A novel human antitumor dimeric immunoRNase.

Abstract

We report on the construction, production, and characterization of a new fully human dimeric immunoRNase, obtained by fusion of Erbicin, a human anti-ErbB2 single-chain antibody fragment (scFv), with a dimeric mutant of human pancreatic RNase (HHP2-RNase). This novel immunoagent with 2 scFv moieties each fused to 1 of the 2 subunits of the dimeric RNase, called ERB-HHP2-RNase, has shown improved biologic properties with respect to the previously reported monomeric ERB-hRNase immunoRNase: it selectively binds ErbB2-positive cancer cells with an increased avidity; it is not inhibited by the cytosolic ribonuclease inhibitor; it is endowed with a more powerful cytotoxic activity.

• Authors: Gennaro Riccio, Marianna Borriello, Giuseppe D'Alessio, Claudia De Lorenzo
• Journal: Journal of immunotherapy (Hagerstown, Md. : 1997) (J Immunother) Vol. 31 Issue 5 Pg. 440-5 (Jun 2008) ISSN: 1524-9557 [Print] United States
• PMID: 18463541 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Immunoglobulin Variable Region
• Receptor, ErbB-2
• Ribonucleases

Topics

• Cell Line, Tumor
• Dimerization
• Gene Expression
• Humans
• Immunoglobulin Variable Region (immunology)
• Immunotherapy
• Neoplasms (enzymology, immunology, therapy)
• Pancreas (enzymology)
• Receptor, ErbB-2 (immunology)
• Ribonucleases (genetics, immunology, isolation & purification, metabolism)