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. 2022 Aug 1;7:261. doi: 10.1038/s41392-022-01118-4

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© 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/.

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Fig. 2 — APOE3 interacts with ACE2 and reduces ACE2-mediated Spike docking onto the cell surface. a Co-immunoprecipitation between APOE and ACE2 in 293T-ACE2 cells overexpressing APOE3-Flag. b Cell-free protein pull-down analysis of ACE2-Fc and recombinant APOE3 protein with indicated amounts. c Bio-layer interferometry analysis of immobilized ACE2-Fc proteins bound to APOE3 proteins at the following concentrations: 1000, 500, 250, 125, and 62.5 nM (corresponding to kinetic curves from top to bottom). d Immuno-electron microscopic analysis of the localization of ACE2, APOE and the SARS-CoV-2 pseudo-virus in 293T-ACE2 cellular cultures with (right panel) or without APOE treatment (left panel). e–h Super-resolution (e, f) and immuno-electron (g, h) microscopic analyses of the amount of Spike-Fc protein bound to the surface of 293T-ACE2 cells in the presence of recombinant APOE3 proteins at varying concentrations. n = 4 independent experiments. Data are presented as mean ± S.E.M. Statistical significances were determined by one-way ANOVA tests. *P < 0.05; **P < 0.01