Sen S, Houghten R A, Sherr C J, Sen A
Proc Natl Acad Sci U S A. 1983 Mar;80(5):1246-50. doi: 10.1073/pnas.80.5.1246.
Oligopeptides predicted from the nucleotide sequence of the oncogene v-fes of feline sarcoma virus (FeSV) were synthesized chemically and used to generate specific antibodies. Antisera against a 12-amino-acid-long oligopeptide (12-mer) located 42 residues from the carboxyl terminus of the v-fes coding sequence efficiently recognized the transforming proteins encoded by Snyder-Theilen (ST) and Gardner-Arnstein (GA) strains of FeSV. This 12-mer also contains 10 amino acid residues homologous in order and position to those predicted from the nucleotide sequence of the oncogene v-fps of avian Fujinami sarcoma virus (FSV). The anti-12-mer immunoprecipitated the FSV-specific transforming protein molecules from FSV-transformed cells. Binding of these antipeptide antibody molecules to the v-fes and the v-fps gene products inhibited their associated tyrosine-specific protein kinase (EC 2.7.1.37) activities. The ability to generate such site-specific antisera to the products of related oncogenes will be valuable in the molecular characterization of retroviral transforming proteins and their normal cellular homologs.
化学合成了从猫肉瘤病毒（FeSV）致癌基因v-fes的核苷酸序列预测的寡肽，并用于产生特异性抗体。针对位于v-fes编码序列羧基末端42个残基处的一个12个氨基酸长的寡肽（12聚体）的抗血清，有效地识别了由FeSV的斯奈德-泰伦（ST）和加德纳-阿恩斯坦（GA）毒株编码的转化蛋白。这个12聚体还包含10个氨基酸残基，其顺序和位置与从禽 Fujinami 肉瘤病毒（FSV）致癌基因v-fps的核苷酸序列预测的氨基酸残基同源。抗12聚体抗体从FSV转化细胞中免疫沉淀出FSV特异性转化蛋白分子。这些抗肽抗体分子与v-fes和v-fps基因产物的结合抑制了它们相关的酪氨酸特异性蛋白激酶（EC 2.7.1.37）活性。产生针对相关致癌基因产物的这种位点特异性抗血清的能力，在逆转录病毒转化蛋白及其正常细胞同源物的分子特征研究中将具有重要价值。
