Human anti-V2 monoclonal antibody that neutralizes primary but not laboratory isolates of human immunodeficiency virus type 1. 1994

M K Gorny, and J P Moore, and A J Conley, and S Karwowska, and J Sodroski, and C Williams, and S Burda, and L J Boots, and S Zolla-Pazner
New York University Medical Center, New York.

A human immunoglobulin G1 lambda monoclonal antibody (MAb), 697-D, was developed that recognizes the V2 region of human immunodeficiency virus type 1 (HIV-1) gp120. Substitutions at amino acid positions 176/177, 179/180, 183/184, and 192 to 194 in the V2 loop of gp120 each completely abolished the binding capacity of 697-D in an enzyme-linked immunosorbent assay format. Competition analysis with three different neutralizing murine anti-V2 MAbs confirmed the specificity of 697-D. The 697-D epitope is primarily conformation dependent, although there was weak reactivity of the MAb with a V2 peptide spanning residues 161 to 180. Treatment of recombinant gp120 HIVIIIB with sodium metaperiodate, which oxidizes carbohydrates, abolished the binding of the MAb, showing the dependence of the epitope on intact carbohydrates. The broad reactivity of 697-D was displayed by its binding to the gp120 molecules from four of four laboratory isolates and five of five primary isolates. The MAb 697-D neutralized three out of four primary isolates but failed to neutralize any of four laboratory strains of HIV-1. 697-D and a human anti-V3 MAb, 447-52-D, displayed similar potency in neutralizing primary isolates, indicating that the V2 region of gp120, like the V3 region and the CD4-binding domain, can induce potent neutralizing antibodies against HIV-1 in humans.

UI MeSH Term Description Entries
D007074 Immunoglobulin G The major immunoglobulin isotype class in normal human serum. There are several isotype subclasses of IgG, for example, IgG1, IgG2A, and IgG2B. Gamma Globulin, 7S,IgG,IgG Antibody,Allerglobuline,IgG(T),IgG1,IgG2,IgG2A,IgG2B,IgG3,IgG4,Immunoglobulin GT,Polyglobin,7S Gamma Globulin,Antibody, IgG,GT, Immunoglobulin
D008969 Molecular Sequence Data Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories. Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D009500 Neutralization Tests The measurement of infection-blocking titer of ANTISERA by testing a series of dilutions for a given virus-antiserum interaction end-point, which is generally the dilution at which tissue cultures inoculated with the serum-virus mixtures demonstrate cytopathology (CPE) or the dilution at which 50% of test animals injected with serum-virus mixtures show infectivity (ID50) or die (LD50). Neutralization Test,Test, Neutralization,Tests, Neutralization
D010504 Periodic Acid A strong oxidizing agent. Paraperiodic Acid,Periodic Acid (HIO4),Periodic Acids,Acid, Paraperiodic,Acid, Periodic,Acids, Periodic
D011994 Recombinant Proteins Proteins prepared by recombinant DNA technology. Biosynthetic Protein,Biosynthetic Proteins,DNA Recombinant Proteins,Recombinant Protein,Proteins, Biosynthetic,Proteins, Recombinant DNA,DNA Proteins, Recombinant,Protein, Biosynthetic,Protein, Recombinant,Proteins, DNA Recombinant,Proteins, Recombinant,Recombinant DNA Proteins,Recombinant Proteins, DNA
D004797 Enzyme-Linked Immunosorbent Assay An immunoassay utilizing an antibody labeled with an enzyme marker such as horseradish peroxidase. While either the enzyme or the antibody is bound to an immunosorbent substrate, they both retain their biologic activity; the change in enzyme activity as a result of the enzyme-antibody-antigen reaction is proportional to the concentration of the antigen and can be measured spectrophotometrically or with the naked eye. Many variations of the method have been developed. ELISA,Assay, Enzyme-Linked Immunosorbent,Assays, Enzyme-Linked Immunosorbent,Enzyme Linked Immunosorbent Assay,Enzyme-Linked Immunosorbent Assays,Immunosorbent Assay, Enzyme-Linked,Immunosorbent Assays, Enzyme-Linked
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000595 Amino Acid Sequence The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION. Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein
D000911 Antibodies, Monoclonal Antibodies produced by a single clone of cells. Monoclonal Antibodies,Monoclonal Antibody,Antibody, Monoclonal
D000918 Antibody Specificity The property of antibodies which enables them to react with some ANTIGENIC DETERMINANTS and not with others. Specificity is dependent on chemical composition, physical forces, and molecular structure at the binding site. Antibody Specificities,Specificities, Antibody,Specificity, Antibody

Related Publications

M K Gorny, and J P Moore, and A J Conley, and S Karwowska, and J Sodroski, and C Williams, and S Burda, and L J Boots, and S Zolla-Pazner
May 1997, AIDS research and human retroviruses,
M K Gorny, and J P Moore, and A J Conley, and S Karwowska, and J Sodroski, and C Williams, and S Burda, and L J Boots, and S Zolla-Pazner
November 1994, Journal of virology,
M K Gorny, and J P Moore, and A J Conley, and S Karwowska, and J Sodroski, and C Williams, and S Burda, and L J Boots, and S Zolla-Pazner
June 1998, The Journal of infectious diseases,
M K Gorny, and J P Moore, and A J Conley, and S Karwowska, and J Sodroski, and C Williams, and S Burda, and L J Boots, and S Zolla-Pazner
December 1998, Journal of virology,
M K Gorny, and J P Moore, and A J Conley, and S Karwowska, and J Sodroski, and C Williams, and S Burda, and L J Boots, and S Zolla-Pazner
April 1994, Proceedings of the National Academy of Sciences of the United States of America,
M K Gorny, and J P Moore, and A J Conley, and S Karwowska, and J Sodroski, and C Williams, and S Burda, and L J Boots, and S Zolla-Pazner
March 2004, Antiviral research,
M K Gorny, and J P Moore, and A J Conley, and S Karwowska, and J Sodroski, and C Williams, and S Burda, and L J Boots, and S Zolla-Pazner
November 1990, Proceedings of the National Academy of Sciences of the United States of America,
M K Gorny, and J P Moore, and A J Conley, and S Karwowska, and J Sodroski, and C Williams, and S Burda, and L J Boots, and S Zolla-Pazner
February 1994, Journal of virology,
M K Gorny, and J P Moore, and A J Conley, and S Karwowska, and J Sodroski, and C Williams, and S Burda, and L J Boots, and S Zolla-Pazner
January 1992, AIDS (London, England),
M K Gorny, and J P Moore, and A J Conley, and S Karwowska, and J Sodroski, and C Williams, and S Burda, and L J Boots, and S Zolla-Pazner
September 1997, Journal of virology,
Copied contents to your clipboard!