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. 2020 Apr 22;8:346. doi: 10.3389/fchem.2020.00346

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Copyright © 2020 Göritzer, Goet, Duric, Maresch, Altmann, Obinger and Strasser.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Biophysical and functional characterization of recombinant monomeric, dimeric and tetrameric IgA. (A) Overlay of normalized SE-HPLC-MALS chromatograms of affinity and gel-filtration purified IgA1 and IgA2m(2) monomers, dimers and tetramers produced in HEK293F cells and N. benthamiana ΔXT/FT plants. (B) SDS-PAGE under reducing (+DTT) and non-reducing conditions of purified monomeric (m) and dimeric (d) IgA1 and IgA2m(2) produced in N. benthamiana ΔXT/FT plants followed by Coomassie Brilliant Blue staining. (C) Binding of the IgA variants to the antigen HER2. The EC₅₀ vales were determined as the mean ± standard deviation from three independent measurements. “m” monomeric, “d” dimeric, “t” tetrameric IgA. (D) Binding affinities of IgA1 and IgA2m(2) monomers and dimers to FcαRI. K_D values were obtained by SPR spectroscopy in single-cycle kinetic experiments from three independent measurements. Error bars represent standard deviation.