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. 2020 Jun 5;11:2841. doi: 10.1038/s41467-020-16639-1

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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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Fig. 3 — a High-performance size-exclusion chromatography (HPSEC) profiles and b sedimentation velocity profiles of HPV16 VLPs, HPV52 VLPs, HPV16L1-C175A–HPV52L1-C428A chVLPs, HPV52L1-C175A–HPV16L1-C428A chVLPs, HPV16L1-C175A, HPV52L1-C175A, HPV16L1-C428A, and HPV52L1-C428A. c Dynamic light scattering analysis of HPV16 VLPs, HPV52 VLPs, HPV16L1-C175A–HPV52L1-C428A chVLPs, and HPV52L1-C175A–HPV16L1-C428A chVLPs. d Differential scanning calorimetry reveals an additional melted phase of the original capsomeres for HPV16L1-C175A–HPV52L1-C428A chVLPs and HPV52L1-C175A–HPV16L1-C428A chVLPs as compared with WT VLPs. The dominant phase transition peak lies between the parental HPV16 and HPV52 VLPs, which have a single Tm peak in the scanning curves. Tm values for HPV16 VLPs, HPV52 VLPs, HPV16L1-C175A–HPV52L1-C428A chVLPs, HPV52L1-C175A–HPV16L1-C428A chVLPs, and HPV16-C175A and HPV52-C428A L1 proteins were 68.9 °C, 64.2 °C, 67.7 °C, 67.1 °C, 66.9 °C, and 57.0 °C, respectively. e Micrographs of vitrified HPV16, 52 L1 VLPs and HPV16L1-C175A–HPV52L1-C428A chVLPs (top). Scale bar, 100 nm. One representative image from three biological repeats is shown. Reconstructed 3D cryo-electron microscopy (cryo-EM) maps of HPV16 and HPV52 L1 VLPs and HPV16L1-C175A–HPV52L1-C428A chVLPs (below). In terms of morphology, chVLPs present as a T = 7 icosahedral arrangement similar to the wild-type VLPs.