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M9610759.TXT
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1996-01-30
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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).