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. 2019 Nov 6;10:2478. doi: 10.3389/fimmu.2019.02478

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Copyright © 2019 Bornhöfft, Rebl, Gallagher, Viergutz, Zlatina, Reid and Galuska.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Investigation of the sialic acid binding properties of human and bovine Siglec-8. (A) Overlay of the tertiary structure of hSiglec-8 (gray) and bovine Siglec-8 (blue). The components of the glycan are differently labeled: sialic acid (purple), fucose (yellow), galactose-6-P (cyan), N-acetylgalactosamine (magenta), 3-aminopropan-1-ol (green). (B) Differences in the tertiary structure of hSiglec-8 (gray) and bovine Siglec-8 (blue). Different views of the glycan-binding domain are shown (1–4). (3,4) 6-P is labeled in red. All figures were created by Chimera 1.13.1. Red circle demonstrates potential differences in glycan-binding properties. The structure of hSiglec-8 is based on Pröpster et al. (41) and the structure of bovine Siglec-8 was designed using Phyre².