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Waking the wimp: Redox-modulation activates human beta-defensin 1
Dr. Margarete Fischer-Bosch-Institute of Clinical Pharmacology; Stuttgart and University of Tübingen; Tübingen, Germany.ORCID iD: 0000-0002-6716-8284
2011 (English)In: Gut microbes, ISSN 1949-0976, E-ISSN 1949-0984, Vol. 2, no 4, p. 262-266Article in journal (Refereed) Published
Abstract [en]

Antimicrobial peptides are key players of the innate immune system and form a primary barrier against infection by microorganisms. In humans, several classes of antimicrobial peptides are produced, including the defensins. These small, cationic peptides show broad spectrum antimicrobial activity against bacteria, some fungi and some viruses. Defensins are characterized by six conserved cysteine residues which are connected via three disulphide bridges. Depending on the pattern of connectivity, human defensins are either classified as α- or β-defensins. Human β-defensin 1 (hBD-1) is constitutively expressed by epithelia, but in comparison with other antimicrobial peptides the antimicrobial activity of hBD-1 was comparably low. We recently found that after reduction of hBD-1's three disulphide bonds its antimicrobial activity is strongly enhanced. Reduction can be either performed by a reducing environment, as it is present in parts of the human intestine, the oral cavity and other locations, or enzymatically by the thioredoxin-system, which is one of the major redox regulators. Reduced hBD-1 is able to kill Gram-positive anaerobic bacteria of the human normal flora as well as an opportunistic pathogenic fungus, whereas the oxidized peptide does not show activity against these microorganisms. Herein we provide additional data about reduced hBD-1 and discuss the biological context of our findings.

Place, publisher, year, edition, pages
Taylor & Francis, 2011. Vol. 2, no 4, p. 262-266
Keywords [en]
antimicrobial peptides, human beta defensin 1, disulphide bridges, thioredoxin, redox-modulation, mucosal host defence, intestinal microbiota, commensal bacteria, innate immunity
National Category
Immunology Microbiology
Identifiers
URN: urn:nbn:se:umu:diva-166029DOI: 10.4161/gmic.2.4.17692PubMedID: 21983064Scopus ID: 2-s2.0-80054061296OAI: oai:DiVA.org:umu-166029DiVA, id: diva2:1376358
Note

Addendum to: Schroeder BO, et al. Reduction of disulphide bonds unmasks potent antimicrobial activity of human beta-defensin 1. Nature 2011; 469: 419–23; DOI: 10.1038/nature09674

Available from: 2019-12-09 Created: 2019-12-09 Last updated: 2019-12-13Bibliographically approved

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