Parsons S J, Wilson L D, Ely C M, Parsons J T, Benjamin D C
Hybridoma. 1984;3(1):25-31. doi: 10.1089/hyb.1984.3.25.
The major component of the core structure of avian sarcoma leukosis viruses is a 27 kD molecular weight polypeptide, p27. Spleen cells from mice immunized with the Schmidt-Ruppin strain of Rous sarcoma virus (RSV) were fused with mouse myeloma cells (SP2/0), and hybridoma cell lines producing monoclonal antibodies to p27 were isolated. The monoclonal antibodies were all of the IgG1 subclass with kappa light chains. These antibodies immunoprecipitated p27 and its precursor proteins from extracts of RSV-transformed cells. Reciprocal competitive binding experiments defined five nonoverlapping antigenic determinants within p27. The monoclonal antibodies also immunoprecipitated the transforming protein, p110gag-myc, from avian myelocytomatosis virus transformed cells. Their usefulness in studies of virion maturation and viral oncogenesis is discussed.
禽肉瘤白血病病毒核心结构的主要成分是一种分子量为27kD的多肽，即p27。用劳氏肉瘤病毒（RSV）的施密特-鲁平株免疫的小鼠脾细胞与小鼠骨髓瘤细胞（SP2/0）融合，分离出产生针对p27的单克隆抗体的杂交瘤细胞系。这些单克隆抗体均为带有κ轻链的IgG1亚类。这些抗体从RSV转化细胞的提取物中免疫沉淀p27及其前体蛋白。相互竞争结合实验确定了p27内五个不重叠的抗原决定簇。这些单克隆抗体还从禽骨髓细胞瘤病毒转化细胞中免疫沉淀转化蛋白p110gag-myc。讨论了它们在病毒粒子成熟和病毒肿瘤发生研究中的用途。
