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. 2021 Feb 11;11:3551. doi: 10.1038/s41598-021-82893-y

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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 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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The surface exposure of the peptides in the folded forms of the RSV-F protein. (a) the pre-fusion F protein (PDB 3RRR) and (b) the post-fusion F protein (PDB 6APD) are shown in a cartoon-presentation (left panel) and as a surface presentation (right panel). Both forms exist as trimers with the three-fold axis aligned with the vertical axis. The peptides have been colored (P1 green, P2 blue, P3 red, P4 violet and P6 brown; the atomic coordinates for P5 and P6 are missing completely in the post-fusion F protein structure and only 10 residues of P6 have been determined in the pre-fusion F protein structure (brown α-helix in a). P1, P3 and P4 display several surface exposed regions, whereas P2 is mainly buried.