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. 2020 Jul 6;27:78. doi: 10.1186/s12929-020-00669-4

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© The Author(s) 2020

Open AccessThis 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/. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated in a credit line to the data.

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Fig. 2 — E2 epitopes (I to III) adopt distinct conformations when complexed with different antibodies. a Conformations of epitope I: (Upper) Closed β-hairpin in complex with nAb HCV1 (PDB: 4DGY); (Middle) extended-coil conformation in complex with nAb 3/11 (PDB: 4WHY); and (Lower) intermediate-coil conformation with an anti-parallel β-sheet in complex with nAb HC33.1 (PDB:4XVJ). b Conformations of epitope II: (Upper) Preferred state of E2 in the viral particle containing a short 1.5-turn α-helix (aa437–442) and an extended conformation (aa443–446, not shown) in complex with nAb HC84.27 (PDB: 4JZO); and (Lower) conformational changes through short α-helix flipping out (‘open state’) to expose aa437(W) and aa438(L) residues for nAb mAb#8 (PDB: 4HZL). c Conformations of epitope III: (Upper) Open and stabilized strand in β-sheet conformation with aa537(F) and aa539(L) residues flipped out into the hydrophobic part of the Ig-like domain in complex with AR3C Fab (PDB: 4MWF); and (Lower) helical disordered conformation with aa537(F) and aa539(L) residues solvent-exposed in complex with non-nAb DAO5 (PDB: 5NPJ)