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. 2020 Oct 12;10:16984. doi: 10.1038/s41598-020-73210-0

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© The Author(s) 2020

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 licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence 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 licence, visit http://creativecommons.org/licenses/by/4.0/.

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(a) Computer Model of ToxAll. The core particle is composed of the pentameric and trimeric coiled coils. They are shown in green and blue, respectively. Attached to the trimeric coiled coil is the TLR5 agonist flagellin (purple) while the B cell epitope MIC1 (red) is attached to the pentameric coiled coil. The HLA-A*11:01 CD8⁺ epitopes (gold) are engineered into flagellin, the CD4⁺ epitope is engineered into the trimeric coiled coil, the HLA-A*02:01 and HLA-B*07:01 CD8⁺ epitopes are attached to the N-terminal end of the protein chain. While the B-cell epitope MIC1 appears to be hidden in the assembled particle, the structures of the pentamer and trimer reveal that there is ample void space that allows antibodies to bind to MIC1 in the assembled structure. (b) Biochemical and Biophysical Analysis. Part (A) SDS-PAGE of the purified construct. Part (B) Transmission electron microscopy of ToxAll showing relatively uniform and non-aggregating nanoparticles. The bar corresponds to 100 nm. Part (C) DLS size distribution analysis of ToxAll showing an average nanoparticle size of ~ 40 nm.