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. 2020 Jun 30;11:3279. doi: 10.1038/s41467-020-17047-1

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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. 4 — a, b Heatmap displays of differential scanning fluorimetry (DSF) analyses to query (a) capsid protein unfolding (uncoating) and (b) DNA accessibility (vector genome extrusion) at pHs 7, 6, 5, and 4. Color scaling depicted represent relative peak signals from highest to lowest value (brightest to dimmest, respectively). c–e Each defining amino acid residue of AAVv66 was converted to those of AAV2 by site-directed mutagenesis and examined for changes in c packaging yield, d capsid stability, and e genome release at pH 7. Values represent mean ± SD. p Values were determined by one-way ANOVA. *p < 0.05, **p < 0.01, ***p < 0.001, ****p < 0.0001. n = 3/group.