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. 2021 Oct 14;20:198. doi: 10.1186/s12934-021-01689-x

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© The Author(s) 2021

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 — Structural variation of model glycoproteins. A Structural models of (i) NGRP, (ii) scFv13R4 and scFv13R4CM were generated by Phyre2 based on protein homology prediction (≥ 99% confidence) [113]. (iii) X-ray crystallographic structure of RNase A (PDB code 3WMR). Ribbon model of the proteins was drawn by UCSF Chimera [114]. Position of the sequon variants (D/E-X-N-X-S/T, X ≠ P) within the protein is indicated. Disulphide-bonds are highlighted in yellow. C-terminal sequon (DQNAT) of scFv13R4 is not displayed in the protein model. B Linear representation of proteins; (i) NGRP, (ii) scFv13R4, (iii) scFv13R4CM, and (iv) RNase A. Position of disulphide-bonds (C–C) and glycosylation sites (N) are indicated with amino acid positions