Barbacid M, Stephenson J R, Aaronson S A
J Biol Chem. 1976 Aug 25;251(16):4859-66.
Low molecular weight polypeptides of several mammalian type C RNA tumor viruses were purified by sequential ion exchange chromatography and molecular sizing techniques. These included a polypeptide with a molecular weight of 10,000 to 11,000, p 10, from two type C viruses of mouse origin. Rauscher- and Moloney-murine leukemia virus (MuL virus), and from an infectious type C virus isolate of the woolly monkey. The p12 structural polypeptides of these viruses as well as Rauscher-MuL virus p15 were also purified. By using radioimmunoassays developed for each polypeptide, it was possible to demonstrate that all three low molecular weight polypeptides, p15, p12, and p10, were immunologically unique. Among type C viral structural polypeptides, p10 has been least well characterized immunologically. The results of the present study indicate that p10 is virus-coded and possesses strong group-specific antigenic determinants. By use of appropriate immunoassays, broadly reactive interspecies determinants shared by mammalian type C virus isolates of murine, feline, and primate origin, were also demonstrated. The interspecies antigenic determinants of p10 were shown to be as broadly cross-reactive as those exhibited by the major type C virus structural polypeptide, p30.
通过连续离子交换色谱法和分子大小分离技术，纯化了几种哺乳动物C型RNA肿瘤病毒的低分子量多肽。这些多肽包括来自两种小鼠源C型病毒的分子量为10,000至11,000的多肽p10，即劳舍尔鼠白血病病毒和莫洛尼鼠白血病病毒（MuL病毒），以及来自绒毛猴的一种感染性C型病毒分离株。这些病毒的p12结构多肽以及劳舍尔-MuL病毒的p15也被纯化出来。通过使用针对每种多肽开发的放射免疫测定法，能够证明所有三种低分子量多肽p15、p12和p10在免疫学上都是独特的。在C型病毒结构多肽中，p10在免疫学上的特征描述最少。本研究结果表明，p10是病毒编码的，并且具有强的群特异性抗原决定簇。通过使用适当的免疫测定法，还证明了鼠、猫和灵长类动物源的哺乳动物C型病毒分离株共有的广泛反应性种间决定簇。p10的种间抗原决定簇显示出与主要的C型病毒结构多肽p30一样广泛的交叉反应性。
