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. 2020 Nov 5;10:19122. doi: 10.1038/s41598-020-75571-y

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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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Structure of Gc protein and its conversion to GcMAF. Yamamoto et al. proposed (Model A) for the structure of DBP/Gc1F protein and its conversion to GcMAF²⁵. In this model, GalNAc is covalently bound to Thr⁴²⁰ of the Gc1F protein and galactose and sialic acid are bound to GalNAc in a Y-branched arrangement. Therefore, removal of galactose and sialic acid exposes the GalNAc moiety and leads to the formation of activated GcMAF. However, Ravnsborg et al. recently proposed a linear model (Model B) based on mass spectrometry findings²³. In this model, the three sugar moieties attached to threonine 420 are arranged in a linear fashion with GalNAc covalently bound to threonine, and galactose and sialic acid attached to the GalNAc in this order. Non-glycosylated Gc2 is also illustrated based on current mass spectrometry findings.