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Molecular Immunology
Vol. 82, 2017, Pages: 46–49

Quantification and simultaneous evaluation of the bioactivity of antibody produced in CHO cell culture—The use of the ectodomain of Fc?RI and surface plasmon resonance-based biosensor

July Dorion-Thibaudeau, Yves Durocher, Gregory De Crescenzo

Department of Chemical Engineering, Groupe de Recherche en Sciences et Technologies Biomédicales, Bio-P2 Research Unit, École Polytechnique de Montréal, P.O. Box 6079, succ. Centre-Ville, Montreal, QC H3C 3A7, Canada.

Abstract

A surface plasmon resonance (SPR)-based assay has been developed in order to quantify the monoclonal antibody (Mab) Trastuzumab within the supernatant of a mammalian cell culture using the ectodomain of FcγRI (CD64) and confirm Mab bioactivity, i.e. binding to its antigen Her2, in a single biosensing experiment. Under partial mass transport limitation, we were able to quantify Mab present in unpurified samples taken throughout the cell culture. While Mab capture on the biosensor surface confirmed the ability of its Fc region to bind to FcγRI, the binding activity of its Fab region was also tested by injecting increasing concentrations of the Mab antigen (Her2). The kinetics of the interactions we recorded from 48 h post transfection until the end of the culture, were superimposable, which highly suggested that the quality attributes of the antibody were conserved throughout the process. This SPR methodology is thus of great interest for atline quality control analysis during Mab production campaign.

Keywords: Fc?R; Monoclonal antibody; Surface plasmon resonance (SPR); Bioprocess monitoring.

 
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