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Galectin-3 Is a Target for Proteases Involved in the Virulence of Staphylococcus aureus
- Source :
- Infection and Immunity; May 2017, Vol. 85 Issue: 7
- Publication Year :
- 2017
-
Abstract
- ABSTRACTStaphylococcus aureusis a major cause of skin and soft tissue infection. The bacterium expresses four major proteases that are emerging as virulence factors: aureolysin (Aur), V8 protease (SspA), staphopain A (ScpA), and staphopain B (SspB). We hypothesized that human galectin-3, a β-galactoside-binding lectin involved in immune regulation and antimicrobial defense, is a target for these proteases and that proteolysis of galectin-3 is a novel immune evasion mechanism. Indeed, supernatants from laboratory strains and clinical isolates of S. aureuscaused galectin-3 degradation. Similar proteolytic capacities were found in Staphylococcus epidermidisisolates but not in Staphylococcus saprophyticus. Galectin-3-induced activation of the neutrophil NADPH oxidase was abrogated by bacterium-derived proteolysis of galectin-3, and SspB was identified as the major protease responsible. The impact of galectin-3 and protease expression on S. aureusvirulence was studied in a murine skin infection model. In galectin-3+/+mice, SspB-expressing S. aureuscaused larger lesions and resulted in higher bacterial loads than protease-lacking bacteria. No such difference in bacterial load or lesion size was detected in galectin-3−/−mice, which overall showed smaller lesion sizes than the galectin-3+/+animals. In conclusion, the staphylococcal protease SspB inactivates galectin-3, abrogating its stimulation of oxygen radical production in human neutrophils and increasing tissue damage during skin infection.
Details
- Language :
- English
- ISSN :
- 00199567 and 10985522
- Volume :
- 85
- Issue :
- 7
- Database :
- Supplemental Index
- Journal :
- Infection and Immunity
- Publication Type :
- Periodical
- Accession number :
- ejs42588804
- Full Text :
- https://doi.org/10.1128/IAI.00177-17