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. 2024 May 21;15:4301. doi: 10.1038/s41467-024-48514-8

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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 HmAb64 binding to gp120 Env proteins. HmAb64 showed strong binding to wild-type gp120 antigens from multiple HIV-1 isolates but not to their D368R mutants, indicating CD4-binding site specificity. Data are presented as mean values ± SEM (n = 2 duplicated wells). b Neutralization breadth. HmAb64 neutralized 20 viruses (10%) from diverse clades of the 208-strain NIAID panel. c Neutralization titers (IC₅₀) and tier designation of VRC panel viruses neutralized by HmAb64. d Number and percentage in each tier designation of VRC panel viruses neutralized by HmAb64. Source data are provided as a Source Data file.