Monoclonal antibodies to a glycolipid antigen on human neuroblastoma cells.

TLDR

Four murine monoclonal antibodies (three IgM and one IgG3) were generated by somatic cell hybridization against a neuroblastoma cell surface glycolipid antigen. The antibodies bound strongly to >98 % of neuroblastoma cells, killed all cells with complement, reacted with melanoma and osteogenic sarcoma but not most other tumors, showed no cross‑reactivity with normal tissues, and could detect as few as 0.1 % tumor cells in bone marrow, indicating diagnostic and therapeutic potential.

Abstract

Using a somatic cell hybridization technique, four murine monoclonal antibodies (three immunoglobulin M and one immunoglobulin G3) were produced against a human neuroblastoma cell surface glycolipid antigen. They reacted strongly with all human neuroblastoma tumor-containing specimens and six of eight human neuroblastoma cell lines. More than 98% of each neuroblastoma cell population possessed this surface antigen, and in the presence of complement, 100% of them were killed. While melanoma and osteogenic sarcoma carried this antigen, leukemia and most Ewing's and Wilms' tumors did not. There was no cross-reaction with 30 normal or remission bone marrow samples and none with normal human tissues other than neurons in vitro. This antigen was neuraminidase sensitive, separable on thin-layer chromatogram, and did not modulate after combining with the monoclonal antibodies. These antibodies could detect less than 0.1% tumor cells deliberately seeded in the bone marrow samples. Because of their unique properties, these monoclonal antibodies may have diagnostic and therapeutic potentials.