Document 0586
 DOCN  M9460586
 TI    Two neutralizing domains in the V3 region in the envelope glycoprotein
       gp125 of HIV type 2.
 DT    9404
 AU    Bjorling E; Chiodi F; Utter G; Norrby E; Department of Virology,
       Karolinska Institute, Stockholm, Sweden.
 SO    J Immunol. 1994 Feb 15;152(4):1952-9. Unique Identifier : AIDSLINE
       MED/94165492
 AB    The purposes of this study were to map the targets for neutralizing Abs
       in the HIV-2 glycoproteins with particular emphasis on the role of the
       V3 region. Sera obtained from guinea pig immunized with peptides
       representing five immunogenic regions of the envelope proteins were used
       in cross-neutralization experiments with nine HIV-2 isolates. Broad
       cross-neutralizing activity was elicited by immunization with two
       peptides representing the central and COOH-terminal portions of the
       HIV-2 V3 loop. Murine mAbs were established from animals immunized with
       two corresponding overlapping peptides. Six mAbs showed neutralizing
       activity against the homologous virus isolate SBL-6669. Peptide
       absorption experiments were performed to define the target regions for
       human neutralizing Abs in the HIV-2 envelope glycoproteins. A
       significant blocking of neutralizing activity of five HIV-2 Ab-positive
       sera was seen in the presence of two peptides corresponding to the V3
       region. Two overlapping deletion sets of peptides, representing amino
       acids Ser311 and Arg337, were used to identify the role of individual
       HIV-2 V3 amino acids in the binding of polyclonal and mAbs. Two distinct
       antigenic sites were identified in this region, the first corresponding
       to a region including the conserved motif Phe-His-Ser (amino acid
       315-317) and the second in proximity of the COOH-terminal cysteine
       Trp-Cys-Arg (amino acid 329-331). Potentially these two sites can
       interact to represent a single discontinuous antigenic site. Taken
       together, these results indicate that V3 is an important neutralizing
       domain of HIV-2.
 DE    Amino Acid Sequence  Animal  Antibodies, Monoclonal/IMMUNOLOGY  Binding
       Sites, Antibody  Gene Products, env/CHEMISTRY/*IMMUNOLOGY  Guinea Pigs
       HIV-2/*IMMUNOLOGY  Immune Sera/IMMUNOLOGY  Mice  Mice, Inbred BALB C
       Molecular Sequence Data  Neutralization Tests  Peptide
       Fragments/IMMUNOLOGY  Protein Precursors/CHEMISTRY/*IMMUNOLOGY  Species
       Specificity  Support, Non-U.S. Gov't  JOURNAL ARTICLE

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