ArticlePLoS pathogens2009
Protein C inhibitor--a novel antimicrobial agent.
Article in PLoS pathogens, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 42 citations in OpenAlex.
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- The host genetics affects gut microbiome diversity in Chinese depressed patients.Frontiers in genetics · 2022Article
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- In Vitro Evaluation of the Effects of Commercial Prebiotic GOS and FOS Products on Human Colonic Caco-2 Cells.Nutrients · 2020Article
- An ecoimmunological approach to study evolutionary and ancient links between coagulation, complement and Innate immunity.Virulence · 2018Article
- Serpin functions in host-pathogen interactions.PeerJ · 2018Article
- Immunohaemostasis: a new view on haemostasis during sepsis.Annals of intensive care · 2017Review
- Vertebrate TFPI-2 C-terminal peptides exert therapeutic applications against Gram-negative infections.BMC microbiology · 2016Article
- Proteomic analysis of egg white heparin-binding proteins: towards the identification of natural antibacterial molecules.Scientific reports · 2016Article
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- Proteolytic activation transforms heparin cofactor II into a host defense molecule.Journal of immunology (Baltimore, Md. : 1950) · 2013Article
- Ovalbumin-related protein X is a heparin-binding ov-serpin exhibiting antimicrobial activities.The Journal of biological chemistry · 2013Article
- Tissue factor pathway inhibitor 2 is found in skin and its C-terminal region encodes for antibacterial activity.PloS one · 2012Article
- Collagen VI encodes antimicrobial activity: novel innate host defense properties of the extracellular matrix.Journal of innate immunity · 2012Article
- Article
Corrections and comments
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Authors and funding
9 authors at 5 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protein C inhibitor (PCI) is a heparin-binding serine proteinase inhibitor belonging to the family of serpin proteins. Here we describe that PCI exerts broad antimicrobial activity against bacterial pathogens. This ability is mediated by the interaction of PCI with lipid membranes, which subsequently leads to their permeabilization. As shown by negative staining electron microscopy, treatment of Escherichia coli or Streptococcus pyogenes bacteria with PCI triggers membrane disruption followed by the efflux of bacterial cytosolic contents and bacterial killing. The antimicrobial activity of PCI is located to the heparin-binding site of the protein and a peptide spanning this region was found to mimic the antimicrobial activity of PCI, without causing lysis or membrane destruction of eukaryotic cells. Finally, we show that platelets can assemble PCI on their surface upon activation. As platelets are recruited to the site of a bacterial infection, these results may explain our finding that PCI levels are increased in tissue biopsies from patients suffering from necrotizing fasciitis caused by S. pyogenes. Taken together, our data describe a new function for PCI in innate immunity.
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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.