Antigenic regions defined by monoclonal antibodies correspond to structural domains of avian lysozyme.
Antigenic regions defined by monoclonal antibodies correspond to structural domains of avian lysozyme.
复制标题
由单克隆抗体定义的抗原区域对应于禽类溶菌酶的结构域。
作者：
S. Smith‐Gill;T. Lavoie;C. Mainhart
对6个新的蛋清溶菌酶蛋白抗原特异性BALB/c杂交瘤所识别的表位进行了详细的定位。尽管所有抗体的精细特异性都是不同的，但许多表位以复杂的模式重叠。抗体可分为三个互补组，其中一个还包括先前表征的对Arg68特异性的HyHEL -5。在互补组之间和互补组内，抗体之间观察到复杂的相互作用，包括非互惠竞争和增强的结合。其中两个互补基团位于催化位点附近的新抗原区域。抗体HyHEL -8和HyHEL -10具有非常相似和重叠的特异性，并且可能识别非常密切相关的表位。结果表明，抗原表位可能形成一个连续的抗原表面，抗原区域对应于由HEL三级结构定义的结构域。
The epitopes recognized by six new BALB/c hybridomas specific for the protein antigen hen egg-white lysozyme (HEL) were mapped in detail. Although fine specificities of all the antibodies were distinct, many of the epitopes overlap in complex patterns. The antibodies could be grouped into three complementation groups, one of which also included the previously characterized HyHEL -5 which is specific for Arg68 . Complex interactions were observed among the antibodies, both among and within complementation groups, including nonreciprocal competition and enhanced binding. Two of the complementation groups mapped near the catalytic site in a new antigenic region. The antibodies HyHEL -8 and HyHEL -10 had very similar and over-lapping specificities, and may recognize very closely related epitopes. The results suggest that the epitopes may form a continuous antigenic surface, and that antigenic regions correspond to structural domains defined by the tertiary structure of HEL.