ArticlePloS one2009
Antimicrobial activity of human prion protein is mediated by its N-terminal region.
Article in PloS one, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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Who cites it
41 citing papers in PubMed, 88 citations in OpenAlex.
- Encrypted immunity mediated by peptides.PLoS biology · 2026Review
- The Many Lives of a Single Sequence: Functional Plasticity Through Amyloid Polymorphism.Sub-cellular biochemistry · 2026Review
- Prion Protein Endoproteolysis: Cleavage Sites, Mechanisms and Connections to Prion Disease.Journal of neurochemistry · 2025Review
- Unveiling the multifaceted potential of amyloid fibrils: from pathogenic myths to biotechnological marvels.Biophysical reviews · 2024Review
- MAD-microbial (origin of) Alzheimer's disease hypothesis: from infection and the antimicrobial response to disruption of key copper-based systems.Frontiers in neuroscience · 2024Review
- Selective protein aggregation confines and inhibits endotoxins in wounds: Linking host defense to amyloid formation.iScience · 2023Article
- Testing Antimicrobial Properties of Selected Short Amyloids.International journal of molecular sciences · 2023Article
- Amyloid peptides with antimicrobial and/or microbial agglutination activity.Applied microbiology and biotechnology · 2022Review
- Zn(II) binding to pramlintide results in a structural kink, fibril formation and antifungal activity.Scientific reports · 2022Article
- Repurposing of intestinal defensins as multi-target, dual-function amyloid inhibitorsChemical science · 2022Article
- pH- and concentration-dependent supramolecular assembly of a fungal defensin plectasin variant into helical non-amyloid fibrils.Nature communications · 2022Article
- Mammals' humoral immune proteins and peptides targeting the bacterial envelope: from natural protection to therapeutic applications against multidrug-resistant Gram-negatives.Biological reviews of the Cambridge Philosophical Society · 2022Review
- Unravelling the antimicrobial activity of peptide hydrogel systems: current and future perspectives.Soft matter · 2021Review
- Parkinson's Disease: A Prionopathy?International journal of molecular sciences · 2021Review
- Antimicrobial α-defensins as multi-target inhibitors against amyloid formation and microbial infection.Chemical science · 2021Article
- Neurometals in the Pathogenesis of Prion Diseases.International journal of molecular sciences · 2021Review
- The amphibian antimicrobial peptide uperin 3.5 is a cross-α/cross-β chameleon functional amyloid.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Peptide Self-Assembly Is Linked to Antibacterial, but Not Antifungal, Activity of Histatin 5 Derivatives.mSphere · 2020Article
- Prion protein PrP nucleic acid binding and mobilization implicates retroelements as the replicative component of transmissible spongiform encephalopathy.Archives of virology · 2020Review
- Functional Reciprocity of Amyloids and Antimicrobial Peptides: Rethinking the Role of Supramolecular Assembly in Host Defense, Immune Activation, and Inflammation.Frontiers in immunology · 2020Review
Corrections and comments
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Authors and funding
9 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundCellular prion-related protein (PrP(c)) is a cell-surface protein that is ubiquitously expressed in the human body. The multifunctionality of PrP(c), and presence of an exposed cationic and heparin-binding N-terminus, a feature characterizing many antimicrobial peptides, made us hypothesize that PrP(c) could exert antimicrobial activity. METHODOLOGY AND PRINCIPAL
findingsIntact recombinant PrP exerted antibacterial and antifungal effects at normal and low pH. Studies employing recombinant PrP and N- and C-terminally truncated variants, as well as overlapping peptide 20mers, demonstrated that the antimicrobial activity is mediated by the unstructured N-terminal part of the protein. Synthetic peptides of the N-terminus of PrP killed the Gram-negative bacteria Escherichia coli and Pseudomonas aeruginosa, and the Gram-positive Bacillus subtilis and Staphylococcus aureus, as well as the fungus Candida parapsilosis. Fluorescence studies of peptide-treated bacteria, paired with analysis of peptide effects on liposomes, showed that the peptides exerted membrane-breaking effects similar to those seen after treatment with the "classical" human antimicrobial peptide LL-37. In contrast to LL-37, however, no marked helix induction was detected for the PrP-derived peptides in presence of negatively charged (bacteria-mimicking) liposomes. PrP furthermore showed an inducible expression during wounding of human skin ex vivo and in vivo, as well as stimulation of keratinocytes with TGF-alpha in vitro.
conclusionsThe demonstration of an antimicrobial activity of PrP, localisation of its activity to the N-terminal and heparin-binding region, combined with results showing an increased expression of PrP during wounding, indicate that PrPs could have a previously undisclosed role in host defense.
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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.