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. 2022 Nov 12;12:19411. doi: 10.1038/s41598-022-23272-z

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© The Author(s) 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 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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Docking studies of multi-epitope protein-based subunit vaccine candidate against LSDV and modeled bovine TLR4. (A) Three-dimensional model of bovine TLR4 obtained by homology modeling and refinement. LRR domain and TIR domain shown in magenta and orange color, respectively, (B) Docked complex of TLR4 and multi-epitope protein based subunit vaccine candidate, where green color represents the TLR4, red color represents the multi-epitope vaccine candidate, blue color and green color with surface models showed the interacting region of the multi-epitope protein and bovine TLR4, magenta with surface model showed the interacting region of LRR domain of TLR4 with multi-epitope protein, (C) Binding residue of the LRR domain of the TLR4 and multi-epitope protein with sticks model, (D) Molecular Dynamics Simulation of multi-epitope protein and bovine TLR4 for 100 ns.