ArticleThe Journal of biological chemistry2014
Actin enables the antimicrobial action of LL-37 peptide in the presence of microbial proteases.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
What it found
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Who cites it
12 citing papers in PubMed, 20 citations in OpenAlex.
- Bioactive peptides in Endodontic infections: The Good, The Bad, and The Ugly.Probiotics and antimicrobial proteins · 2026Review
- Anti-Fibrotic Activity of an Antimicrobial Peptide in a Drosophila Model.Journal of innate immunity · 2021Article
- Cofilin-1-induced actin reorganization in stored platelets.Transfusion · 2020Article
- Activation of vitamin D in the gingival epithelium and its role in gingival inflammation and alveolar bone loss.Journal of periodontal research · 2019Article
- Interactions of histatin-3 and histatin-5 with actin.BMC biochemistry · 2017Article
- Article
- Actin and DNA Protect Histones from Degradation by Bacterial Proteases but Inhibit Their Antimicrobial Activity.Frontiers in microbiology · 2016Article
- Antimicrobial peptides in 2014.Pharmaceuticals (Basel, Switzerland) · 2015Review
- Mechanisms of Antimicrobial Peptide Resistance in Gram-Negative Bacteria.Antibiotics (Basel, Switzerland) · 2015Article
- Polymicrobial synergy and dysbiosis in inflammatory disease.Trends in molecular medicine · 2015Review
- Identification and characterization of fusolisin, the Fusobacterium nucleatum autotransporter serine protease.PloS one · 2014Article
- Article
Corrections and comments
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Host defense peptides play an important host-protective role by their microcidal action, immunomodulatory functions, and tissue repair activities. Proteolysis is a common strategy of pathogens used to neutralize host defense peptides. Here, we show that actin, the most abundant structural protein in eukaryotes, binds the LL-37 host defense peptide, protects it from degradation by the proteases of Pseudomonas aeruginosa and Porphyromonas gingivalis, and enables its antimicrobial activity despite the presence of the proteases. Co-localization of LL-37 with extracellular actin was observed in necrotized regions of samples from oral lesions. Competition assays, cross-linking experiments, limited proteolysis, and mass spectrometry revealed that LL-37 binds by specific hydrophobic interactions to the His-40-Lys-50 segment of actin, located in the DNase I binding loop. The integrity of the binding site of both LL-37 and actin is a prerequisite to the binding. Our results demonstrate that actin, presumably released by dead cells and abundant in infected sites, might be utilized by the immune system to enhance spatio-temporal immunity in an attempt to arrest infection and control inflammation.
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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.