Figure - PMC

Skip to main content

An official website of the United States government

Here's how you know

Here's how you know

Official websites use .gov
A .gov website belongs to an official government organization in the United States.

Secure .gov websites use HTTPS
A lock ( ) or https:// means you've safely connected to the .gov website. Share sensitive information only on official, secure websites.

View full-text article in PMC

. 2022 May 2;13:2378. doi: 10.1038/s41467-022-29950-w

Search in PMC
Search in PubMed
View in NLM Catalog
Add to search

© The Author(s) 2022

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/.

PMC Copyright notice

Fig. 4 — a, b Cryo-EM maps of the 28-12-H1 (a) and 28-12-H3 (b) complexes. One HA protomer and the cognate 28-12 Fab fragment are highlighted in color, and the other two copies in the trimer are colored gray. H1 HA1/HA2 and H3 HA1/HA2 are colored in navy blue, orange, blue, and gold, respectively. The heavy and light chains of 28-12 Fab are colored in lime green and turquoise, respectively. This color scheme was followed throughout. c, f Epitopes of the 28-12 Fab on H1 (c) and H3 (f), respectively. The epitopes in helix A (indicated by black dashed box) and fusion peptide/HA1 (indicated by red dashed box) are colored in purple and magenta, respectively. H3 residue N49_HA2 is specifically showed in red. d, g Hydrogen bonds between 28-12 Fab and the fusion peptide/HA1 of H1 (d) or H3 (g). e, h Hydrogen bonds formed between helix A of H1 (e) or H3 (h) and 28-12 Fab. The salt bridge and hydrogen bond are shown as red and black dashed lines, respectively. i, k Hydrophobic epitopes in the H1 (i) and H3 (k) HAs. The hydrophobic epitopes are classified into two parts, helix A in the dashed black box and the fusion peptide and HA1 residues in the dashed magenta circle. j, l The Fab residues involved in hydrophobic contacts with H1 (j) and H3 (l) are shown with side chains. m The number of atom-to-atom contacts between 28-12 Fab and the fusion peptide/HA1 residues. n The number of atom-to-atom contacts between 28-12 Fab and the helix A. The epitopes involved in the hydrophobic interaction, hydrogen bond, and salt bridge are colored in blue. o, p 28-12 binding to H1 and H3 HA mutants with alanine substitutions. Each value is calculated as the binding ratio relative to that of the WT HA (%). The two black dotted lines represent 100 and 125% relative binding to the WT data, respectively. The mean values of duplicates are shown from two independent experiments (o, p).