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. 2018 Dec 18;9:5360. doi: 10.1038/s41467-018-07199-6

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© The Author(s) 2018

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. 7 — Crystal structures of the chimeric pentamers. a The modified L1 sequence on the BC and HI loop(s) of the lead candidates of the double- and triple-type chimeric VLPs: H58-33BC and H58-33BC-52HI. The consensus is determined based on an alignment of L1 sequences from 20 different HPV serotypes (also see Supplementary Fig. 4). b A structural comparison of pentamers among HPV58 (gray), HPV33 (light blue), HPV52 (pale cyan), and the chimeric proteins H58-33BC (pale green) and H58-33BC-52HI (light pink). Loops BC and HI are boxed in red and black, respectively. c Structural comparisons of the BC loops of WT (HPV58 [gray], HPV33 [light blue]) and chimeric L1 proteins (H58-33BC [pale green], H58-33BC-52HI [pale pink]). Upper left: Ribbon display of superimposed main-chain carbon atoms. Side-chains of the different amino acids between HPV58 and HPV33 are labeled and shown as sticks. Upper middle, right and lower: Pairwise structural comparisons with surface display among HPV58, HPV33, H58-33BC and H58-33BC-52HI. d Structural comparisons of HI loops of WT (HPV58 [gray], HPV52 [pale cyan]) and the chimeric L1 protein (H58-33BC-52HI [light pink]). Upper left: Ribbon display of superimposed main-chain carbon atoms. Side-chains of the different amino acids between HPV58 and HPV52 are labeled and shown as sticks. Upper right and lower: Pairwise structural comparisons with surface display among HPV58, HPV52 and H58-33BC-52HI. For presentation clarity, the surface of the chimera in the pairwise surface comparisons in c, d is shown with 50% transparency and embracing the model rendered in stick mode; the surface of the wild-type model is shown with full opaqueness