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Dermatan sulphate is released by proteinases of common pathogenic bacteria and inactivates antibacterial alpha-defensin

Schmidtchen, Artur LU ; Frick, Inga-Maria LU and Björck, Lars LU (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.
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author
organization
publishing date
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
2008-07-14 10:59:24
date last changed
2018-04-08 03:33:22
@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},
  volume       = {39},
  year         = {2001},
}