Recombinant IgY for improvement of immunoglobulin-based analytical applications

Clinical Biochemistry
Kerstin GreunkeEdzard Spillner

Abstract

In order to provide superior tools for diagnostic approaches and to prevent assay interference and background binding, the objective of this study was the establishment and evaluation of monoclonal IgY which are phylogenetically distant from mammalian immunoglobulins but have been unavailable so far. Human, murine and avian monoclonal model antibodies were established and produced in mammalian cells. Their interaction with human serum components and Fc gamma receptors was compared by ELISA and fluorescence activated cell sorting (FACS). The use of monoclonal IgY in contrast to mammalian antibodies prevented interference phenomena in absorbance measurements generated by human sera containing rheumatoid factor (RF) or heterophilic antibodies. Additionally, monoclonal IgY exhibited no interaction with the human and murine high-affinity receptor FCGR1 (CD64) and human low affinity receptor FCGR3a (CD16A). The data obtained demonstrate the advantageous behaviour of monoclonal IgY as detection or capture antibodies compared to conventional mammalian immunoglobulins and provide a strategy for improvement of assay performance and accuracy.

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Citations

Apr 18, 2012·Protein Engineering, Design & Selection : PEDS·P J ConroyS Hearty
Jul 4, 2012·Biologicals : Journal of the International Association of Biological Standardization·Edzard SpillnerDion du Plessis
Jul 26, 2018·Journal of Immunoassay & Immunochemistry·Natália Maria LanzariniMarcelo Alves Pinto
Jul 7, 2012·Journal of Receptor and Signal Transduction Research·Zehua Tian, Xiaoying Zhang

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