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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. 2 — a Transmission electron microscopy (TEM) views show the ratio profiles of various molar pairings of HPV16L1-C175A and HPV52L1-C428A, with better VLP assembly in the pictures along the forward diagonal of the array (see images with red boxes). This suggests a preference for an equal molar ratio of two distinct capsomeres in hybrid assembly. Scale bar, 100 nm. One representative image from three biological repeats is shown. b Size-exclusion chromatography resolves the components of hybrid-assembling samples with various molar ratio mixing. The resultant chVLPs were retained at earlier retention time with respect to original pentamer. The unassembled pentamer component nearly disappears in the elution curve of 1:1(molar ratio) mixture of HPV16L1-C175A and HPV52L1-C428A. HPV16 and HPV52 VLPs, HPV16L1-C175A and HPV52L1-C428A mutants were used as elution markers in the chromatography. c Coomassie-stained SDS-PAGE showed the comparable amounts of HPV16 and HPV52 L1 mutants within assembled HPV16L1-C175A–HPV52L1-C428A chVLPs and HPV52L1-C175A–HPV16L1-C428A chVLPs. The different length of HPV16 and HPV52 L1 constructs allows to be separated and quantified in gel and they were verified by type-specific mAb western-blotting, respectively. The results reveal the optimized stoichiometry for hybrid-assembling is equal molar ratio of paired pentamer mutants, originals, and overloading of either pentamer over 1:1 ratio disturbs the assembly procedure and leads to irregular aggregation. The uncropped original scans can be found in Supplementary Fig. 18.