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Membrane damage by MBP-1 is mediated by pore formation and amplified by mtDNA. | LitMetric

Membrane damage by MBP-1 is mediated by pore formation and amplified by mtDNA.

Cell Rep

Institute of Pharmacology, University of Bern, 3010 Bern, Switzerland; Institute of Biochemistry, Brandenburg Medical School, 16816 Neuruppin, Germany. Electronic address:

Published: April 2024

Eosinophils play a crucial role in host defense while also contributing to immunopathology through the release of inflammatory mediators. Characterized by distinctive cytoplasmic granules, eosinophils securely store and rapidly release various proteins exhibiting high toxicity upon extracellular release. Among these, major basic protein 1 (MBP-1) emerges as an important mediator in eosinophil function against pathogens and in eosinophil-associated diseases. While MBP-1 targets both microorganisms and host cells, its precise mechanism remains elusive. We demonstrate that formation of small pores by MBP-1 in lipid bilayers induces membrane permeabilization and disrupts potassium balance. Additionally, we reveal that mitochondrial DNA (mtDNA) present in eosinophil extracellular traps (EETs) amplifies MBP-1 toxic effects, underscoring the pivotal role of mtDNA in EETs. Furthermore, we present evidence indicating that absence of CpG methylation in mtDNA contributes to the regulation of MBP-1-mediated toxicity. Taken together, our data suggest that the mtDNA scaffold within extracellular traps promotes MBP-1 toxicity.

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Source
http://dx.doi.org/10.1016/j.celrep.2024.114084DOI Listing

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