scholarly journals Fusion proteins of HIV-1 envelope glycoprotein gp120 with CD4-induced antibodies showed enhanced binding to CD4 and CD4 binding site antibodies

2012 ◽  
Vol 425 (4) ◽  
pp. 931-937 ◽  
Author(s):  
Weizao Chen ◽  
Yang Feng ◽  
Yanping Wang ◽  
Zhongyu Zhu ◽  
Dimiter S. Dimitrov
Virology ◽  
2008 ◽  
Vol 372 (2) ◽  
pp. 409-420 ◽  
Author(s):  
Maria Luisa Visciano ◽  
Michael Tuen ◽  
Miroslaw K. Gorny ◽  
Catarina E. Hioe

2005 ◽  
Vol 280 (22) ◽  
pp. 21353-21357 ◽  
Author(s):  
Romain R. Vivès ◽  
Anne Imberty ◽  
Quentin J. Sattentau ◽  
Hugues Lortat-Jacob

Virology ◽  
2008 ◽  
Vol 377 (2) ◽  
pp. 330-338 ◽  
Author(s):  
Ira Berkower ◽  
Chiraag Patel ◽  
Yisheng Ni ◽  
Konstantin Virnik ◽  
Zhexin Xiang ◽  
...  

2012 ◽  
Vol 8 ◽  
pp. 1858-1866 ◽  
Author(s):  
Julia Meier ◽  
Kristin Kassler ◽  
Heinrich Sticht ◽  
Jutta Eichler

Based on the structure of the HIV-1 glycoprotein gp120 in complex with its cellular receptor CD4, we have designed and synthesized peptides that mimic the binding site of CD4 for gp120. The ability of these peptides to bind to gp120 can be strongly enhanced by increasing their conformational stability through cyclization, as evidenced by binding assays, as well as through molecular-dynamics simulations of peptide–gp120 complexes. The specificity of the peptide–gp120 interaction was demonstrated by using peptide variants, in which key residues for the interaction with gp120 were replaced by alanine or D-amino acids.


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