EXPRESSION AND PURIFICATION OF GLUTATHIONE S-TRANSFERASE-TAGGED HIV-1 GP120 - NO EVIDENCE OF AN INTERACTION WITH CD26

被引：30

作者：

WANG, YH ^{[1
]}

DAVIES, AH ^{[1
]}

JONES, IM ^{[1
]}

机构：

[1] NERC,INST VIROL,OXFORD OX1 3SR,ENGLAND

来源：

VIROLOGY | 1995年 / 208卷 / 01期

关键词：

D O I：

10.1006/viro.1995.1137

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

We describe the use of a new baculovirus expression Vector to enable the secretion of the major surface glycoprotein of HIV-1 (gp120) fused to the carboxy-terminus of the widely used affinity tag glutathione S-transferase. The secreted protein can be purified in a single step with the minimum of denaturation on immobilised glutathione and is as active as the parental molecule in binding CD4. We use this molecule in a variety of assay formats to examine the gp120 interaction with CD26, a reported auxiliary molecule in the HIV entry process. We find no evidence of a CD26-gp120 interaction in the absence or presence of CD4. (C) 1995 Academic Press, Inc.

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页码：142 / 146

页数：5

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