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. 2018 Apr 11;8:5820. doi: 10.1038/s41598-018-23552-7

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© The Author(s) 2018

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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Intrinsically disordered regions in VP0, VP1 and VP3 can interact with HPeV1 RNA. (A) RCAP results of peptides from VP0, VP1, and VP3 that could interact with the HPeV1 RNA. The residues in the peptides crosslinked to RNA are underlined. The VP0-A, VP1-A and VP3-A peptides were all missing from the X-ray structure and predicted to be intrinsically disordered. The VP0-B, VP1-B and VP3-B peptides were all modelled in the X-ray structure. (B) Peptides from intrinsically disordered regions of VP0, VP1, and VP3 can bind to HPeV1 RNA in a fluorescence anisotropy assay. Each error bar shows one standard deviation of three independent measurements. The asterisk denotes the samples whose anisotropy values differ from the anisotropy value of the peptide alone by a p value of <0.02 in the Student’s T-test.