BIOMAT Database Logo BIOMAT Database Logo

Efficient neutralization of primary isolates of HIV-1 by a recombinant human monoclonal antibody. 1994

D R Burton, and J Pyati, and R Koduri, and S J Sharp, and G B Thornton, and P W Parren, and L S Sawyer, and R M Hendry, and N Dunlop, and P L Nara
Department of Immunology, Scripps Research Institute, La Jolla, CA 92037.

The ability of antibodies to neutralize diverse primary isolates of human immunodeficiency virus-type 1 in vitro has been questioned, with implications for the likely efficacy of vaccines. A recombinant human antibody to envelope glycoprotein gp120 was generated and used to show that primary isolates are not refractory to antibody neutralization. The recombinant antibody neutralized more than 75 percent of the primary isolates tested at concentrations that could be achieved by passive immunization, for example, to interrupt maternal-fetal transmission of virus. The broad specificity and efficacy of the antibody implies the conservation of a structural feature on gp120, which could be important in vaccine design.

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
D007116 Immunization, Passive Transfer of immunity from immunized to non-immune host by administration of serum antibodies, or transplantation of lymphocytes (ADOPTIVE TRANSFER). Convalescent Plasma Therapy,Immunoglobulin Therapy,Immunotherapy, Passive,Normal Serum Globulin Therapy,Passive Antibody Transfer,Passive Transfer of Immunity,Serotherapy,Passive Immunotherapy,Therapy, Immunoglobulin,Antibody Transfer, Passive,Passive Immunization,Therapy, Convalescent Plasma,Transfer, Passive Antibody
D007140 Immunoglobulin Fab Fragments Univalent antigen-binding fragments composed of one entire IMMUNOGLOBULIN LIGHT CHAIN and the amino terminal end of one of the IMMUNOGLOBULIN HEAVY CHAINS from the hinge region, linked to each other by disulfide bonds. Fab contains the IMMUNOGLOBULIN VARIABLE REGIONS, which are part of the antigen-binding site, and the first IMMUNOGLOBULIN CONSTANT REGIONS. This fragment can be obtained by digestion of immunoglobulins with the proteolytic enzyme PAPAIN. Fab Fragment,Fab Fragments,Ig Fab Fragments,Immunoglobulins, Fab Fragment,Fab Immunoglobulin Fragments,Immunoglobulin Fab Fragment,Immunoglobulins, Fab,Fab Fragment Immunoglobulins,Fab Fragment, Immunoglobulin,Fab Fragments, Immunoglobulin,Fragment Immunoglobulins, Fab,Fragment, Fab,Immunoglobulin Fragments, Fab
D007223 Infant A child between 1 and 23 months of age. Infants
D007231 Infant, Newborn An infant during the first 28 days after birth. Neonate,Newborns,Infants, Newborn,Neonates,Newborn,Newborn Infant,Newborn Infants
D008297 Male Males
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
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
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man

Related Publications

D R Burton, and J Pyati, and R Koduri, and S J Sharp, and G B Thornton, and P W Parren, and L S Sawyer, and R M Hendry, and N Dunlop, and P L Nara
Neutralization of HIV-1 primary isolates by polyclonal and monoclonal human antibodies.
September 1997, International immunology,
D R Burton, and J Pyati, and R Koduri, and S J Sharp, and G B Thornton, and P W Parren, and L S Sawyer, and R M Hendry, and N Dunlop, and P L Nara
Neutralization of primary HIV-1 isolates by anti-envelope monoclonal antibodies.
August 1995, AIDS (London, England),
D R Burton, and J Pyati, and R Koduri, and S J Sharp, and G B Thornton, and P W Parren, and L S Sawyer, and R M Hendry, and N Dunlop, and P L Nara
Recombinant human monoclonal antibody IgG1b12 neutralizes diverse human immunodeficiency virus type 1 primary isolates.
May 1997, AIDS research and human retroviruses,
D R Burton, and J Pyati, and R Koduri, and S J Sharp, and G B Thornton, and P W Parren, and L S Sawyer, and R M Hendry, and N Dunlop, and P L Nara
Efficient neutralization of primary isolates by the plasma from HIV-1 infected Indian children.
October 2011, Viral immunology,
D R Burton, and J Pyati, and R Koduri, and S J Sharp, and G B Thornton, and P W Parren, and L S Sawyer, and R M Hendry, and N Dunlop, and P L Nara
Antibody neutralization-resistant primary isolates of human immunodeficiency virus type 1.
December 1998, Journal of virology,
D R Burton, and J Pyati, and R Koduri, and S J Sharp, and G B Thornton, and P W Parren, and L S Sawyer, and R M Hendry, and N Dunlop, and P L Nara
Neutralization of primary human immunodeficiency virus type 1 isolates by the broadly reactive anti-V3 monoclonal antibody, 447-52D.
November 1994, Journal of virology,
D R Burton, and J Pyati, and R Koduri, and S J Sharp, and G B Thornton, and P W Parren, and L S Sawyer, and R M Hendry, and N Dunlop, and P L Nara
Neutralization of divergent human immunodeficiency virus type 1 variants and primary isolates by IAM-41-2F5, an anti-gp41 human monoclonal antibody.
April 1994, Proceedings of the National Academy of Sciences of the United States of America,
D R Burton, and J Pyati, and R Koduri, and S J Sharp, and G B Thornton, and P W Parren, and L S Sawyer, and R M Hendry, and N Dunlop, and P L Nara
Structural rationale for the broad neutralization of HIV-1 by human monoclonal antibody 447-52D.
February 2004, Structure (London, England : 1993),
D R Burton, and J Pyati, and R Koduri, and S J Sharp, and G B Thornton, and P W Parren, and L S Sawyer, and R M Hendry, and N Dunlop, and P L Nara
Genetic diversity of primary HIV-1 isolates and their sensitivity to antibody-mediated neutralization.
July 2000, Virology,
D R Burton, and J Pyati, and R Koduri, and S J Sharp, and G B Thornton, and P W Parren, and L S Sawyer, and R M Hendry, and N Dunlop, and P L Nara
A human monoclonal antibody neutralizes diverse HIV-1 isolates by binding a critical gp41 epitope.
October 2005, Proceedings of the National Academy of Sciences of the United States of America,
Copied contents to your clipboard!