Dermatan sulphate is released by proteinases of common pathogenic bacteria and inactivates antibacterial alpha-defensin
(2001) In Molecular Microbiology 39(3). p.708-713- Abstract
- Defensins represent an evolutionarily conserved group of small peptides with potent antibacterial activities. We report here that extracellular proteinases secreted by the human pathogens Pseudomonas aeruginosa, Enterococcus faecalis and Streptococcus pyogenes release dermatan sulphate by degrading dermatan sulphate-containing proteoglycans, such as decorin. Dermatan sulphate was found to bind to neutrophil-derived alpha-defensin, and this binding completely neutralized its bactericidal activity. During infection, proteoglycan degradation and release of dermatan sulphate may therefore represent a previously unknown virulence mechanism, which could serve as a target for novel antibacterial strategies.
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1121015
- author
- Schmidtchen, Artur LU ; Frick, Inga-Maria LU and Björck, Lars LU
- organization
- publishing date
- 2001
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Molecular Microbiology
- volume
- 39
- issue
- 3
- pages
- 708 - 713
- publisher
- Wiley-Blackwell
- external identifiers
-
- pmid:11169110
- scopus:0035131955
- ISSN
- 1365-2958
- DOI
- 10.1046/j.1365-2958.2001.02251.x
- language
- English
- LU publication?
- yes
- id
- 8902c75e-53f7-4c3e-b6f1-86f3eac31287 (old id 1121015)
- date added to LUP
- 2016-04-01 11:47:40
- date last changed
- 2022-02-03 05:13:21
@article{8902c75e-53f7-4c3e-b6f1-86f3eac31287, abstract = {{Defensins represent an evolutionarily conserved group of small peptides with potent antibacterial activities. We report here that extracellular proteinases secreted by the human pathogens Pseudomonas aeruginosa, Enterococcus faecalis and Streptococcus pyogenes release dermatan sulphate by degrading dermatan sulphate-containing proteoglycans, such as decorin. Dermatan sulphate was found to bind to neutrophil-derived alpha-defensin, and this binding completely neutralized its bactericidal activity. During infection, proteoglycan degradation and release of dermatan sulphate may therefore represent a previously unknown virulence mechanism, which could serve as a target for novel antibacterial strategies.}}, author = {{Schmidtchen, Artur and Frick, Inga-Maria and Björck, Lars}}, issn = {{1365-2958}}, language = {{eng}}, number = {{3}}, pages = {{708--713}}, publisher = {{Wiley-Blackwell}}, series = {{Molecular Microbiology}}, title = {{Dermatan sulphate is released by proteinases of common pathogenic bacteria and inactivates antibacterial alpha-defensin}}, url = {{http://dx.doi.org/10.1046/j.1365-2958.2001.02251.x}}, doi = {{10.1046/j.1365-2958.2001.02251.x}}, volume = {{39}}, year = {{2001}}, }