Expression and Purification of Glutathione S-Transferase-Tagged HIV-1 gp120: No Evidence of an Interaction with CD26
- Resource Type
- Article
- Authors
- Wang, Yong-Hong; Davies, Anthony H.; Jones, Ian M.
- Source
- Virology; April 1995, Vol. 208 Issue: 1 p142-146, 5p
- Subject
- Language
- ISSN
- 00426822; 10960341
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.