Document 1022
 DOCN  M9541022
 TI    Influence of deletions in N or C terminus of HIV-1 glycoprotein 120 on
       binding of infectivity-enhancing antibody.
 DT    9504
 AU    Lee CN; Robinson J; Cheng YL; Essex M; Lee TH; Department of Cancer
       Biology, Harvard School of Public Health,; Boston, Massachusetts 02115.
 SO    AIDS Res Hum Retroviruses. 1994 Sep;10(9):1065-9. Unique Identifier :
       AIDSLINE MED/95127288
 AB    Human monoclonal antibody 2.3a was previously shown to enhance human
       immunodeficiency virus type 1 (HIV-1) infection in vitro. This enhancing
       antibody recognizes a conserved epitope of envelope glycoprotein gp120.
       We report here that binding of the 2.3a antibody to gp120 is
       significantly affected by deletions of certain N- or C-terminal residues
       of gp120. However, not all such deletions affect the epitope recognized
       by a broadly neutralizing human monoclonal antibody, 1.5e. These
       findings suggest the feasibility of designing a gp120 antigen that is
       free of 2.3a epitope while retaining the conformation of the 1.5e
       epitope.
 DE    Amino Acid Sequence  *Antibodies, Monoclonal  Antigenic
       Determinants/ANALYSIS/CHEMISTRY/IMMUNOLOGY  Base Sequence  Binding
       Sites, Antibody  Human  HIV Envelope Protein
       gp120/BIOSYNTHESIS/CHEMISTRY/*IMMUNOLOGY
       HIV-1/*PHYSIOLOGY/PATHOGENICITY  Molecular Sequence Data  Mutagenesis,
       Site-Directed  Oligodeoxyribonucleotides  Recombinant
       Proteins/BIOSYNTHESIS/CHEMISTRY/IMMUNOLOGY  *Sequence Deletion  Support,
       U.S. Gov't, Non-P.H.S.  Support, U.S. Gov't, P.H.S.  JOURNAL ARTICLE

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