Binding dynamics analysis of IgG and IgA antibodies by surface plasmon resonance (SPR) analysis.

(A) F045-092 IgG1 (black), monomeric IgA1 (red, A1Mo), and monomeric IgA2m2 (blue, A2m2Mo) antibodies were subjected to SPR analysis of their binding dynamics to the recombinant trimeric HA proteins from JP305 virus (H2N2). (B) Binding dynamics of F045-092 IgG1 (black), monomeric IgA1 (red, A1Mo), dimeric SIgA1 (orange, A1Di), and tetrameric SIgA1 (blue, A1Te) antibodies to the recombinant trimeric HA proteins from JP305 virus (H2N2) were examined. (C) Binding dynamics of F045-092 IgG1 (black), monomeric IgA2m2 (red, A2m2Mo), and tetrameric SIgA2m2 (blue, A2m2Te) antibodies to the recombinant trimeric HA proteins from JP305 virus (H2N2) were examined. Sensorgrams were x and y-axis adjusted (x = 0, y = 0: baseline, y = 100:binding) to allow comparisons between different antibody forms in terms of the dissociation rate of IgA from HA.