Targeting Receptors on Cancer Cells with Protein Toxins
Antonella Antignani,
Eric Chun Hei Ho,
Maria Teresa Bilotta,
Rong Qiu,
Robert Sarnvosky,
David J. FitzGerald
Affiliations
Antonella Antignani
Biotherapy Section, Laboratory of Molecular Biology, Center of Cancer Research, National Cancer Institute, NIH., 37 Convent Dr, Room 5124, Bethesda, MD 20892, USA
Eric Chun Hei Ho
Biotherapy Section, Laboratory of Molecular Biology, Center of Cancer Research, National Cancer Institute, NIH., 37 Convent Dr, Room 5124, Bethesda, MD 20892, USA
Maria Teresa Bilotta
Biotherapy Section, Laboratory of Molecular Biology, Center of Cancer Research, National Cancer Institute, NIH., 37 Convent Dr, Room 5124, Bethesda, MD 20892, USA
Rong Qiu
Biotherapy Section, Laboratory of Molecular Biology, Center of Cancer Research, National Cancer Institute, NIH., 37 Convent Dr, Room 5124, Bethesda, MD 20892, USA
Robert Sarnvosky
Biotherapy Section, Laboratory of Molecular Biology, Center of Cancer Research, National Cancer Institute, NIH., 37 Convent Dr, Room 5124, Bethesda, MD 20892, USA
David J. FitzGerald
Biotherapy Section, Laboratory of Molecular Biology, Center of Cancer Research, National Cancer Institute, NIH., 37 Convent Dr, Room 5124, Bethesda, MD 20892, USA
Cancer cells frequently upregulate surface receptors that promote growth and survival. These receptors constitute valid targets for intervention. One strategy involves the delivery of toxic payloads with the goal of killing those cancer cells with high receptor levels. Delivery can be accomplished by attaching a toxic payload to either a receptor-binding antibody or a receptor-binding ligand. Generally, the cell-binding domain of the toxin is replaced with a ligand or antibody that dictates a new binding specificity. The advantage of this “immunotoxin” approach lies in the potency of these chimeric molecules for killing cancer cells. However, receptor expression on normal tissue represents a significant obstacle to therapeutic intervention.
