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. 2024 May 31;15:4629. doi: 10.1038/s41467-024-48059-w

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© The Author(s) 2024

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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Fig. 1 — A Schematic of the RV3 F ectodomain used to screen for stabilizing substitutions in the head domain. The domain organization is color-coded, with start and end residue numbers indicated. Location of N-linked glycosylation sites are shown. B, C Expression of preF protein variants in supernatant as measured by BioLayer Interferometry (BLI) using immobilized PIA174. The initial slope, V0, at the start of binding is plotted as the average of three independent transfections; shown is the mean with error bars representing the standard deviation (SD). B Individual substitutions were tested and are colored by design feature. The dotted red line indicates the binding rate of the backbone construct RV3 F-GCN4. C Combinations (orange) of promising stabilizing substitutions of (B) were tested and compared to the individual substitutions (green and blue).