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. 2022 Feb 16;13:903. doi: 10.1038/s41467-022-28450-1

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© The Author(s) 2022

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 Circular dichroism spectra of five cyclic V2 peptides and three V1V2-tags proteins. b Pie charts depicting the percentage of secondary structure (random coil [turquoise], α-helix [light green], or β-sheet [dark blue]) determined by the circular dichroism spectra and calculated by CD-FIT software (https://www.ruppweb.org/Xray/comp/cdfit.htm). c Schematic diagram created with BioRender.com showing the alterative structures of the V2 C-strand (V2C) between an α-helix (left) and a β-strand (right). According to the proportion of each molecule present in the two conformations, the antigens will react preferentially with V2p Abs (left), V2i Abs (right), or both (middle). Abbreviations as in Fig. 1.