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. 2020 Jan 17;10:603. doi: 10.1038/s41598-019-57283-0

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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 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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Schematic diagram and predicted 3D model of designed chimeric multiepitope vaccines. (A) The schematic diagram depicting the chimeric multiepitope vaccine of the 45F2 and 42E2 constructs containing 5 different B cell epitopes in α-helical structures (Rip1, BAC6, BAC5, SPB1_1, Sip2, and CSF1 illustrated in violet, blue, brown, green, yellow and orange, respectively) linked with 6 fragments of a β-pleated sheet of the flavodoxin backbone (gray color). (B) The predicted 3D protein structures of the 45F2 and 42E2 models, which were the two best vaccine candidates, are shown as α/β proteins with a flavodoxin fold. Their colors are represented as colors in the schematic diagram, and their N terminus and C terminus are indicated by arrows. These vaccines were designed based on the desirable construction of the TIM-barrel structure, as shown in Fig. 4B.