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

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.

journal_name

Mol Microbiol

journal_title

Molecular microbiology

authors

Schmidtchen A,Frick IM,Björck L

doi

10.1046/j.1365-2958.2001.02251.x

subject

Has Abstract

pub_date

2001-02-01 00:00:00

pages

708-13

issue

3

eissn

0950-382X

issn

1365-2958

pii

mmi2251

journal_volume

39

pub_type

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