Recombinant antibody constructs in cancer therapy

Curr Opin Immunol. 1999 Oct;11(5):548-57. doi: 10.1016/s0952-7915(99)00013-8.

Abstract

Recombinant antibodies and their fragments now represent over 30% of all biological proteins undergoing clinical trials for diagnosis and therapy. The focus on antibodies as the ideal cancer-targeting reagents recently culminated in approval by the Food and Drugs Administration for the first engineered therapeutic antibodies. In the past year, important advances have been made in the design, selection and production of new types of engineered antibodies. Innovative selection methods have enabled the isolation of high-affinity cancer-targeting and antiviral antibodies, the latter capable of redirecting viruses for gene therapy applications. In other strategies for cancer diagnosis and therapy, recombinant antibody fragments have been fused to radioisotopes, drugs, toxins, enzymes and biosensor surfaces. Bispecific antibodies and related fusion proteins have been produced for cancer immunotherapy, effectively enhancing the human immune response in anticancer vaccines and T cell recruitment strategies.

Publication types

  • Review

MeSH terms

  • Animals
  • Antibodies, Neoplasm / genetics
  • Antibodies, Neoplasm / therapeutic use*
  • Clinical Trials as Topic
  • Drug Approval
  • Humans
  • Immunoglobulin Fab Fragments / genetics
  • Immunoglobulin Fab Fragments / therapeutic use*
  • Immunoglobulin G / genetics
  • Immunoglobulin G / therapeutic use*
  • Mice
  • Mice, Transgenic
  • Neoplasms / diagnosis
  • Neoplasms / therapy*
  • Protein Engineering
  • Recombinant Proteins / therapeutic use*

Substances

  • Antibodies, Neoplasm
  • Immunoglobulin Fab Fragments
  • Immunoglobulin G
  • Recombinant Proteins