Chimeric human antibody molecules: mouse antigen-binding domains with human constant region domains.

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Abstract
Mouse-human antibody molecules of defined antigen-binding specificity were created by taking the variable region genes of a mouse antibody-producing myeloma cell line with known antigen-binding specificity and joining them to human Ig constant region genes using recombinant DNA techniques. Chimeric genes were constructed that utilized the rearranged and expressed antigen-binding variable region exons from the myeloma cell line S107, which produces an IgA (.kappa.) anti-phosphocholine antibody. The H chain variable region exon was joined to human IgG1 or IgG2 H chain constant region genes, and the L chain variable region exon from the same myeloma was joined to the human .kappa. L chain gene. These genes were transfected into mouse myeloma cell lines, generating transformed cells that produce chimeric mouse-human IgG (.kappa.) or IgA (.kappa.) anti-phosphocholine antibodies. The transformed cell lines remained tumorigenic in mice and the chimeric molecules were present in the ascitic fluids and sera of tumor-bearing mice.