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. 2021 Nov 18;12:6705. doi: 10.1038/s41467-021-27075-0

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© The Author(s) 2021

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 Binding of biotinylated DARPins to cells expressing Env (JR-FL) was assessed by flow cytometry. Histograms of normalized fluorescence intensities and corresponding plots showing mean fluorescence intensities (MFI) as a function of concentration are depicted. Top: DARPin (0.5 µM) binding in the presence of increasing concentrations of sCD4. Bottom: DARPin binding at increasing concentrations in the presence of 2 µM sCD4. Background binding was assessed on cells expressing Mulv Env (shown are representative MFI data for the three bnDs). b Competition ELISA to probe for V3-crown conformational preferences of DARPins. DARPin binding to immobilized recombinant Env-derived proteins was measured at a concentration just before reaching saturation. Env proteins were chosen to maximize the dynamic binding range for the individual DARPin (bnD1: BG505gp120∆V1V2; bnD.2: JR-FLgp120; bnD.3: trimeric BG505-SOSIP). Each DARPin/Env pair was competed with increasing concentrations of the BG505 V3 peptides indicated in the legend.