai, Hettick Justin M, Siegel Paul D
Health Effects Laboratory Division, National Institute for Occupational Safety and Health, Centers for Disease Control and Prevention, MS L-2040, 1095 Willowdale Road, Morgantown, WV 26505, USA.
J Allergy (Cairo). 2011;2011:839682. doi: 10.1155/2011/839682. Epub 2011 Jun 30.
Low molecular weight chemical (LMW) allergens are commonly referred to as haptens. Haptens must complex with proteins to be recognized by the immune system. The majority of occupationally related haptens are reactive, electrophilic chemicals, or are metabolized to reactive metabolites that form covalent bonds with nucleophilic centers on proteins. Nonelectrophilic protein binding may occur through disulfide exchange, coordinate covalent binding onto metal ions on metalloproteins or of metal allergens, themselves, to the major histocompatibility complex. Recent chemical reactivity kinetic studies suggest that the rate of protein binding is a major determinant of allergenic potency; however, electrophilic strength does not seem to predict the ability of a hapten to skew the response between Th1 and Th2. Modern proteomic mass spectrometry methods that allow detailed delineation of potential differences in protein binding sites may be valuable in predicting if a chemical will stimulate an immediate or delayed hypersensitivity. Chemical aspects related to both reactivity and protein-specific binding are discussed.
低分子量化学（LMW）过敏原通常被称为半抗原。半抗原必须与蛋白质结合才能被免疫系统识别。大多数与职业相关的半抗原是具有反应性的亲电子化学物质，或者被代谢为与蛋白质上亲核中心形成共价键的反应性代谢物。非亲电子性的蛋白质结合可能通过二硫键交换、配位共价结合到金属蛋白上的金属离子或金属过敏原自身与主要组织相容性复合体发生。最近的化学反应动力学研究表明，蛋白质结合速率是致敏效力的主要决定因素；然而，亲电子强度似乎并不能预测半抗原偏向Th1和Th2反应的能力。现代蛋白质组质谱方法能够详细描绘蛋白质结合位点的潜在差异，这对于预测一种化学物质是否会引发速发型或迟发型超敏反应可能具有重要价值。本文讨论了与反应性和蛋白质特异性结合相关的化学方面。
