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. 2023 Mar 23;14:1606. doi: 10.1038/s41467-023-37225-1

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© The Author(s) 2023, corrected publication 2023

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 Illustration of the assembly process and working principle of AMF-Bac. B The design of plasmids I and II. C The growth of Bac-HlpA/EGFP-BLPs and Bac-HlpA/EGFP after 42 °C treatment for the indicated times (0–120 min), as monitored by OD₆₀₀. The data are shown as the mean ± SD (n = 3 independent experiments). D Bacteria from the different groups at 6 h in C were seeded on agar plates, and the number of colonies formed was counted. CFU, colony forming unit. The data are shown as the mean ± SD (n = 3 independent experiments). E The lysis of Fe-Bac-HlpA/EGFP-BLPs after AMF treatment (310 kHz and 23.8 kA/m) for the indicated times (0–80 min), as observed by CLSM. The bacteria were tracked by their EGFP expression, and the Fe₃O₄ NPs on the bacterial membrane were labeled with Cy5.5. Scale bar, 10 μm. F, G The lysis of engineered bacteria induced by AMF treatment in vivo. Mice bearing CT-26-luc xenografts were treated with engineered bacteria. The number of live bacteria in the tumor was measured by the spread plate method (G). The data (G) are shown as the mean ± SD (n = 4 mice). H Optimization of the inducible expression conditions for overnight expression of CD47nb in the Fe-Bac-HlpA/CD47nb-BLPs. I The release of CD47nb (containing a Myc tag) from Fe-Bac-HlpA/CD47nb-BLPs upon 42 °C treatment for the indicated times (0–120 min) by western blot analysis using an anti-Myc tag antibody. J The release of CD47nb from Fe-Bac-HlpA/CD47nb-BLPs after AMF treatment (310 kHz and 23.8 kA/m) for the indicated times (0–160 min), as examined by dot blotting. K The affinity of the released CD47nb to the CD47 protein was verified by dot blotting. L Competition binding assay using the anti-CD47 antibody to examine the affinity of released CD47nb to CD47 in CT-26 cells. The data are shown as the mean ± SD (n = 3 independent experiments). These experiments (E, H–K) were repeated three times independently with similar results. Source data are provided as a Source Data file.