IDEAS home Printed from https://ideas.repec.org/a/nat/nature/v469y2011i7330d10.1038_nature09674.html
   My bibliography  Save this article

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

Author

Listed:
  • Bjoern O. Schroeder

    (Dr. Margarete Fischer-Bosch-Institute of Clinical Pharmacology
    University of Tübingen)

  • Zhihong Wu

    (University Hospital Schleswig-Holstein, Campus Kiel)

  • Sabine Nuding

    (Dr. Margarete Fischer-Bosch-Institute of Clinical Pharmacology
    University of Tübingen)

  • Sandra Groscurth

    (Max Planck Institute for Developmental Biology
    Present address: Bruker BioSpin AG, 8117 Fällanden, Switzerland.)

  • Moritz Marcinowski

    (Center for Integrated Protein Science Munich, Technische Universität München)

  • Julia Beisner

    (Dr. Margarete Fischer-Bosch-Institute of Clinical Pharmacology
    University of Tübingen)

  • 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
    University of Tübingen
    Robert Bosch Hospital)

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.

Suggested Citation

  • Bjoern O. Schroeder & Zhihong Wu & Sabine Nuding & Sandra Groscurth & Moritz Marcinowski & Julia Beisner & Johannes Buchner & Martin Schaller & Eduard F. Stange & Jan Wehkamp, 2011. "Reduction of disulphide bonds unmasks potent antimicrobial activity of human β-defensin 1," Nature, Nature, vol. 469(7330), pages 419-423, January.
    • Handle: RePEc:nat:nature:v:469:y:2011:i:7330:d:10.1038_nature09674
    DOI: 10.1038/nature09674
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/nature09674
    File Function: Abstract
    Download Restriction: Access to the full text of the articles in this series is restricted.
    File URL: https://libkey.io/10.1038/nature09674?utm_source=ideas
    LibKey link: if access is restricted and if your library uses this service, LibKey will redirect you to where you can use your library subscription to access this item
    ---><---

    As the access to this document is restricted, you may want to search for a different version of it.

    Citations

    Citations are extracted by the CitEc Project, subscribe to its RSS feed for this item.
    as


    Cited by:

    1. Soumitra Mohanty & Witchuda Kamolvit & Andrea Scheffschick & Anneli Björklund & Jonas Tovi & Alexander Espinosa & Kerstin Brismar & Thomas Nyström & Jens M. Schröder & Claes-Göran Östenson & Pontus As, 2022. "Diabetes downregulates the antimicrobial peptide psoriasin and increases E. coli burden in the urinary bladder," Nature Communications, Nature, vol. 13(1), pages 1-15, December.
    2. Alizee Lebeau & Diane Bruyere & Patrick Roncarati & Paul Peixoto & Eric Hervouet & Gael Cobraiville & Bernard Taminiau & Murielle Masson & Carmen Gallego & Gabriel Mazzucchelli & Nicolas Smargiasso & , 2022. "HPV infection alters vaginal microbiome through down-regulating host mucosal innate peptides used by Lactobacilli as amino acid sources," Nature Communications, Nature, vol. 13(1), pages 1-20, December.

    More about this item

    Statistics

    Access and download statistics

    Corrections

    All material on this site has been provided by the respective publishers and authors. You can help correct errors and omissions. When requesting a correction, please mention this item's handle: RePEc:nat:nature:v:469:y:2011:i:7330:d:10.1038_nature09674. See general information about how to correct material in RePEc.

    If you have authored this item and are not yet registered with RePEc, we encourage you to do it here. This allows to link your profile to this item. It also allows you to accept potential citations to this item that we are uncertain about.

    We have no bibliographic references for this item. You can help adding them by using this form .

    If you know of missing items citing this one, you can help us creating those links by adding the relevant references in the same way as above, for each refering item. If you are a registered author of this item, you may also want to check the "citations" tab in your RePEc Author Service profile, as there may be some citations waiting for confirmation.

    For technical questions regarding this item, or to correct its authors, title, abstract, bibliographic or download information, contact: Sonal Shukla or Springer Nature Abstracting and Indexing (email available below). General contact details of provider: http://www.nature.com .

    Please note that corrections may take a couple of weeks to filter through the various RePEc services.

    IDEAS is a RePEc service. RePEc uses bibliographic data supplied by the respective publishers.