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. 2017 Sep 27;8:1197. doi: 10.3389/fimmu.2017.01197

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Copyright © 2017 Darling, Sherwood and Hayhurst.

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) or licensor 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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Purification of single-domain antibody (sdAb) proteins and recombinant nucleoprotein (NP) for ELISA characterization. Coomassie stained SDS-PAGE gel showing 5 µg of each sdAb monomer (A) and dimer (B) purified from Escherichia coli periplasm. (C) Silver stained SDS-PAGE gel of Marburgvirus (MARV) (M) and Ebolavirus (EBOV) (Z) NP preparations following large-scale transient transfection and purification through centrifugation steps and banding on CsCl gradients. (D) ELISA titration of the anti-MARV sdAb monomers and dimers over MARV NP with the highest concentration also applied to Bundibugyo NP (this was expressed at higher levels than Zaire NP and so was convenient to use for controls yet shares high homology at the C-terminal domain for our studies). (E) ELISA titration of anti-EBOV sdAb E monomer and dimer over EBOV NP and MARV NP.