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. 2021 Jan 17;10(1):37–50. doi: 10.1080/22221751.2020.1862631

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© 2021 The Author(s). Published by Informa UK Limited, trading as Taylor & Francis Group, on behalf of Shanghai Shangyixun Cultural Communication Co., Ltd

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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Figure 1. — Generation and characterization of mAbs specific for precore/core proteins. (A) Schematic diagram of mAbs which generated in this study and their binding epitopes on precore/core proteins. (B) Binding activities of mAbs to recombinant core/precore proteins of aa (−10)-149, aa (−10)-152, aa (−10)-183, and aa1–183 by indirect chemiluminescent immunoassay. (C) SPR sensorgrams showing the binding kinetics for the proteins of aa (−10)-152 and aa1–183 to immobilized NTR-mAbs of 9F10 and 16D9. Coloured lines represented a global fit of the data at known concentrations using a 1:1 binding model. (D) Peptide competitive ELISA-binding assay to analysis the accurate targeting epitopes of the two NTR-mAbs. The sequences of peptide competitors were showed on the left Y-axis. Peptide competitors with an over 50% inhibition indicated the corresponding peptides contain the binding motif of the NTR-mAbs.