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. 2020 Sep 14;10:14991. doi: 10.1038/s41598-020-71748-7

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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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Sequence of the S protein (NCBI: YP_009724390.1) used to generate the 3D model of the glycoprotein. Residues 1–26 and 1,147–1,273 were not included in the 3D structure due to a lack of relevant template structures. Sequences within a rectangle were predicted to consist of one or more HLA antigens using the RankPep server (imed.med.ucm.es/Tools/rankpep^55,56). Glycosites are indicated with asterisks, residues reported to interact with the ACE2 receptor⁶² are underlined, and the protease cleavage site is indicated with a triangle above the RS junction. (a) The sequence is colored according to antibody accessibility computed for the site-specific glycoform from white to red (least to most accessible). (b) Antibody accessibility computed for the non-glycosylated (nude) protein. (c) The difference in accessibilities between the site-specific and non-glycosylated glycoforms is plotted as the fold change in epitope accessibility during the simulation, from − 4 (blue) to 0 (white), where blue indicates glycosylation-dependent surface shielding.