ArticleJournal of innate immunity2014
Novel role of the antimicrobial peptide LL-37 in the protection of neutrophil extracellular traps against degradation by bacterial nucleases.
Article in Journal of innate immunity, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 85 papers, 1 of them a synthesis that pooled it.
What it found
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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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
85 citing papers in PubMed, 1 synthesis or guideline pooled it, 134 citations in OpenAlex.
- Vitamin D deficiency in patients with cystic fibrosis: a systematic review and meta-analysis.Journal of health, population, and nutrition · 2024Pooled it
- Vitamin D for the Immune System in Cystic Fibrosis (DISC): a double-blind, multicenter, randomized, placebo-controlled clinical trial.The American journal of clinical nutrition · 2019Trial
- Impact of cathelicidin cleavage by SpeB onbioRxiv : the preprint server for biology · 2026Article
- Building Blocks of 2,3-Diaminopropionic Acid Functionalized with an Oxa-Acid Spacer Shift the Functional Profile of Human Cathelicidin LL-37: Enhanced Enzymatic Stability and Selective Suppression of Neutrophil Degranulation.Pharmaceuticals (Basel, Switzerland) · 2026Article
- Human cathelicidin peptide LL-37 compacts nucleic acids and alters neutrophil extracellular trap structure.Scientific reports · 2026Article
- LL-37 selectively targets Plasmodium-infected erythrocytes and exhibits antimalarial activity.PLoS pathogens · 2026Article
- Investigation of Regulation and Binding Patterns of the Human Cathelicidin Peptide LL-37 in Complexation with Nucleic Acids, and its Impact on Neutrophil Extracellular Traps.bioRxiv : the preprint server for biology · 2026Article
- Immune evasion byAIMS microbiology · 2026Article
- Microbial allies in skin trauma recovery: from immune modulation to engineered probiotic therapeutics.Burns & trauma · 2026Review
- Extended-Spectrum β-Lactamase-ProducingAntibiotics (Basel, Switzerland) · 2025Review
- Article
- Equine Asthma Is Characterised by Severity-Dependent Correlations Between Blood Neutrophil Cholesterol Content and NET Formation.European journal of immunology · 2025Article
- Update on antimicrobial peptides: key elements inThe Journal of general virology · 2025Review
- naRNA-LL37 composite DAMPs define sterile NETs as self-propagating drivers of inflammation.EMBO reports · 2024Article
- Between good and evil: Complexation of the human cathelicidin LL-37 with nucleic acids.Biophysical journal · 2024Review
- NETQUANT2: automated web-based quantification of neutrophil extracellular traps from fluorescence microscopy.Frontiers in immunology · 2024Article
- How Neutrophils Shape the Immune Response: Reassessing Their Multifaceted Role in Health and Disease.International journal of molecular sciences · 2023Review
- Neutrophil swarming: Is a good offense the best defense?iScience · 2023Review
- The Contribution of Antimicrobial Peptides to Immune Cell Function: A Review of Recent Advances.Pharmaceutics · 2023Review
- Review
25 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
14 authors at 10 institutions in 6 countries.
Funding
Abstract
Neutrophil extracellular traps (NETs) have been described as a fundamental innate immune defence mechanism. They consist of a nuclear DNA backbone associated with different antimicrobial peptides (AMPs) which are able to engulf and kill pathogens. The AMP LL-37, a member of the cathelicidin family, is highly present in NETs. However, the function of LL-37 within NETs is still unknown because it loses its antimicrobial activity when bound to DNA in the NETs. Using immunofluorescence microscopy, we demonstrate that NETs treated with LL-37 are distinctly more resistant to S. aureus nuclease degradation than nontreated NETs. Biochemical assays utilising a random LL-37-fragment library indicated that the blocking effect of LL-37 on nuclease activity is based on the cationic character of the AMP, which facilitates the binding to neutrophil DNA, thus protecting it from degradation by the nuclease. In good correlation to these data, the cationic AMPs human beta defensin-3 and human neutrophil peptide-1 showed similar protection of neutrophil-derived DNA against nuclease degradation. In conclusion, this study demonstrates a novel role of AMPs in host immune defence: beside its direct antimicrobial activity against various pathogens, cationic AMPs can stabilise neutrophil-derived DNA or NETs against bacterial nuclease degradation.
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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.