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. 2021 Jan 25;12:559. doi: 10.1038/s41467-020-20879-6

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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 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. 1 — a X-ray structure of H3 hemagglutinin bound by Fab 3I14. One HA protomer is shown in cartoon with HA1 colored orange and HA2 colored red. The other two HA protomers are shown in surface representation and colored white or gray. 3I14 is shown in surface representation with heavy chain colored blue and light chain colored green. b Zoomed in view of the box from a showing the H3-3I14 interface and the major structural elements of HA, which are recognized. Helix A is colored red, the fusion peptide is colored cyan, HA1 is colored orange, and a second HA protomer is colored gray. The 3I14 CDRs are shown as cartoons. A group 2-specific sugar residue at position 38 of HA1 is labeled as NAG38*. c Similar view as in b showing the H6-3I14^D93N interface. A group 1-specific sugar on the second HA protomer, which interacts with 3I14 is labeled as NAG33*.