OLIGOMERIC STRUCTURE OF THE HUMAN IMMUNODEFICIENCY VIRUS TYPE-1 ENVELOPE GLYCOPROTEIN

被引：350

作者：

EARL, PL ^{[1
]}

DOMS, RW ^{[1
]}

MOSS, B ^{[1
]}

机构：

[1] NCI,PATHOL LAB,BETHESDA,MD 20892

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 1990年 / 87卷 / 02期

关键词：

AIDS; retrovirus; vaccinia virus vector;

D O I：

10.1073/pnas.87.2.648

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

The envelope (env) glycoprotein of human immunodeficiency virus type 1 (HIV-1) consists of two noncovalently associated subunits, gp120 and gp41, that are formed by cleavage of a precursor molecule, gp160. Using velocity gradient sedimentation, polyacrylamide gel electrophoresis, and chemical cross-linking, we show that gp160 is synthesized as a monomer and subsequently forms stable homodimers. The molecule remains dimeric after cleavage to gp120/gp41 but is less stable to detergent solubilization and centrifugation. Analysis of wild-type and mutated env proteins indicated that interactions between the ectodomain regions of adjoining gp41 subunits are important for dimer formation and stability. A higher-order oligomeric form was also recovered, probably a tetramer consisting of two noncovalently associated dimers. The proposed subunit composition of the HIV-1 env protein is identical to that previously observed for the paramyxovirus envelope proteins F and HN.

引用

页码：648 / 652

页数：5

共 23 条

[1] MAJOR GLYCOPROTEIN ANTIGENS THAT INDUCE ANTIBODIES IN AIDS PATIENTS ARE ENCODED BY HTLV-III [J].