Human Antibodies 20 (2011) 65â68 DOI 10.3233/HAB-2011-0256 IOS Press Direct selection of synthetic antibody fragments on cell surface targets from a phage-displayed library Amandeep K. Gakhal et al. University of Toronto, Toronto, Canada The considerable heterogeneity of cell surfaces makes selection of phage-displayed antibody libraries against cell-surface antigens quite challenging. However, many proteins require the membrane environment for proper folding and stability, and as such, the ability to select phage-displayed antibody libraries against cell-surface epitopes remains crucial. We report the development of a novel method for rapidly isolating phage-displayed antibody fragments (Fabs) to cell-surface targets, using the oncogenic human epidermal growth factor receptor 2 (Her2) as a model. Our method enabled us to recover antibody fragments from a phage-displayed synthetic Fab library that bind speciï¬cally and with high afï¬nity to Her2, as assessed by surface plasmon resonance. Flow cytometry and immunoï¬uorescence staining demonstrates that the isolated Fabs also bind speciï¬cally to Her2 expressed on the surface of transiently transfected cells and Her2+ breast cancer cell lines. Competitive ELISAs revealed that speciï¬c Fabs bind to epitopes that are unique from that recognized by the monoclonal antibody (mAb) Herceptin, which has been one of the most successful targeted molecular therapies
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, Volume 20 (3)
IOS Press – Jan 1, 2011
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