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. 2022 Jan 5;12:790415. doi: 10.3389/fimmu.2021.790415

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Copyright © 2022 Vanderheijden, Stevaert, Xie, Ren, Barbezange, Noppen, Desombere, Verhasselt, Geldhof, Vereecke, Stroobants, Oh, Vanhee, Naesens and Nauwynck

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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Isolation of peptide-purified antibodies (pAbs) from human serum. (A) Pepscan analysis of human serum sample #20Hu384 (obtained from a COVID-19 convalescent patient) prior to purification. (B) Purification principle. Serum #20Hu384 was submitted to peptide-affinity chromatography using immobilized PEP3, PEP71, PEP72 or PEP79. (C) Elution profiles during chromatography. The fractions with the highest concentrations were combined. (D) Pepscan analysis of the pAbs purified on columns with immobilized PEP3, PEP71, PEP72 or PEP79. The lowest panel shows the profile of the control sample containing late (low-protein) elution fractions (= fractions 8 and 9 from PEP79 column). The bars show the OD_{450 nm} value. (E) Western blot analysis of S-plasmid transfected PK-15 cells shows binding of pAb-PEP3 to cleaved (S2) and full-length SARS-CoV-2 S. (F) Antibody titers of serum #20Hu384, the four pAbs and elution buffer in IPMA assays for SARS-CoV-2 S and N; HCoV-229E and -OC43; and FeCV.