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Aim:To investigate the antitumor activities of an anti-ErbB2 scFv-Fc-interleukin2 (IL-2) fusion protein (HFI) in vitro and in vivo.Methods:Fusion protein HFI wasconstructed.The efficacy of HFI in mediating tumor cell lysis was determined bycolorimetric lactate dehydrogenase release assays.The antitumor activity of HFIwas evaluated in tumor xenograft models.Results:The fusion protein was foldedas a homodimer formed by covalently linking Fc portions and it retained ErbB2specificity and IL-2 biological activity.HFI mediated antibody-dependent cell-mediated cytotoxicity (ADCC) at low effector-to-target ratios in vitro and im-proved the therapeutic efficacy of IL-2 in experiments in vivo.Conclusion:Thegenetically-engineered anti-ErbB2 scFv-Fc-IL-2 fusion protein exhibited high ef-ficiency both in mediating ADCC in vitro and significant antitumor activity intumor xenograft models.
Aim: To investigate the antitumor activities of an anti-ErbB2 scFv-Fc-interleukin2 (HF-I) fusion in vitro and in vivo. Methods: Fusion protein HFI wasconstructed. The efficacy of HFI in mediating tumor cell lysis was determined by colorimetric lactate dehydrogenase release assays. The antitumor activity of HFI as evaluated in tumor xenograft models. Results: The fusion protein was folded as a homodimer formed by covalently linking Fc portions and it retains ErbB2 specificity and IL-2 biological activity. HFI mediated antibody-dependent cell -mediated cytotoxicity (ADCC) at low effector-to-target ratios in vitro and im-proved the therapeutic efficacy of IL-2 in experiments in vivo. Conlusion: The genetically-engineered anti-ErbB2 scFv-Fc-IL-2 fusion protein exhibits high ef-ficiency both mediating ADCC in vitro and significant antitumor activity intumor xenograft models.