Document 0001
 DOCN  M9580001
 TI    Inhibition of anti-V3 domain antibody binding to human immunodeficiency
       virus type-1-infected cells by sulfated polysaccharides.
 DT    9506
 AU    Okada T; Patterson BK; Gurney ME; Department of Cell, Molecular, and
       Structural Biology,; Northwestern University Medical School, Chicago, IL
       60611, USA.
 SO    Biochem Biophys Res Commun. 1995 Apr 26;209(3):850-8. Unique Identifier
       : AIDSLINE MED/95251713
 AB    The third variable domain (V3 domain) of the human immunodeficiency
       virus type 1 (HIV-1) envelope glycoprotein gp120 is an immunodominant
       region. Anti-V3 domain antibodies neutralize both HIV-1 infection and
       syncytium formation. The V3 domain has a high density of positive charge
       which is a potential binding site for anti-HIV-1 sulfated
       polysaccharides. To investigate the inhibitory effect of sulfated
       polysaccharides on the binding of anti-V3 domain antibody,
       fluorescence-activating cell sorting analysis was performed using two
       kinds of antibodies, NEA9284 (purified, 0.25 micrograms/ml) and 0.5 beta
       (ascite, 2.0 mg/ml), and HIV-1-infected CEM cells. When the binding
       assay with a 1:100 dilution of each antibody was performed in the
       presence of dextran sulfate, heparin, and inositol hexasulfate at
       concentrations which are antiviral, the compounds did not inhibit the
       binding of either antibody. As the antibody concentration was decreased
       with higher dilution, dextran sulfate was able to reduce antibody
       binding by 50-60%. Thus, antagonism of anti-V3 domain antibody binding
       by sulfated polysaccharides is not as extensive as reported previously
       by several groups.
 DE    Amino Acid Sequence  Antibodies/METABOLISM  Binding Sites, Antibody/DRUG
       EFFECTS  Cell Line  Chondroitin Sulfates/*PHARMACOLOGY  Dextran
       Sulfate/*PHARMACOLOGY  Dextrans/PHARMACOLOGY  Heparin/PHARMACOLOGY
       Human  HIV Envelope Protein gp120/CHEMISTRY/IMMUNOLOGY/*METABOLISM
       HIV-1/*PHYSIOLOGY  Inositol/PHARMACOLOGY  Molecular Sequence Data
       Mutagenesis, Site-Directed  Phytic Acid/PHARMACOLOGY  Point Mutation
       Recombinant Proteins/CHEMISTRY/IMMUNOLOGY/METABOLISM  Support, Non-U.S.
       Gov't  Support, U.S. Gov't, P.H.S.  Transfection  Tumor Cells, Cultured
       JOURNAL ARTICLE

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