Antigen-binding affinity and thermostability of chimeric mouse-chicken IgY and mouse-human IgG antibodies with identical variable domains

Abstract

Constant (C)-region switching of heavy (H) and/or light (L) chains in antibodies (Abs) can affect their affinity and specificity, as demonstrated using mouse, human, and chimeric mouse-human (MH) Abs. However, the consequences of C-region switching between evolutionarily distinct mammalian and avian Abs remain unknown. To explore C-region switching in mouse-chicken (MC) Abs, we investigated antigen-binding parameters and thermal stability of chimeric MC-6C407 and MC-3D8 IgY Abs compared with parental mouse IgGs and chimeric MH Abs (MH-6C407 IgG and MH-3D8 IgG) bearing identical corresponding variable (V) regions. The two MC-IgYs exhibited differences in antigen-binding parameters and thermal stability from their parental mouse Abs. However, changes were similar to or less than those between chimeric MH Abs and their parental mouse Abs. The results demonstrate that mammalian and avian Abs share compatible V-C region interfaces, which may be conducive for the design and utilization of mammalian-avian chimeric Abs.

A Novel Approach for Development of Intraocular Biodegradable Ranibizumab Implant: A Solution for Stability of Protein Activity

“…In a study conducted in 2019 on the thermal stability of IgG1 antibody, it was found that almost half of the binding activity of the antibody decreased after two minutes at 90°C, and Fab (e.g., ranibizumab) was very sensitive to heat treatment. 26 , 29 , 30 The present results also indicated that half of the antibody activity decreased in in vitro angiogenesis of HUVECs after about five minutes of heating at 100°C, whereas Fab complexation led to higher thermal stability.…”

Generation and Evaluation of Chicken IgY-scFv for the Purposes of CPV Diagnosis and Therapy

“…Designing on chimeric antibody could be the next step for IgY-scFv study in order to provide better compatibility of the antibody in the host system, and to recoup the possibly decreased speci city and a nity of antibody fragments as compared to full length antibody. Recent study con rmed that mammalian IgG and avian IgY shared compatible V-C region interfaces, which may be conducive for the design and utilization of mammalian-avian chimeric Abs (24).…”

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