Reshaping human antibodies for therapy

A human IgGI antibody has been reshaped for serotherapy in humans by introducing the six hypervariable regions from the heavy- and light-chain variable domains of a rat antibody directed against human lymphocytes. The reshaped human antibody is as effective as the rat antibody in complement and is m...

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Veröffentlicht in:	Nature (London) 1988-03, Vol.332 (6162), p.323-327
Hauptverfasser:	Riechmann, Lutz, Clark, Michael, Waldmann, Herman, Winter, Greg
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Animals Antibodies, immunoglobulins Antibodies, Monoclonal - genetics Antibodies, Monoclonal - therapeutic use Base Sequence Binding Sites, Antibody Biological and medical sciences Fundamental and applied biological sciences. Psychology Fundamental immunology Genes, Synthetic Humans Immunity (Disease) Immunoglobulin G - genetics Immunoglobulin G - therapeutic use Immunoglobulin Heavy Chains - genetics Immunoglobulin Light Chains - genetics Immunoglobulin Variable Region - genetics Lymphocytes Lymphocytes - immunology Medical research Molecular immunology Molecular Sequence Data Rats Recombinant Fusion Proteins - genetics Recombinant Fusion Proteins - therapeutic use Recombinant Proteins - genetics Species Specificity Structure Therapy
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Beschreibung
Zusammenfassung:	A human IgGI antibody has been reshaped for serotherapy in humans by introducing the six hypervariable regions from the heavy- and light-chain variable domains of a rat antibody directed against human lymphocytes. The reshaped human antibody is as effective as the rat antibody in complement and is more effective in cell-mediated lysis of human lymphocytes.
ISSN:	0028-0836 1476-4687
DOI:	10.1038/332323a0