Selective cytotoxic activity of immunotoxins composed of a monoclonal anti-Thy 1.1 antibody and the ribosome-inactivating proteins bryodin and momordin

Br J Cancer. 1988 Nov;58(5):558-61. doi: 10.1038/bjc.1988.258.

Abstract

The ribosome-inactivating proteins, bryodin, from Bryonia dioica, and momordin, from Momordica charantia, were coupled by a disulphide bond to a monoclonal anti-Thy 1.1 antibody (OX7). Both immunotoxins were specifically cytotoxic to the Thy 1.1-expressing mouse lymphoma cell line AKR-A in vitro. The OX7-bryodin immunotoxins were the more powerfully toxic and reduced protein synthesis in AKR-A cells by 50% at a concentration of 1-4 x 10(-11) M as compared with 1 x 10(-9) M for the OX7-momordin immunotoxins. Neither of the immunotoxins was toxic to mouse lymphoma EL4 cells, which lack the Thy 1.1 antigen, at concentrations up to 3 x 10(-8) M. Further, bryodin and momordin immunotoxins made from an antibody (R10) of irrelevant specificity were without effect on AKR-A cells.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Antibodies, Monoclonal / therapeutic use
  • Antimetabolites, Antineoplastic / therapeutic use
  • Immunotoxins / therapeutic use*
  • Isoantibodies
  • Lymphoma / drug therapy
  • Mice
  • N-Glycosyl Hydrolases*
  • Plant Proteins / therapeutic use*
  • Ribosome Inactivating Proteins, Type 1
  • Ribosome Inactivating Proteins, Type 2
  • T-Lymphocytes / immunology
  • Toxins, Biological*
  • Tumor Cells, Cultured / drug effects

Substances

  • Antibodies, Monoclonal
  • Antimetabolites, Antineoplastic
  • Immunotoxins
  • Isoantibodies
  • Plant Proteins
  • Ribosome Inactivating Proteins, Type 1
  • Ribosome Inactivating Proteins, Type 2
  • Toxins, Biological
  • anti-Thy antibody
  • bryodin
  • N-Glycosyl Hydrolases