Abstract
Two human monoclonal antibodies, RF-1 and RF-2, specifically recognize the fusion protein of the human respiratory syncytial virus (RSV). These were isolated from spontaneous tumors in SCID mice reconstituted with human splenocytes and boosted with fusion protein. The tumors consisted of Epstein-Barr virus-transformed human B cells in animals with antigen-specific antibody titers>105. The binding affinity of RF-1 and RF-2 to the fusion protein is 1010 and 109 M-1, respectively. The antibodies bind specifically to a conformational epitope of the fusion protein on RSV-infected HEp-2 cells. Both antibodies display virus-neutralizing properties in vitro at concentrations varying between 8 and 1000 ng/mL. Virus neutralization applies to a broad variety of wild and laboratory-adapted virus strains belonging to both virus types A and B. These antibodies are potential candidates for passive immunotherapy of severe RSV infections.
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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Animals
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Antibodies, Monoclonal / immunology*
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Antibodies, Monoclonal / isolation & purification
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Antibodies, Monoclonal / metabolism
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Antibodies, Viral / immunology*
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Antibodies, Viral / isolation & purification
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Antibodies, Viral / metabolism
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Antibody Specificity
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B-Lymphocytes / virology
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Cell Transformation, Viral
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Enzyme-Linked Immunosorbent Assay
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HN Protein*
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Herpesviridae Infections / immunology
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Herpesviridae Infections / virology
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Herpesvirus 4, Human / immunology
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Humans
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Immunoblotting
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Mice
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Mice, SCID
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Neoplasms, Experimental / immunology*
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Neutralization Tests
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Respiratory Syncytial Viruses / immunology*
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Spleen / cytology
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Tumor Virus Infections / immunology
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Tumor Virus Infections / virology
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Viral Envelope Proteins
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Viral Fusion Proteins / immunology*
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Viral Proteins / immunology*
Substances
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Antibodies, Monoclonal
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Antibodies, Viral
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HN Protein
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Viral Envelope Proteins
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Viral Fusion Proteins
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Viral Proteins
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attachment protein G