Change search
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf
Paneth cell α-defensin 6 (HD-6) is an antimicrobial peptide
Dr Margarete Fischer-Bosch-Institute of Clinical Pharmacology, Stuttgart, Germany; University of Tuebingen, Tuebingen, Germany; Department of Microbiology and Immunology, School of Medicine, University of California, Davis, California, USA; Present address: Wallenberg Laboratory, University of Gothenburg, Gothenburg, Sweden.ORCID iD: 0000-0002-6716-8284
Show others and affiliations
2015 (English)In: Mucosal Immunology, ISSN 1933-0219, E-ISSN 1935-3456, Vol. 8, no 3, p. 661-671Article in journal (Refereed) Published
Abstract [en]

Defensins protect human barriers from commensal and pathogenic microorganisms. Human α-defensin 6 (HD-6) is produced exclusively by small intestinal Paneth cells but, in contrast to other antimicrobial peptides (AMPs) for HD-6, no direct antibacterial killing activity has been detected so far. Herein, we systematically tested how environmental factors, like pH and reducing conditions, affect antimicrobial activity of different defensins against anaerobic bacteria of the human intestinal microbiota. Remarkably, by mimicking the intestinal milieu we detected for the first time antibacterial activity of HD-6. Activity was observed against anaerobic gut commensals but not against some pathogenic strains. Antibiotic activity was attributable to the reduced peptide and independent of free cysteines or a conserved histidine residue. Furthermore, the oxidoreductase thioredoxin, which is also expressed in Paneth cells, is able to reduce a truncated physiological variant of HD-6. Ultrastructural analyses revealed that reduced HD-6 causes disintegration of cytoplasmic structures and alterations in the bacterial cell envelope, while maintaining extracellular net-like structures. We conclude that HD-6 is an antimicrobial peptide. Our data suggest two distinct antimicrobial mechanisms by one peptide: HD-6 kills specific microbes depending on the local environmental conditions, whereas known microbial trapping by extracellular net structures is independent of the reducing milieu.

Place, publisher, year, edition, pages
Nature Publishing Group, 2015. Vol. 8, no 3, p. 661-671
National Category
Microbiology Immunology Gastroenterology and Hepatology
Identifiers
URN: urn:nbn:se:umu:diva-166025DOI: 10.1038/mi.2014.100ISI: 000354085700020PubMedID: 25354318OAI: oai:DiVA.org:umu-166025DiVA, id: diva2:1376367
Available from: 2019-12-09 Created: 2019-12-09 Last updated: 2019-12-11Bibliographically approved

Open Access in DiVA

fulltext(3918 kB)45 downloads
File information
File name FULLTEXT01.pdfFile size 3918 kBChecksum SHA-512
89379f4e64264ca4ed0033f16eb23c120a4d3ebca9bcfb6cd57e8c9573c87396c791d58b4a0bdfbbe7594958711e76380e05a81f92ab2a1d63fb367f9263429c
Type fulltextMimetype application/pdf

Other links

Publisher's full textPubMed

Search in DiVA

By author/editor
Schröder, Björn
In the same journal
Mucosal Immunology
MicrobiologyImmunologyGastroenterology and Hepatology

Search outside of DiVA

GoogleGoogle Scholar
Total: 45 downloads
The number of downloads is the sum of all downloads of full texts. It may include eg previous versions that are now no longer available

doi
pubmed
urn-nbn

Altmetric score

doi
pubmed
urn-nbn
Total: 49 hits
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf