ArticleProceedings of the National Academy of Sciences of the United States of America2001
Delivery of proteins into living cells by reversible membrane permeabilization with streptolysin-O.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 139 papers.
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139 citing papers in PubMed, 332 citations in OpenAlex.
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- Calpains orchestrate secretion of annexin-containing microvesicles during membrane repair.The Journal of cell biology · 2025Article
- Mechanistic Insights into the Tools for Intracellular Protein Delivery.Chem & bio engineering · 2025Review
- Mechanosensitive nuclear uptake of chemotherapy.Science advances · 2024Article
- Multiwell-based G0-PCC assay for radiation biodosimetry.Scientific reports · 2024Article
- RNA structure promotes liquid-to-solid phase transition of short RNAs in neuronal dysfunction.Communications biology · 2024Article
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- Ryanodine receptor 1-mediated CaJournal of experimental & clinical cancer research : CR · 2022Article
- The pore conformation of lymphocyte perforin.Science advances · 2022Article
- The cellular response to plasma membrane disruption for nanomaterial delivery.Nano convergence · 2022Review
- Gasdermins in Innate Host Defense AgainstFrontiers in immunology · 2022Review
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- Beyond pore formation: reorganization of the plasma membrane induced by pore-forming proteins.Cellular and molecular life sciences : CMLS · 2021Review
- Bead Loading Proteins and Nucleic Acids into Adherent Human Cells.Journal of visualized experiments : JoVE · 2021Article
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- Glycolytic ATP fuels phosphoinositide 3-kinase signaling to support effector T helper 17 cell responses.Immunity · 2021Article
79 more citing papers are in PubMed but not listed here.
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7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The pore-forming toxin streptolysin O (SLO) can be used to reversibly permeabilize adherent and nonadherent cells, allowing delivery of molecules with up to 100 kDa mass to the cytosol. Using FITC-labeled albumin, 10(5)-10(6) molecules were estimated to be entrapped per cell. Repair of toxin lesions depended on Ca(2+)-calmodulin and on intact microtubules, but was not sensitive to actin disruption or to inhibition of protein synthesis. Resealed cells were viable for days and retained the capacity to endocytose and to proliferate. The active domains of large clostridial toxins were introduced into three different cell lines. The domains were derived from Clostridium difficile B-toxin and Clostridium sordelli lethal toxin, which glycosylate small G-proteins, and from Clostridium botulinum C2 toxin, which ADP-ribosylates actin. After delivery with SLO, all three toxins disrupted the actin cytoskeleton to cause rounding up of the cells. Glucosylation assays demonstrated that G-proteins Rho and Ras were retained in the permeabilized cells and were modified by the respective toxins. Inactivation of these G-proteins resulted in reduced stimulus-dependent granule secretion, whereas ADP-ribosylation of actin by the C. botulinum C2-toxin resulted in enhanced secretion in cells. The presented method for introducing proteins into living cells should find multifaceted application in cell biology.
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