Journal article
Beta toxin catalyzes formation of nucleoprotein matrix in staphylococcal biofilms
Proceedings of the National Academy of Sciences - PNAS, Vol.107(32), pp.14407-14412
08/10/2010
DOI: 10.1073/pnas.0911032107
PMCID: PMC2922554
PMID: 20660751
Abstract
Biofilms are surface-associated communities of microbes encompassed by an extracellular matrix. It is estimated that 80% of all bacterial infections involve biofilm formation, but the structure and regulation of biofilms are incompletely understood. Extracellular DNA (eDNA) is a major structural component in many biofilms of the pathogenic bacterium
Staphylococcus aureus
, but its role is enigmatic. Here, we demonstrate that beta toxin, a neutral sphingomyelinase and a virulence factor of
S. aureus
, forms covalent cross-links to itself in the presence of DNA (we refer to this as biofilm ligase activity, independent of sphingomyelinase activity) producing an insoluble nucleoprotein matrix in vitro. Furthermore, we show that beta toxin strongly stimulates biofilm formation in vivo as demonstrated by a role in causation of infectious endocarditis in a rabbit model. Together, these results suggest that beta toxin cross-linking in the presence of eDNA assists in forming the skeletal framework upon which staphylococcal biofilms are established.
Details
- Title: Subtitle
- Beta toxin catalyzes formation of nucleoprotein matrix in staphylococcal biofilms
- Creators
- Medora J Huseby - Biochemistry, Molecular Biology, and Biophysics andAndrew C Kruse - Biochemistry, Molecular Biology, and Biophysics andJeff Digre - Biochemistry, Molecular Biology, and Biophysics andPetra L Kohler - University of MinnesotaJillian A Vocke - University of MinnesotaEthan E Mann - University of Nebraska Medical CenterKenneth W Bayles - University of Nebraska Medical CenterGregory A Bohach - University of IdahoPatrick M Schlievert - University of MinnesotaDouglas H Ohlendorf - Biochemistry, Molecular Biology, and Biophysics andCathleen A Earhart - Biochemistry, Molecular Biology, and Biophysics and
- Resource Type
- Journal article
- Publication Details
- Proceedings of the National Academy of Sciences - PNAS, Vol.107(32), pp.14407-14412
- DOI
- 10.1073/pnas.0911032107
- PMID
- 20660751
- PMCID
- PMC2922554
- NLM abbreviation
- Proc Natl Acad Sci U S A
- ISSN
- 0027-8424
- eISSN
- 1091-6490
- Publisher
- National Academy of Sciences
- Language
- English
- Date published
- 08/10/2010
- Academic Unit
- Microbiology and Immunology; Internal Medicine
- Record Identifier
- 9984001146402771
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