Ingman-Baker J, Hinze E, Levy J G, Pawson T
J Virol. 1984 May;50(2):572-8. doi: 10.1128/JVI.50.2.572-578.1984.
Two monoclonal antibodies have been obtained that recognize antigenic determinants within the C-terminal fps-encoded region of P140gag-fps, the transforming protein of Fujinami avian sarcoma virus (FSV). The hybridomas which secrete these antibodies (termed 88AG and p26C) were isolated after the fusion of NS-1 mouse myeloma cells with B lymphocytes from Fischer rats that had been immunized with FSV-transformed rat-1 cells. FSV P140gag-fps immunoprecipitated by either antibody is active as a tyrosine-specific kinase and is able to autophosphorylate and to phosphorylate enolase in vitro. The fps-encoded proteins of all FSV variants, including the gag- p91fps protein of F36 virus, are recognized by both monoclonal antibodies. However, the product of the avian cellular c-fps gene. NCP98, and the transforming proteins of the recently isolated fps-containing avian sarcoma viruses 16L and UR1 are recognized only by the p26C antibody. The 88AG antibody therefore defines an epitope specific for FSV fps, whereas the epitope for p26C is conserved between cellular and viral fps proteins. The P105gag-fps protein of the PRCII virus is not precipitated by p26C (nor by 88AG), presumably as a consequence of the deletion of N-terminal fps sequences. These data indicate that the fps-encoded peptide sequences of 16L P142gag-fps and UR1 P150gag-fps are more closely related to NCP98 than that of FSV P140gag-fps. This supports the view that 16L and UR1 viruses represent recent retroviral acquisitions of the c-fps oncogene. The P85gag-fes transforming protein of Snyder-Theilen feline sarcoma virus is not precipitated by either monoclonal antibody but is recognized by some antisera from FSV tumor-bearing rats, demonstrating that fps-specific antigenic determinants are conserved in fes-encoded proteins.
已获得两种单克隆抗体，它们可识别 Fujinami 禽肉瘤病毒（FSV）的转化蛋白 P140gag-fps 的 C 末端 fps 编码区域内的抗原决定簇。分泌这些抗体的杂交瘤（称为 88AG 和 p26C）是在 NS-1 小鼠骨髓瘤细胞与用 FSV 转化的大鼠-1 细胞免疫的 Fischer 大鼠的 B 淋巴细胞融合后分离得到的。用任何一种抗体免疫沉淀的 FSV P140gag-fps 作为酪氨酸特异性激酶具有活性，并且能够在体外自磷酸化并磷酸化烯醇化酶。所有 FSV 变体的 fps 编码蛋白，包括 F36 病毒的 gag-p91fps 蛋白，都能被这两种单克隆抗体识别。然而，禽细胞 c-fps 基因的产物 NCP98，以及最近分离的含 fps 的禽肉瘤病毒 16L 和 UR1 的转化蛋白，仅被 p26C 抗体识别。因此，88AG 抗体定义了一个 FSV fps 特有的表位，而 p26C 的表位在细胞和病毒 fps 蛋白之间是保守的。PRCII 病毒的 P105gag-fps 蛋白不能被 p26C（也不能被 88AG）沉淀，推测这是由于 N 末端 fps 序列缺失的结果。这些数据表明，16L P142gag-fps 和 UR1 P150gag-fps 的 fps 编码肽序列与 NCP98 的关系比与 FSV P140gag-fps 的关系更密切。这支持了 16L 和 UR1 病毒代表最近逆转录病毒获得 c-fps 癌基因的观点。Snyder-Theilen 猫肉瘤病毒的 P85gag-fes 转化蛋白不能被任何一种单克隆抗体沉淀，但能被一些来自 FSV 荷瘤大鼠的抗血清识别，表明 fps 特异性抗原决定簇在 fes 编码蛋白中是保守的。
