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

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.

[1]  M. Robert-Guroff,et al.  HTLV-III-neutralizing antibodies in patients with AIDS and AIDS-related complex , 1985, Nature.

[2]  M. Gonda,et al.  Simple, rapid, quantitative, syncytium-forming microassay for the detection of human immunodeficiency virus neutralizing antibody. , 1987, AIDS research and human retroviruses.

[3]  S. Green,et al.  A versatile in vivo and in vitro eukaryotic expression vector for protein engineering , 1988, Nucleic Acids Res..

[4]  J. Moore,et al.  An enzyme-linked immunosorbent assay for antibodies to the envelope glycoproteins of divergent strains of HIV-1. , 1989, AIDS.

[5]  W. O'brien,et al.  HIV-1 tropism for mononuclear phagocytes can be determined by regions of gp120 outside the CD4-binding domain , 1990, Nature.

[6]  J. Moore,et al.  Characterization of recombinant gp120 and gp160 from HIV-1: binding to monoclonal antibodies and soluble CD4. , 1990, AIDS.

[7]  H. Sheppard,et al.  Application of a rapid microplaque assay for determination of human immunodeficiency virus neutralizing antibody titers , 1990, Journal of clinical microbiology.

[8]  M. Champe,et al.  Protection of chimpanzees from infection by HIV-1 after vaccination with recombinant glycoprotein gp120 but not gp160 , 1990, Nature.

[9]  D. Ho,et al.  High concentrations of recombinant soluble CD4 are required to neutralize primary human immunodeficiency virus type 1 isolates. , 1990, Proceedings of the National Academy of Sciences of the United States of America.

[10]  T. Matthews,et al.  Preparation and characterization of an intravenous solution of IgG from human immunodeficiency virus-seropositive donors , 1991 .

[11]  D. Ho,et al.  Conformational epitope on gp120 important in CD4 binding and human immunodeficiency virus type 1 neutralization identified by a human monoclonal antibody , 1991, Journal of virology.

[12]  C. Barbas,et al.  Assembly of combinatorial antibody libraries on phage surfaces: the gene III site. , 1991, Proceedings of the National Academy of Sciences of the United States of America.

[13]  D R Burton,et al.  A large array of human monoclonal antibodies to type 1 human immunodeficiency virus from combinatorial libraries of asymptomatic seropositive individuals. , 1991, Proceedings of the National Academy of Sciences of the United States of America.

[14]  D. Ho,et al.  Mapping genetic determinants for human immunodeficiency virus type 1 resistance to soluble CD4 , 1992, Journal of virology.

[15]  L. De,et al.  Selective disruption of growth hormone transcription machinery by viral infection. , 1992, Proceedings of the National Academy of Sciences of the United States of America.

[16]  E. G. Shpaer,et al.  Genetic relationships determined by a DNA heteroduplex mobility assay: analysis of HIV-1 env genes. , 1993, Science.

[17]  R. Siliciano,et al.  Induction of HIV-1-neutralising and syncytium-inhibiting antibodies in uninfected recipients of HIV-1IIIB rgp120 subunit vaccine , 1993, The Lancet.

[18]  D. Burke,et al.  Phylogenetic analysis of gag genes from 70 international HIV‐1 isolates provides evidence for multiple genotypes , 1993, AIDS.

[19]  G R Pilkington,et al.  Molecular profile of an antibody response to HIV-1 as probed by combinatorial libraries. , 1993, Journal of molecular biology.

[20]  N. Letvin.  Vaccines against human immunodeficiency virus--progress and prospects. , 1993, The New England journal of medicine.

[21]  Jitters jeopardize AIDS vaccine trials. , 1993, Science.

[22]  J. Sodroski,et al.  Probing the structure of the human immunodeficiency virus surface glycoprotein gp120 with a panel of monoclonal antibodies , 1994, Journal of virology.

[23]  D R Burton,et al.  Recognition properties of a panel of human recombinant Fab fragments to the CD4 binding site of gp120 that show differing abilities to neutralize human immunodeficiency virus type 1 , 1994, Journal of virology.

[24]  E. Emini,et al.  Neutralization of divergent human immunodeficiency virus type 1 variants and primary isolates by IAM-41-2F5, an anti-gp41 human monoclonal antibody. , 1994, Proceedings of the National Academy of Sciences of the United States of America.

[25]  J. Mascola,et al.  Two antigenically distinct subtypes of human immunodeficiency virus type 1: viral genotype predicts neutralization serotype. , 1994, The Journal of infectious diseases.

[26]  D R Burton,et al.  In vitro evolution of a neutralizing human antibody to human immunodeficiency virus type 1 to enhance affinity and broaden strain cross-reactivity. , 1994, Proceedings of the National Academy of Sciences of the United States of America.

[27]  J. Bradac,et al.  Neutralization of HIV-1. , 1994, AIDS research and human retroviruses.

[28]  L. Sawyer,et al.  Neutralization sensitivity of human immunodeficiency virus type 1 is determined in part by the cell in which the virus is propagated , 1994, Journal of virology.

[29]  J. Cohen.  The HIV vaccine paradox. , 1994, Science.

[30]  J. Moore,et al.  Macrophage-tropic and T-cell line-adapted chimeric strains of human immunodeficiency virus type 1 differ in their susceptibilities to neutralization by soluble CD4 at different temperatures , 1994, Journal of virology.