| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 1971371 | Clinical Biochemistry | 2008 | 8 Pages |
ObjectivesIn 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.Design and methodsHuman, murine and avian monoclonal model antibodies were established and produced in mammalian cells. Their interaction with human serum components and Fcγ receptors was compared by ELISA and fluorescence activated cell sorting (FACS).ResultsThe 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).ConclusionsThe 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.
