       Document 0759
 DOCN  M9610759
 TI    Contribution of hypervariable domains to the conformation of a broadly
       neutralizing glycoprotein 120 epitope.
 DT    9601
 AU    Lee CN; Robinson J; Mazzara G; Cheng YL; Essex M; Lee TH; Department of
       Cancer Biology, Harvard School of Public Health,; Boston, Massachusetts
       02115, USA.
 SO    AIDS Res Hum Retroviruses. 1995 Jul;11(7):777-81. Unique Identifier :
       AIDSLINE MED/96053839
 AB    Three of the five hypervariable domains (V1-V3) of human
       immunodeficiency virus type 1 (HIV-1) envelope glycoprotein gp120 have
       previously been shown to be dispensable for antigenic epitopes
       recognized by broadly neutralizing monoclonal antibodies. In this study,
       the influence of the V4 and V5 domains on an epitope recognized by a
       broadly neutralizing human monoclonal antibody, 1.5e, was investigated.
       In contrast with the V1, V2, and V3 domains of gp120, the V4 and V5
       domains were found to be critical for binding to both CD4 and 1.5e. Our
       results suggest that V4 and V5 are in structurally less flexible regions
       of gp120 than V1, V2, and V3 and raises the question of whether variable
       domains V4 and V5 are also indispensable for other broadly neutralizing
       antibodies in the same class as 1.5e.
 DE    Antibodies, Monoclonal  Antigens, CD/IMMUNOLOGY  Antigens,
       CD4/IMMUNOLOGY  Base Sequence  Binding Sites, Antibody
       Epitopes/*CHEMISTRY  Human  HIV Envelope Protein
       gp120/*CHEMISTRY/*GENETICS/IMMUNOLOGY  HIV-1/GENETICS/*IMMUNOLOGY
       Molecular Sequence Data  Mutagenesis, Site-Directed  Neutralization
       Tests  Oligodeoxyribonucleotides  *Protein Conformation  Recombinant
       Proteins/CHEMISTRY/IMMUNOLOGY  Sequence Deletion  Support, U.S. Gov't,
       Non-P.H.S.  Support, U.S. Gov't, P.H.S.  *Variation (Genetics)  JOURNAL
       ARTICLE

       SOURCE: National Library of Medicine.  NOTICE: This material may be
       protected by Copyright Law (Title 17, U.S.Code).

