Work

Dermatan sulphate is released by proteinases of common pathogenic bacteria and inactivates antibacterial α‐defensin

Year: 2001

Type: article

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.

Source: Molecular Microbiology

DOI: 10.1046/j.1365-2958.2001.02251.x

Authors: Artur Schmidtchen, Inga‐Maria Frick, Lars Björck

Institutions: Lund University, Skåne University Hospital

Language: English

Topic: Antimicrobial Peptides and Activities

Subfield: Microbiology

Field: Immunology and Microbiology

Domain: Life Sciences

SDG: Good health and well-being

Open Access status: bronze

Funders: Kungliga Fysiografiska Sällskapet i Lund, Active Biotech, Medical Research Council