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. 2021 Apr 26;11:8921. doi: 10.1038/s41598-021-87959-5

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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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Fc fusion and N-linked glycans improve the production profile of GDF15. (a) Schematic representation of proposed Fc-glyco GDF15 therapeutic. Red, Knob-Fc chain. Blue, Hole-Fc chain. Light blue, mature GDF15 homodimer. N and C termini are highlighted. (b) Mature GDF15 amino acid sequence (UniProt Q99988, PRO_0000033993). Sites to introduce N-linked glycosylation are underlined. Red, putative serum cleavage sites. (c) Location of introduced N-glycan sites modeled on the GDF15-GFRAL crystal structure (PDB 5VZ4) using The PyMOL Molecular Graphics System, Version 2.0 Schrödinger, LLC (https://pymol.org/). Introduced asparagine (N) mutations are shown as spheres. Numbers correspond to glyco-variant number (eg. Mutant 2). (d) Summary of Fc-GDF15 NxT mutant expression and purification yields, including expression titer (mg/L), Protein of Interest (POI) percentage following size exclusion chromatography (SEC), and SEC yield.