ArticleThe Journal of biological chemistry2014
Antimicrobial effects of helix D-derived peptides of human antithrombin III.
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 13 papers.
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Who cites it
13 citing papers in PubMed, 20 citations in OpenAlex.
- Identifying dynamic antithrombin Ⅲ trajectories to predict clinical outcomes in intra-abdominal sepsis.Journal of intensive medicine · 2026Article
- IFN-Inducible SerpinA5 Triggers Antiviral Immunity by Regulating STAT1 Phosphorylation and Nuclear Translocation.International journal of molecular sciences · 2023Article
- 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
- The host genetics affects gut microbiome diversity in Chinese depressed patients.Frontiers in genetics · 2022Article
- Antithrombin and Its Role in Host Defense and Inflammation.International journal of molecular sciences · 2021Review
- Anticoagulant and signaling functions of antithrombin.Journal of thrombosis and haemostasis : JTH · 2020Review
- Antithrombin: An anticoagulant, anti-inflammatory and antibacterial serpin.Journal of thrombosis and haemostasis : JTH · 2020Article
- Antimicrobial Peptide JH-3 Effectively Kills Salmonella enterica Serovar Typhimurium Strain CVCC541 and Reduces Its Pathogenicity in Mice.Probiotics and antimicrobial proteins · 2019Article
- An ecoimmunological approach to study evolutionary and ancient links between coagulation, complement and Innate immunity.Virulence · 2018Article
- Auxiliary activation of the complement system and its importance for the pathophysiology of clinical conditions.Seminars in immunopathology · 2018Review
- Immunohaemostasis: a new view on haemostasis during sepsis.Annals of intensive care · 2017Review
- Aggregation of thrombin-derived C-terminal fragments as a previously undisclosed host defense mechanism.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Vertebrate TFPI-2 C-terminal peptides exert therapeutic applications against Gram-negative infections.BMC microbiology · 2016Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Antithrombin III (ATIII) is a key antiproteinase involved in blood coagulation. Previous investigations have shown that ATIII is degraded by Staphylococcus aureus V8 protease, leading to release of heparin binding fragments derived from its D helix. As heparin binding and antimicrobial activity of peptides frequently overlap, we here set out to explore possible antibacterial effects of intact and degraded ATIII. In contrast to intact ATIII, the results showed that extensive degradation of the molecule yielded fragments with antimicrobial activity. Correspondingly, the heparin-binding, helix D-derived, peptide FFFAKLNCRLYRKANKSSKLV (FFF21) of human ATIII, was found to be antimicrobial against particularly the Gram-negative bacteria Escherichia coli and Pseudomonas aeruginosa. Fluorescence microscopy and electron microscopy studies demonstrated that FFF21 binds to and permeabilizes bacterial membranes. Analogously, FFF21 was found to induce membrane leakage of model anionic liposomes. In vivo, FFF21 significantly reduced P. aeruginosa infection in mice. Additionally, FFF21 displayed anti-endotoxic effects in vitro. Taken together, our results suggest novel roles for ATIII-derived peptide fragments in host defense.
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