Chen S S
Institute of Biomedical Sciences, Academia Sinica, Taipei, Taiwan, ROC.
Intervirology. 1996;39(4):242-8. doi: 10.1159/000150524.
The human immunodeficiency virus type 1 (HIV-1) envelope glycoprotein was expressed by a vaccinia vector that encodes the late promotor P11. The envelope protein synthesized mediated syncytia formation with SupT1 cells and was efficiently cleaved to produce mature gp120 and gp41 in CV-1 cells. gp 160 precursor processing was neither affected by a change in culture medium nor by a heterologous vesicular stomatitis virus coinfection. These results suggest that the proteolytic cleavage of gp160 is an efficient process and that coinfection with other viruses may not affect precursor processing of the HIV-1 Env protein.
1型人类免疫缺陷病毒（HIV-1）包膜糖蛋白由编码晚期启动子P11的痘苗载体表达。合成的包膜蛋白介导与SupT1细胞形成合胞体，并在CV-1细胞中被有效切割以产生成熟的gp120和gp41。gp160前体的加工既不受培养基变化的影响，也不受异源水疱性口炎病毒共感染的影响。这些结果表明，gp160的蛋白水解切割是一个高效的过程，与其他病毒的共感染可能不会影响HIV-1 Env蛋白前体的加工。
