Human monoclonal antibody that recognizes the V3 region of human immunodeficiency virus gp120 and neutralizes the human T-lymphotropic virus type IIIMN strain

We describe a human IgG1 monoclonal antibody (N701.9b) derived by Epstein-Barr virus transformation of B cells from a human immunodeficiency virus-seropositive asymptomatic donor. This antibody was shown to recognize the principal neutralizing domain contained within the V3 region of gp120 of the MN...

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Bibliographic Details
Published in:	Proceedings of the National Academy of Sciences - PNAS 1990-11, Vol.87 (21), p.8597-8601
Main Authors:	C F Scott, Jr, S Silver, A T Profy, S D Putney, A Langlois, K Weinhold, J E Robinson
Format:	Article
Language:	eng
Subjects:	AIDS/HIV Amino Acid Sequence Antibodies, Monoclonal - immunology Antibody-Dependent Cell Cytotoxicity B-Lymphocytes - immunology Biological and medical sciences Epitopes - analysis Epitopes - immunology Fundamental and applied biological sciences. Psychology HIV - genetics HIV - immunology HIV Envelope Protein gp120 - genetics HIV Envelope Protein gp120 - immunology HIV-1 - immunology HIV-1 - isolation & purification Humans Microbiology Molecular Sequence Data Neutralization Tests Species Specificity Vaccines, antisera, therapeutical immunoglobulins and monoclonal antibodies Vaccinia virus - genetics Virology
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Summary:	We describe a human IgG1 monoclonal antibody (N701.9b) derived by Epstein-Barr virus transformation of B cells from a human immunodeficiency virus-seropositive asymptomatic donor. This antibody was shown to recognize the principal neutralizing domain contained within the V3 region of gp120 of the MN strain of human immunodeficiency virus and MN-like strains, as determined by binding to the PB-1 fragment of MN gp120 and to synthetic peptides corresponding to the V3 region of MN and related virus strains. The epitope identified by monoclonal antibody N701.9b was mapped to a segment of V3 containing at least 7 amino acids (amino acids 316-322), which is located in the "tip" and "right" side of the V3 loop of the MN strain. Furthermore, this antibody manifested potent type-specific fusion-inhibitory activity against the MN strain but not against the IIIB or RF virus strains. This antibody also neutralized four virus isolates that had MN-like V3 region sequences and failed to neutralize three other strains containing unrelated V3 region sequences. Our findings confirm that the V3 region stimulates type-specific neutralizing antibody during natural human immunodeficiency virus infection in humans. The potential clinical use of this antibody is discussed.
ISSN:	0027-8424 1091-6490