Characterization of multiple molecular interactions between human cytomegalovirus (HCMV) and human immunodeficiency virus type 1 (HIV-1)

Virology ◽  
1990 ◽  
Vol 176 (1) ◽  
pp. 87-97 ◽  
Author(s):  
Robert F. Rando ◽  
Alagarsamy Srinivasan ◽  
Jennifer Feingold ◽  
Eva Gonczol ◽  
Stanley Plotkin
2000 ◽  
Vol 11 (1) ◽  
pp. 23-29 ◽  
Author(s):  
Ze-Qi Xu ◽  
Earl R Kern ◽  
Louise Westbrook ◽  
Lois B Allen ◽  
Robert W Buckheit ◽  
...  

Plant-derived and semi-synthetic calanolide compounds with anti-human immunodeficiency virus type 1 (HIV-1) activity were tested for anti-human cytomegalovirus (HCMV) activity in both cytopathic effect inhibition and plaque reduction assays. The results indicated that the anti-HCMV activity of calanolide compounds does not correlate with their activity against HIV-1. The semi-synthetic 12-keto derivatives tended to be more active against HCMV than the corresponding 12-OH congeners, which were more active against HIV-1. It appeared that the 7,8-unsaturated double bond in the chromene ring played a certain role in maintaining activities against both HCMV and HIV-1. Saturation of the double bond increased the EC50 values against both viruses, with concomitant increase in toxicity. The calanolide compounds reported here are the first non-nucleoside analogues capable of inhibiting both HIV-1 and HCMV and, therefore, may be useful chemoprophylactic agents for HCMV in HIV-infected people or vice versa.


2001 ◽  
Vol 75 (14) ◽  
pp. 6692-6699 ◽  
Author(s):  
Michael B. Zwick ◽  
Lori L. C. Bonnycastle ◽  
Alfredo Menendez ◽  
Melita B. Irving ◽  
Carlos F. Barbas ◽  
...  

ABSTRACT Human monoclonal antibody (MAb) b12 recognizes a conformational epitope that overlaps the CD-4-binding site of the human immunodeficiency virus type 1 (HIV-1) envelope. MAb b12 neutralizes a broad range of HIV-1 primary isolates and protects against primary virus challenge in animal models. We report here the discovery and characterization of B2.1, a peptide that binds specifically to MAb b12. B2.1 was selected from a phage-displayed peptide library by using immunoglobulin G1 b12 as the selecting agent. The peptide is a homodimer whose activity depends on an intact disulfide bridge joining its polypeptide chains. Competition studies with gp120 indicate that B2.1 occupies the b12 antigen-binding site. The affinity of b12 for B2.1 depends on the form in which the peptide is presented; b12 binds best to the homodimer as a recombinant polypeptide fused to the phage coat. Originally, b12 was isolated from a phage-displayed Fab library constructed from the bone marrow of an HIV-1-infected donor. The B2.1 peptide is highly specific for b12 since it selected only phage bearing b12 Fab from this large and diverse antibody library.


2004 ◽  
Vol 30 (3) ◽  
pp. 224-228 ◽  
Author(s):  
Chunfu Yang ◽  
Ming Li ◽  
Faye Cowart ◽  
Donna Rudolph ◽  
Bharat Parekh ◽  
...  

1990 ◽  
Vol 616 (1 AIDS) ◽  
pp. 54-63 ◽  
Author(s):  
PETER A. BARRY ◽  
ELISSA PRATT-LOWE ◽  
DONALD J. ALCENDOR ◽  
RONALD E. UNGER ◽  
PAUL A. LUCIW

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