Czaja M, Richards F F, Varga J M
Ann Immunol (Paris). 1976 Jun-Jul;127(3-4):253-60.
It seems likely that immunoglobulins have evolved from some archetypal molecule and those forms which are useful to the animal have been retained. It is this entire population of antibodies which forms the humoral immune system and in such a system, not only the properties of individual antibody combining regions, but the properties of the multiprotein system as a whole, are important for the defences of the body against pathogens. Antibody combining sites may bind a disparate set of structurally related and unrelated ligands. This multispecificity can be biologically meaningful: the same clone can be stimulated by different antigens. In this sense, cell surface immunoglobulins are multifunctional. The major biological consequence of antibody multispecificity is overlapping binding functions within subsets of the total antibody repertoire. The most significant impact of this overlap is: (1) it reduces the number of V genes necessary to code for the total number of combining sites; (2) the cross-stimulation of clones by structurally related and unrelated antigens may be instrumental in the normal maintenance of immune responsiveness and in addition, it may explain the ability to respond to unusual and less ubiquitous antigens; (3) the antigenic history of the animal may contribute to the maturation of the immune response by cross-stimulation of pre-selected clones of antigen binding cells.
免疫球蛋白似乎是从某种原型分子进化而来的，那些对动物有用的形式被保留了下来。正是这一整套抗体构成了体液免疫系统，在这样一个系统中，不仅单个抗体结合区域的特性，而且整个多蛋白系统的特性，对于身体抵御病原体的防御作用都很重要。抗体结合位点可以结合一系列结构相关和不相关的配体。这种多特异性在生物学上可能是有意义的：同一个克隆可以被不同的抗原刺激。从这个意义上说，细胞表面免疫球蛋白是多功能的。抗体多特异性的主要生物学后果是在整个抗体库的子集中存在重叠的结合功能。这种重叠的最重要影响是：（1）它减少了编码结合位点总数所需的V基因数量；（2）结构相关和不相关抗原对克隆的交叉刺激可能有助于正常维持免疫反应性，此外，它可能解释了对不常见和不太普遍的抗原作出反应的能力；（3）动物的抗原史可能通过对预先选择的抗原结合细胞克隆的交叉刺激，促进免疫反应的成熟。
