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. 2022 Jun 11;13:3367. doi: 10.1038/s41467-022-31035-7

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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. 4 — a Structural modeling of the FMC63 binding epitope on CD19. Residues in blue (R144, W140, and P203) are essential for antibody binding and proximal asparagine residues are in red (N125 and N114). b Median Fluorescence Intensity of CD19 as detected by FMC63-APC on the surface of WT, SPPL3^KO or SPPL3^KO CD19^KO (dual KO) Nalm6 cells engineered to express mutated CD19 molecules. Representative data from n = 2 flow cytometry experiments. c Survival of Nalm6 cells over time after combination with CART19 (E:T ratio 0.25:1). Representative data from n = 2 experiments with independent T cell donors. Error bars reflect mean ± standard error of the mean (s.e.m.). ****P < 0.0001 by two-way ANOVA with Bonferroni correction for multiple comparisons. Source Data are provided as a Source Data file.