TOPOLOGICAL MAPPING OF MURINE LEUKEMIA-VIRUS PROTEINS BY COMPETITION-BINDING ASSAYS WITH MONOCLONAL-ANTIBODIES
TOPOLOGICAL MAPPING OF MURINE LEUKEMIA-VIRUS PROTEINS BY COMPETITION-BINDING ASSAYS WITH MONOCLONAL-ANTIBODIES
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DOI：
10.1016/0042-6822(80)90528-0
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发表时间：
1980-01-01
期刊：
影响因子：
3.7
通讯作者：
NOWINSKI, RC
中科院分区：
文献类型：
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作者：
STONE, MR;NOWINSKI, RC
由培养的杂交细胞[小鼠]产生的单克隆抗体是化学上均质的试剂，其以恒定的亲合力与单一抗原决定簇（表位）反应。这些抗体对于复杂抗原蛋白的小区域是非常特异的探针。用一组单克隆抗体进行竞争结合试验，研究AKR白血病病毒包膜蛋白上6个表位的排列。如果单个蛋白质上的2个表位彼此相邻，则抗体与1个表位的结合将在空间上阻碍抗体与另一个表位的结合。如果2个表位位于蛋白质上的较远位点，则抗体与1个表位的结合不会影响抗体与另一个表位的结合。竞争结合试验的结果表明，在gp 70和p15（E）包膜蛋白上存在2个不同的抗原位点。对于gp 70蛋白，1个抗原位点含有gp 70 b和gp 70 c表位;该蛋白上的另一个抗原位点含有gp 70 a表位。对于p15（E），1个抗原位点含有p15（E）B和p15（E）c表位;另一个位点含有p15（E）a表位。证明了这种类型的血清学分析用于研究单个病毒蛋白质的三级结构的效用。
Monoclonal antibodies produced by hybrid cells [mouse] in culture are chemically homogeneous reagents that react with constant avidity to single antigenic determinants (epitopes). These antibodies are remarkably specific probes for small regions of complex antigenic proteins. A panel of monoclonal antibodies was used in competition binding assays to investigate the arrangement of 6 epitopes on the envelope proteins of AKR leukemia virus. If 2 epitopes were adjacent to each other on a single protein, the binding of antibody to 1 epitope would sterically hinder the binding of antibody to the other epitope. If the 2 epitopes were at distant sites on the protein, the binding of antibody to 1 epitope would not influence the binding of antibody to the other epiptope. The results of the competition binding assays demonstrated the presence of 2 distinct antigen sites on the gp70 and p15(E) envelope proteins. With the gp70 protein, 1 antigen site contained the gp70b and gp70c epitopes; the other antigen site on this protein contained the gp70a epitope. With p15(E), 1 antigen site contained the p15(E)b and p15(E)c epitopes; the other site contained the p15(E)a epitope. The utility of this type of serological analysis for the study of the tertiary structure of individual viral proteins was demonstrated.