scholarly journals Characterization of the binding site for nevirapine (BI-RG-587), a nonnucleoside inhibitor of human immunodeficiency virus type-1 reverse transcriptase

1991 ◽  
Vol 266 (22) ◽  
pp. 14670-14674
Author(s):  
K.A. Cohen ◽  
J. Hopkins ◽  
R.H. Ingraham ◽  
C. Pargellis ◽  
J.C. Wu ◽  
...  
Keyword(s):  
Human Immunodeficiency Virus ◽  
Reverse Transcriptase ◽  
Binding Site ◽  
Human Immunodeficiency Virus Type ◽  
Virus Type ◽  
Immunodeficiency Virus

scholarly journals Human immunodeficiency virus type 1 reverse transcriptase Affinity labeling of the primer binding site

FEBS Letters ◽  
1992 ◽  
Vol 312 (2-3) ◽  
pp. 249-251 ◽  
Author(s):  
R.L. Mitina ◽  
S.V. Doronin ◽  
M.I. Dobrikov ◽  
D.R. Tabatadze ◽  
A.S. Levina ◽  
...  
Keyword(s):  
Human Immunodeficiency Virus ◽  
Reverse Transcriptase ◽  
Binding Site ◽  
Human Immunodeficiency Virus Type ◽  
Virus Type ◽  
Primer Binding Site ◽  
Affinity Labeling ◽  
Immunodeficiency Virus

scholarly journals Identification and Characterization of a Peptide That Specifically Binds the Human, Broadly Neutralizing Anti-Human Immunodeficiency Virus Type 1 Antibody b12

2001 ◽  
Vol 75 (14) ◽  
pp. 6692-6699 ◽  
Author(s):  
Michael B. Zwick ◽  
Lori L. C. Bonnycastle ◽  
Alfredo Menendez ◽  
Melita B. Irving ◽  
Carlos F. Barbas ◽  
...  
Keyword(s):  
Human Immunodeficiency Virus ◽  
Binding Site ◽  
Human Immunodeficiency Virus Type ◽  
Virus Type ◽  
Human Monoclonal Antibody ◽  
Recombinant Polypeptide ◽  
Immunodeficiency Virus ◽  
Hiv 1

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.

scholarly journals Characterization of the Reverse Transcriptase of a Human Immunodeficiency Virus Type 1 Group O Isolate

Virology ◽  
1997 ◽  
Vol 236 (2) ◽  
pp. 364-373 ◽  
Author(s):  
Miguel E. Quiñones-Mateu ◽  
Vicente Soriano ◽  
Esteban Domingo ◽  
Luis Menéndez-Arias
Keyword(s):  
Human Immunodeficiency Virus ◽  
Reverse Transcriptase ◽  
Human Immunodeficiency Virus Type ◽  
Virus Type ◽  
Immunodeficiency Virus
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