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. 2018 Nov 7;7:176. doi: 10.1038/s41426-018-0178-y

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© The Author(s) 2018

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 license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license 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 license, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 4 — Homotrimers of H9 HA. Selected receptor-binding residues shown in red (P92, G128, T129, S130, S131, A132, W142, N173, L184, Y185, N214, G215, G218 and R219). Images made in Pymol⁵² (Schrödinger) based on the structure of A/swine/Hong Kong/9/1998 (Protein databank ID:1JSD)⁵³. a Residues recognised by mouse mAbs, positions with updated site H9-A shown in green, H9-B residues shown in blue. b Residues labelled with substitutions that affect the binding of chicken polyclonal antisera. Non-glycosylation altering substitutions shown in yellow; glycosylation site adding mutations shown in black; site 150, which had both glycosylation adding and non-glycosylation adding mutations shown in brown