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. 2019 Nov 26;10:5389. doi: 10.1038/s41467-019-12973-1

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© The Author(s) 2019

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. 6 — MPER-induced PO₄-binding site of H4K3 and PGZL1 lipid site mutant characterization and electrostatics. a, b Stick rendering of the PO₄-binding site in (a) H4K3 and (b) PGZL1. The side chain at LC position 50 in each antibody is surrounded by dots. Select HC residues of the two antibodies are shown in blue (a) and green (b), and the LC is shown in brown. MPER is shown as a pink ribbon. c Binding of H4K3 lipid-binding site mutants to immobilized MPER peptide by BLI. d Binding of H4K3 lipid-binding site mutants to MPER peptide by ELISA and neutralization (log IC₅₀) of HxB2 and Du156.12. e BLI, ELISA binding to MPER peptide, and neutralization statistics. f–i Surface rendering, along the MPER helical axis (red ribbon), of the solvent accessible electrostatic potential contoured at ± 5 kT/e for (f) PGZL1 gVmDmJ, (g) PGZL1, (h) H4K3, and (i) 4E10. Observed lipid fragments and anions are shown as sticks. Source data for h and i are provided as a Source Data file.