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. 2019 Mar 29;69(2):343–354. doi: 10.1136/gutjnl-2018-317725

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© Author(s) (or their employer(s)) 2020. Re-use permitted under CC BY-NC. No commercial re-use. See rights and permissions. Published by BMJ.

This is an open access article distributed in accordance with the Creative Commons Attribution Non Commercial (CC BY-NC 4.0) license, which permits others to distribute, remix, adapt, build upon this work non-commercially, and license their derivative works on different terms, provided the original work is properly cited, appropriate credit is given, any changes made indicated, and the use is non-commercial. See: http://creativecommons.org/licenses/by-nc/4.0/.

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Construction of a unique B cell epitope-based virus-like particulate antigen: CR-T3-SEQ13. (A) Schematic diagram of the design from RBHBcAg to CR-T3-SEQ13; RBHBcAg-aa150-189 was truncated, HBcAg-aa18-27, HBcAg-aa50-69 and HBcAg-aa120-140 were introduced into the RBHBcAg149 by homologous replacement, sequence of SEQ13 polypeptide and linker was inserted by replacement of RBHBcAg-aa79-81, forming a chimeric molecule with a length of 193 amino acid, designated CR-T3-SEQ13. (B) Coomassie blue staining of sodium dodecyl sulfate–polyacrylamide gel electrophoresis (SDS-PAGE) and (C) electron microscopy (EM) picture of recombinant CR-T3-SEQ13 protein. (D) Cryo-EM structure of CR-T3-SEQ13 particle, SEQ13 epitopes are displayed on the spikes of particle. Cryo-EM, cryoelectron microscopy.