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. 2022 Nov 4;13:1039765. doi: 10.3389/fimmu.2022.1039765

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Copyright © 2022 Hurler, Toonen, Kajdácsi, van Bree, Brandwijk, de Bruin, Lyons, Bergamaschi, Cambridge Institute of Therapeutic Immunology and Infectious Disease-National Institute of Health Research (CITIID-NIHR) COVID BioResource Collaboration, Sinkovits, Cervenak, Würzner and Prohászka

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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Cross-reactivity of antibodies and new immunoassays. (A, B) Binding of antibodies to proteins of the respective pathways was tested in a direct ELISA. For classical pathway proteins, detection was done with either the C1-INH or C1s antibody, while for lectin pathway proteins detection was done with the C1-INH and MASP-1 antibodies also used during assay development. Conditions were tested in duplicates, while the experiment was performed in triplicates. (C, D) Cross-reactivity of un-complexed complement components was tested using either purified or recombinant proteins of the complex, dependent on availability. While C1s (purified and recombinant) and C1-INH (purified) were tested in the C1s/C1-INH complex assay (C), MASP-1 (recombinant) and C1-INH (purified) were measured in the MASP-1/C1-INH assay (D). (E, F) Cross-reactivity of serum samples from animal origin was investigated in the assays using human EDTA plasma samples (n=4) as a reference, murine serum (n=3), rat serum (n=1), horse serum (n=1), pig serum (n=1) and dog serum (n=1) (E: C1s/C1-INH complex, F: MASP-1/C1-INH complex). Animal samples were measured 10x less diluted compared to human samples. OD, optical density; nm, nanometer.