THE N-TERMINAL 31 AMINO-ACIDS OF HUMAN-IMMUNODEFICIENCY-VIRUS TYPE-1 ENVELOPE PROTEIN GP120 CONTAIN A POTENTIAL GP41 CONTACT SITE

被引:46
|
作者
IVEYHOYLE, M [1 ]
CLARK, RK [1 ]
ROSENBERG, M [1 ]
机构
[1] SMITHKLINE BEECHAM PHARMACEUT,DEPT CELL SCI,KING OF PRUSSIA,PA 19406
关键词
D O I
10.1128/JVI.65.5.2682-2685.1991
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
We have compared the expression of full-length gp 160 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.
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页码:2682 / 2685
页数:4
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