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

TLDR

Chimeric mouse‑human IgG anti‑phosphocholine antibodies were produced by fusing variable region exons from the S107 myeloma cell line to human IgG1/IgG2 heavy‑chain constant regions and a human kappa light‑chain gene, then transfecting the constructs into mouse myeloma cells. The resulting cell lines remained tumorigenic in mice, and the chimeric antibodies were detected in ascitic fluid and serum of tumor‑bearing animals.

Abstract

We have created mouse-human antibody molecules of defined antigen-binding specificity by taking the variable region genes of a mouse antibody-producing myeloma cell line with known antigen-binding specificity and joining them to human immunoglobulin 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 heavy chain variable region exon was joined to human IgG1 or IgG2 heavy chain constant region genes, and the light chain variable region exon from the same myeloma was joined to the human kappa light chain gene. These genes were transfected into mouse myeloma cell lines, generating transformed cells that produce chimeric mouse-human IgG (kappa) or IgG (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.