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. 2020 Oct 9;10:16944. doi: 10.1038/s41598-020-74101-0

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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 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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Potential phosphorylation of the S1/S2 site. (a) A scheme of the 20-residue segment of the SARS-CoV2 S1/S2 site. In addition to a furin site, the four-residue insertion (PRRA) creates potential phosphorylation sites for proline-directed kinases (S680) and basophilic kinases (S686). (b) Multiple sequence alignment of different S1/S2 sequences used in phosphorylation assays in panel ‘c’. (c) The phosphorylation of S1/S2-GB1 reporter proteins was analyzed in vitro using cyclin B-Cdk1 (CDK) and protein kinase A (PKA) as a representative of proline-directed and basophilic kinases, respectively. The phosphorylation reactions were stopped at 0, 5, 20, and 60 min. Phosphorylation shifts were analyzed using Phos-tag SDS-PAGE, which separates the phosphorylated form from the unphosphorylated form. Coomassie-stained gels are shown. Uncropped images are shown in Supplementary Fig. S3.