Ivey-Hoyle M, Clark R K, Rosenberg M
Department of Gene Expression Sciences, SmithKline Beecham Pharmaceuticals, King of Prussia, Pennsylvania 19406.
J Virol. 1991 May;65(5):2682-5. doi: 10.1128/JVI.65.5.2682-2685.1991.
We have compared the expression of full-length gp160 envelope protein from human immunodeficiency virus type 1 with that of a deletion mutant lacking the N-terminal 31 amino acids of the mature protein (gp160 delta 32). The gp160 and gp160 delta 32 proteins are processed to yield gp41 and gp120 or gp120 delta 32, respectively. In contrast to full-length gp120, gp120 delta 32 failed to associate with gp41 at the cell surface, despite conformational integrity as judged by soluble CD4 binding. Thus, the N-terminal 31 amino acids of gp120, which contain hyperconserved sequences, are likely involved in forming a contact site for gp41.
我们比较了1型人类免疫缺陷病毒全长gp160包膜蛋白与缺失成熟蛋白N端31个氨基酸的缺失突变体（gp160 delta 32）的表达情况。gp160和gp160 delta 32蛋白分别被加工产生gp41和gp120或gp120 delta 32。与全长gp120不同，尽管通过可溶性CD4结合判断其构象完整，但gp120 delta 32在细胞表面未能与gp41结合。因此，gp120的N端31个氨基酸（包含高度保守序列）可能参与形成与gp41的接触位点。
