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

By Niina Veitonmäki, 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 and Björn Frendéus


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

Topics: Cancer and Oncology
Publisher: 'Elsevier BV'
Year: 2013
DOI identifier: 10.1016/j.ccr.2013.02.026
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