Racevskis J, Koch G
J Virol. 1977 Jan;21(1):328-37. doi: 10.1128/JVI.21.1.328-337.1977.
Viral protein synthesis was studied in two Friend virus-induced erythroleukemia cell lines (Ostertag cell lines FSD1-F4 and B8) by the technique of immuno-precipitation with monospecific antisera to the major envelope glycoprotein gp70 and major core protein p30. One of the cell lines (F4) releases active Friend virus complex to the growth medium, where release of virus from the other cell line (B8) is barely or nondetectable. It was found that in the nonproducer cell line B8, a large-molecular-weight protein of about 65,000 containing p30 antigenic determinants is synthesized, yet no p30 is produced upon prolonged incubation and chase, suggesting that this might be the actual lesion that prevents mature virus production by these cells. In both cell lines, the predominant protein species that is immunoprecipitated with monospecific anti-gp70 serum is a protein of 55,000 to 60,000 daltons that is labeled with glucosamine to a much lesser extent that gp70 and appears to become heterogeneous with time. Large amounts of gp70 can be detected in the cell-free medium, but none of the unstable species of 55,00 to 60,000 molecular weight.
通过使用针对主要包膜糖蛋白gp70和主要核心蛋白p30的单特异性抗血清进行免疫沉淀技术,在两种弗氏病毒诱导的红白血病细胞系(奥斯特塔格细胞系FSD1 - F4和B8)中研究了病毒蛋白合成。其中一个细胞系(F4)向生长培养基中释放活性弗氏病毒复合物,而另一个细胞系(B8)几乎不释放或无法检测到病毒释放。研究发现,在非生产性细胞系B8中,合成了一种含有p30抗原决定簇的约65,000的大分子蛋白,但长时间孵育和追踪后未产生p30,这表明这可能是阻止这些细胞产生成熟病毒的实际损伤。在这两种细胞系中,用单特异性抗gp70血清免疫沉淀的主要蛋白种类是一种55,000至60,000道尔顿的蛋白,其被葡糖胺标记的程度远低于gp70,并且似乎随时间变得异质性。在无细胞培养基中可检测到大量的gp70,但未检测到分子量为55,000至60,000的不稳定种类。