Reduction of disulphide bonds unmasks potent antimicrobial activity of human β-defensin 1

Bjoern O. Schroeder, Zhihong Wu, Sabine Nuding, Sandra Groscurth, Moritz Marcinowski, Julia Beisner, Johannes Buchner, Martin Schaller, Eduard F. Stange and Jan Wehkamp ()
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Bjoern O. Schroeder: Dr. Margarete Fischer-Bosch-Institute of Clinical Pharmacology
Zhihong Wu: University Hospital Schleswig-Holstein, Campus Kiel
Sabine Nuding: Dr. Margarete Fischer-Bosch-Institute of Clinical Pharmacology
Sandra Groscurth: Max Planck Institute for Developmental Biology
Moritz Marcinowski: Center for Integrated Protein Science Munich, Technische Universität München
Julia Beisner: Dr. Margarete Fischer-Bosch-Institute of Clinical Pharmacology
Johannes Buchner: Center for Integrated Protein Science Munich, Technische Universität München
Martin Schaller: University Hospital Tübingen
Eduard F. Stange: Robert Bosch Hospital
Jan Wehkamp: Dr. Margarete Fischer-Bosch-Institute of Clinical Pharmacology

Nature, 2011, vol. 469, issue 7330, 419-423

Abstract: Human β-defensin 1 shows its true colours Defensins are key effector molecules of innate immunity, protecting the host from infectious microbes and shaping the composition of the microbiota at mucosal surfaces. Human β-defensin 1 (hBD-1) is one of the most prominent peptides of its class and is expressed by virtually all human epithelial sites, but previous work suggested that it has low antibiotic activity when compared with other defensins. Jan Wehkamp and colleagues now show that in reducing conditions similar to those found in the distal colon, hBD-1 exhibits potent antimicrobial action against the potential pathogens Candia albicans, Bifidobacterium and Lactobacillus species. In vitro evidence points to thioredoxin as the reducing agent most likely to unmask hBD-1's antimicrobial activity in the intestinal epithelium.

Date: 2011
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DOI: 10.1038/nature09674

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