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

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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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Subject classification (UKÄ) – MANDATORY

  • Infectious Medicine
  • Dermatology and Venereal Diseases
Original languageEnglish
Pages (from-to)708-713
JournalMolecular Microbiology
Volume39
Issue number3
Publication statusPublished - 2001
Publication categoryResearch
Peer-reviewedYes