A human ICAM-1 antibody isolated by a function-first approach has potent macrophage-dependent antimyeloma activity in vivo

  • Cancer Cell. 2013 Apr 15;23(4):502-15. doi: 10.1016/j.ccr.2013.02.026.
Niina Veitonmäki  1 ,  Markus Hansson ,  Fenghuang Zhan ,  Annika Sundberg ,  Tobias Löfstedt ,  Anne Ljungars ,  Zhan-Chun Li ,  Titti Martinsson-Niskanen ,  Ming Zeng ,  Ye Yang ,  Lena Danielsson ,  Mathilda Kovacek ,  Andrea Lundqvist ,  Linda Mårtensson ,  Ingrid Teige ,  Guido Tricot ,  Björn Frendéus
Affiliations
  • 1. BioInvent International, Sölvegatan 41, 22370 Lund, Sweden.
PMID: 23597564 DOI: 10.1016/j.ccr.2013.02.026
Abstract

We isolated a tumor B-cell-targeting antibody, BI-505, from a highly diversified human phage-antibody library, using a pioneering "function-first" approach involving screening for (1) specificity for a tumor B cell surface receptor, (2) induction of tumor programmed cell death, and (3) enhanced in vivo antitumor activity compared to currently used treatments. BI-505 bound to intercellular adhesion molecule-1, identifying a previously unrecognized role for this receptor as a therapeutic target in Cancer. The BI-505 epitope was strongly expressed on the surface of Multiple Myeloma cells from both newly diagnosed and relapsed patients. BI-505 had potent macrophage-dependent antimyeloma activity and conferred enhanced survival compared to currently used treatments in advanced experimental models of Multiple Myeloma.

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