Temporal expression of HIV-1 envelope proteins in baculovirus-infected insect cells: Implications for glycosylation and CD4 binding

1990 ◽  
Vol 7 (6) ◽  
pp. 160-171 ◽  
Author(s):  
Cheryl Isaac Murphy ◽  
Michael Lennick ◽  
Sophie M Lehar ◽  
Gerald A Beltz ◽  
Elihu Young
2014 ◽  
Vol 99 ◽  
pp. 87-93 ◽  
Author(s):  
Bingqing Liu ◽  
Ruiqin Wang ◽  
Fang Wu ◽  
Xiaodong Xu ◽  
Hongying Chen

Cell ◽  
1989 ◽  
Vol 59 (1) ◽  
pp. 103-112 ◽  
Author(s):  
Dirk Gheysen ◽  
Eric Jacobs ◽  
Françoise de Foresta ◽  
Clotilde Thiriart ◽  
Myriam Francotte ◽  
...  

2014 ◽  
Vol 30 (S1) ◽  
pp. A152-A152
Author(s):  
Yanli Chen ◽  
Yuanyuan Hu ◽  
Zhenpeng Li ◽  
Li Ren ◽  
Liying Ma ◽  
...  

1992 ◽  
Vol 286 (3) ◽  
pp. 677-680 ◽  
Author(s):  
J D Robishaw ◽  
V K Kalman ◽  
K L Proulx

As a result of the inability to resolve the heterogeneous mixture of G protein beta gamma subunits present in tissues, it has not been possible to compare different beta gamma subunits of the G proteins in terms of their proposed roles in receptor-effector coupling. This study was undertaken to establish the utility of the baculovirus expression system in producing homogeneous beta gamma subunits of defined composition for the comparative analysis of these subunits in reconstitution systems. In this study we report the expression, and appropriate post-translational processing, of recombinant beta 2, gamma 2 and gamma 3 subunits. In addition, we show that the recombinant beta gamma subunits can be readily purified, and can functionally interact with the alpha subunits of the G proteins.


1994 ◽  
Vol 14 (2) ◽  
pp. 99-117 ◽  
Author(s):  
J. A. Javitch ◽  
J. Kaback ◽  
X. Li ◽  
A. Karlin
Keyword(s):  

Immunobiology ◽  
1992 ◽  
Vol 186 (3-4) ◽  
pp. 254-267 ◽  
Author(s):  
Jörg Kupsch ◽  
Kai M. Saizawa ◽  
Klaus Eichmann

Blood ◽  
2000 ◽  
Vol 96 (4) ◽  
pp. 1438-1442 ◽  
Author(s):  
Christina K. Ullrich ◽  
Jerome E. Groopman ◽  
Ramesh K. Ganju

The immune dysfunction and cell destruction that occur in the human immunodeficiency virus (HIV)-infected host appear to result from the direct cytopathic effects of viral infection and the effects of viral proteins on uninfected bystander cells. Recently, the α-chemokine receptor CXCR4 has been reported to mediate apoptosis in neuronal cells and in CD4+ and CD8+ T cells after its binding to HIV-1 envelope proteins. In the current study, it was observed that human umbilical vein endothelial cells (HUVEC) undergo apoptosis after their treatment with the HIV-1 envelope proteins gp120/160. Anti-CXCR4 monoclonal antibody decreased HIV-1 gp120/160-induced apoptosis, suggesting that the CXCR4 chemokine receptor mediates the apoptotic effects of these HIV envelope glycoproteins. Further studies revealed that caspases play an important role in this process because the pretreatment of cells with a general caspase enzyme inhibitor decreased the extent of HUVEC apoptosis induced by gp120/160. In addition, it was found that caspase-3 was activated on HIV-1 gp120/160 treatment of these cells. It was also observed that gp120/160 treatment slightly increased the expression of the pro-apoptotic molecule Bax. These results suggest that HIV-1 envelope glycoproteins can disrupt endothelial integrity through the interaction with CXCR4, thereby facilitating virus transit out of the bloodstream and contributing to the vascular injury syndromes seen in acquired immunodeficiency syndrome.


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