ArticleNature communications2020
Mammalian histones facilitate antimicrobial synergy by disrupting the bacterial proton gradient and chromosome organization.
Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
48 citing papers in PubMed, 77 citations in OpenAlex.
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- Heteroaggregation of Antimicrobial Peptides LL-37 and HNP‑1 Drives Cooperative Neutralization of Cytotoxicity.JACS Au · 2026Article
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- Chromatin-derived histone proteins fromFrontiers in cellular and infection microbiology · 2026Article
- Overcoming multidrug resistance: antimicrobial peptides as a next-generation therapeutic strategy.Frontiers in cellular and infection microbiology · 2026Review
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- Bactericidal activity of mammalian histones is caused by large membrane pore formation.Cell reports · 2025Article
- Bacteria detect neutrophils via a system that responds to hypochlorous acid and flow.bioRxiv : the preprint server for biology · 2025Article
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Authors and funding
9 authors at 3 institutions in 2 countries.
Funding
Abstract
First proposed as antimicrobial agents, histones were later recognized for their role in condensing chromosomes. Histone antimicrobial activity has been reported in innate immune responses. However, how histones kill bacteria has remained elusive. The co-localization of histones with antimicrobial peptides (AMPs) in immune cells suggests that histones may be part of a larger antimicrobial mechanism in vivo. Here we report that histone H2A enters E. coli and S. aureus through membrane pores formed by the AMPs LL-37 and magainin-2. H2A enhances AMP-induced pores, depolarizes the bacterial membrane potential, and impairs membrane recovery. Inside the cytoplasm, H2A reorganizes bacterial chromosomal DNA and inhibits global transcription. Whereas bacteria recover from the pore-forming effects of LL-37, the concomitant effects of H2A and LL-37 are irrecoverable. Their combination constitutes a positive feedback loop that exponentially amplifies their antimicrobial activities, causing antimicrobial synergy. More generally, treatment with H2A and the pore-forming antibiotic polymyxin B completely eradicates bacterial growth.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.