Famulari N G, Buchhagen D L, Klenk H D, Fleissner E
J Virol. 1976 Nov;20(2):501-8. doi: 10.1128/JVI.20.2.501-508.1976.
The murine leukemia virus envelope proteins, p15(E) and gp70, exhibit a mode of processing distinct from that of virion core proteins according to three criteria. First, the incorporation of both p15(E) and gp70 into virions is more sensitive to the metabolic analogue 2-deoxy-D-glucose than the incorporation of core proteins. Second, the kinetics with which the newly synthesized envelope proteins appear in the released virions is delayed relative to the appearance of core proteins. Third, immunoprecipitation of large polypeptides from infected cells reveals the presence of gp70 and p15(E) in a common precursor distinct from the core polyprotein.
根据三个标准,鼠白血病病毒包膜蛋白p15(E)和gp70呈现出一种与病毒粒子核心蛋白不同的加工方式。首先,与核心蛋白的掺入相比,p15(E)和gp70两者掺入病毒粒子的过程对代谢类似物2-脱氧-D-葡萄糖更为敏感。其次,新合成的包膜蛋白出现在释放的病毒粒子中的动力学相对于核心蛋白的出现有所延迟。第三,对感染细胞中大多肽进行免疫沉淀显示,gp70和p15(E)存在于一种不同于核心多蛋白的共同前体中。