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SPR characterization of antibody binding kinetic to FcγRIIIa variants

In the field of therapeutic mAbs, especially for those who mediate ADCC (Antibody Dependent Cellular Cytotoxicity), the attention is focus on their Fc-domain glycosylation.

In the present study, SPR methods were developed to characterize the binding kinetic of differently glycosylated human IgG1 to FcγRIIIa variants, which are the receptors mediating ADCC.

An expected significant impact of core-fucose on binding kinetic to FcγRIIIa was observed, confirming the diagnostic capability of the methods. Furthermore, a strong correlation between Fc galactosylation, binding affinity for FcγRIIIa variants and ADCC was found, demonstrating the potential of SPR-based method to predict the antibody potency during the process development for antibody manufacturing.

Alessandra Mariani
Laboratory technician Analytical Development, Menarini Biotech

Alessandra, obtained a Master's Degree in Medical Biotechnology at University of Perugia and a PhD in Life Science-cellular physiology at GSK Vaccines-University of Siena.

In 2015, she joined Menarini Biotech, in Pomezia (Rome), where she currently holds a position of Laboratory Technician in the Analytical Development department.

Alessandra’s 8 years experience in R&D of pharma companies was mainly focused on polyclonal and monoclonal antibodies, in particular on the development of immunoassays and kinetic assays for antibody characterization.