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. 2024 May 27;15:4505. doi: 10.1038/s41467-024-48758-4

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© The Author(s) 2024

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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Fig. 2 — a Cryo-EM structures of H7.HK1 and H7.HK2 bound to H7 HA in the head region. b Top view of alignment of H7.HK1 and H7.HK2 complex structures. c Surface presentation of the H7.HK1 epitope (orange) on H7 HA1, with interacting CDRs shown. d H7.HK1 heavy chain forms seven hydrogen bonds and one salt bridge with H7 HA1. e H7.HK1 light chain forms one additional hydrogen bond with H7 HA1, and the interactions are stabilized by hydrophobic residues on the periphery of the light chain interface. f Modeling published structures of H7 HA1-binding antibodies (PDB: 6II4, 6II8, 6II9, 5V2A) onto the H7.HK1 bound structure, with an escape mutation R57K (green) reported for mAb 07-5F01. Competition ELISA with biotinylated H7.HK2 binding to the H7 HA monomer, in which unlabeled competing mAbs were titrated at increasing concentrations to evaluate the effect on H7.HK2 binding. Source data is provided in the Source Data file. g Sequence analysis of N = 1,483 H7 HA1s revealed a conserved lateral patch that largely overlaps with the H7.HK1 epitope. h Modeling the binding site of human receptor analogue LSTc (red) based on a previous crystal structure (PDB: 4BSE) onto H7 from the H7.HK1 complex, showing that H7.HK1 does not compete with sialic acid on the adjacent protomer (black). Alignment of the H7.HK1 complex with a previous crystal structure of H7 (PDB: 4BSE) shows that the 220-loop (pink) required for sialic acid binding (G218-G228) is disordered and would clash with the H7.HK1 light chain if it were present. Green asterisk symbol denotes the <2 Å clash between the CDR L1 N28 and the predicted location of P221 on HA1.