DISSOCIATION OF GP120 FROM HIV-1 VIRIONS INDUCED BY SOLUBLE CD4

被引：559

作者：

MOORE, JP ^{[1
]}

MCKEATING, JA ^{[1
]}

WEISS, RA ^{[1
]}

SATTENTAU, QJ ^{[1
]}

机构：

[1] COLUMBIA UNIV COLL PHYS & SURG, HOWARD HUGHES MED INST, NEW YORK, NY 10032 USA

来源：

SCIENCE | 1990年 / 250卷 / 4984期

关键词：

D O I：

10.1126/science.2251501

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 CD4 antigen is the high affinity cellular receptor for the human immunodeficiency virus type-1 (HIV-1). Binding of recombinant soluble CD4 (sCD4) or the purified V1 domain of sCD4 to the surface glycoprotein gp120 on virions resulted in rapid dissociation of gp120 from its complex with the transmembrane glycoprotein gp41. This may represent the initial stage in virus-cell and cell-cell fusion. Shedding of gp120 from virions induced by sCD4 may also contribute to the mechanism by which these soluble receptor molecules neutralize HIV-1.

引用

页码：1139 / 1142

页数：4