Construction of an immunotoxin by linking a monoclonal antibody against the human epidermal growth factor receptor and a hemolytic toxin

• ANA D AVILA ^[1] ; CARLOS F CALDERÓN ^[1] ; RITA M PEREZ ^[1] ; CARMEN PONS ^[1] ; CELIA M PEREDA ^[1] ; ANA R ORTIZ ^[1]
  1. [1] Instituto Nacional de Oncología y Radiobiología Unidad de Evaluación e Investigación de Productos Antitumorales
• Localización: Biological Research, ISSN-e 0717-6287, ISSN 0716-9760, Vol. 40, Nº. 2, 2007, págs. 173-183
• Idioma: inglés
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• Resumen

  • Hybrid molecules obtained through conjugation of monoclonal antibodies and toxins constitute an approach under exploration to generate potential agents for the treatment of cancer and other diseases. A frequently employed toxic component in the construction of such immunotoxins is ricin, a plant toxin which inhibits protein synthesis at ribosomal level and so requires to be internalized by the cell. A hemolytic toxin isolated from the sea anemone Stichodactyla helianthus, which is active at the cell membrane level, was linked through a disulfide bond to the anti-epidermal growth factor receptor monoclonal antibody ior egf/r3. The resulting immunotoxin did not exhibit hemolytic activity except under reducing conditions. It was toxic for H125 cells that express the human epidermal growth factor receptor, but non-toxic for U1906 cells that do not express this receptor