Abstract
A new human monoclonal antibody (hmAb), designated m16, was selected by sequential antigen panning (SAP) of a human phage display library against recombinant soluble HIV-1 envelope glycoproteins (Envs) (gp140s) and their complexes with soluble CD4. It bound with high (nM) affinity to gp120 and gp140; the binding was further enhanced by interactions of the Envs with CD4. m16 inhibited cell fusion mediated by the Envs of 9 HIV-1 isolates from clades A, B, E and G with potency on average comparable to that of the broadly neutralizing human monoclonal antibody Fab X5. The identification of a new hmAb with broad neutralizing activity that exhibits differential inhibitory profile suggests a potential for its use as a component of anti-HIV-1 treatments.
Publication types
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Antibodies, Monoclonal / immunology*
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Antibody Affinity
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CD4 Antigens / immunology
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Cell Fusion
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Gene Products, env / immunology
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Genotype
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HIV Antibodies / immunology*
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HIV Antigens / immunology
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HIV Envelope Protein gp120 / immunology
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HIV-1 / genetics*
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HIV-1 / immunology*
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Humans
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Immunoglobulin Fab Fragments / immunology*
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Neutralization Tests
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Peptide Library
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Protein Binding
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Recombinant Proteins / immunology
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env Gene Products, Human Immunodeficiency Virus
Substances
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Antibodies, Monoclonal
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CD4 Antigens
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Gene Products, env
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HIV Antibodies
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HIV Antigens
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HIV Envelope Protein gp120
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Immunoglobulin Fab Fragments
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Peptide Library
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Recombinant Proteins
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env Gene Products, Human Immunodeficiency Virus
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gp140 envelope protein, Human immunodeficiency virus 1