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. 2022 Jan 27;7:13. doi: 10.1038/s41541-022-00430-y

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© This is a U.S. government work and not under copyright protection in the U.S.; foreign copyright protection may apply 2022

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 1 — A Predicted monomer structures of circular permutants with inserted epitopes (circled). Left (TMV-Junc); middle (TMV-NPNAx5); and right (fully assembled TMV-Junc disk based on 3KML crystal structure). All structures were predicted by Rosetta Protein Prediction Server and images generated using PyMOL software. B Coomassie blue stained SDS-PAGE gels showing Ni-NTA and Q-Sepharose purification results for TMV-Junc and TMV-NPNAx5 proteins (arrow). C Electron micrographs of each purified vaccine preparation. D Representative ELISA titration curve of mAbs 317 (red) and CIS43 (blue) binding to FL-CSP, TMV-NPNAx5, and TMV-Junc (top to bottom).