Abstract
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.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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AIDS Vaccines / immunology
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Acquired Immunodeficiency Syndrome / virology
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Amino Acid Sequence
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Antibodies, Monoclonal / immunology*
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Antibody Specificity
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HIV Antibodies / immunology*
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HIV Core Protein p24 / analysis
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HIV Envelope Protein gp120 / immunology*
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HIV-1 / immunology*
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HIV-1 / isolation & purification
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Humans
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Immunization, Passive
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Immunoglobulin Fab Fragments / immunology
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Immunoglobulin G / immunology
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Infant
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Infant, Newborn
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Male
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Molecular Sequence Data
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Neutralization Tests
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Recombinant Proteins / immunology
Substances
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AIDS Vaccines
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Antibodies, Monoclonal
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HIV Antibodies
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HIV Core Protein p24
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HIV Envelope Protein gp120
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Immunoglobulin Fab Fragments
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Immunoglobulin G
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Recombinant Proteins