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Fibronectin binding by Propionibacterium acnes
Abstract:
Strains of Propionibacterium acnes, isolated from different kinds of orthopaedic and biomaterial-associated infections and from skin flora were shown to express binding of soluble as well as immobilized fibronectin. Among these 7 strains isolated from orthopaedic infections, 2 from breast prostheses, and 9 skin isolates, 2, 2, and 5 strains respectively bound immobilized fibronectin. The fibronectin binding was sensitive to protease and heat treatment, and was inhibited by a cell surface extract from one of the binding strains. In SDS-PAGE and autoradiography of cell surface extracts, a band corresponding to a MW of about 80 kD reacted with fibronectin and the 150 kD fragment of fibronectin. Binding to fibronectin and the 150 kD fragment of fibronectin could be inhibited with heparin. We thus present a first Fn binding protein of P. acnes, a surface exposed protein of 80 kD. None of the strains bound soluble collagen, and only one strain expressed weak binding of vitronectin and bone sialoprotein II.
Insights
Propionibacterium acnes, a common skin bacterium, can bind to fibronectin, a protein found in the body. Researchers identified an 80 kDa surface protein responsible for this binding, which may play a role in infections.
Area of Science:
- Microbiology
- Biochemistry
- Infectious Diseases
Background:
- Propionibacterium acnes (P. acnes) is implicated in various infections, including orthopaedic and biomaterial-associated ones.
- Understanding bacterial adhesion mechanisms is crucial for developing effective treatments and preventative strategies.
Purpose of the Study:
- To investigate the ability of P. acnes strains to bind fibronectin.
- To identify potential fibronectin-binding proteins on the surface of P. acnes.
Main Methods:
- Isolation and characterization of P. acnes strains from clinical samples and skin flora.
- Fibronectin binding assays using immobilized and soluble fibronectin.
- Protease and heat sensitivity assays.
- SDS-PAGE and autoradiography to identify binding proteins.
- Inhibition assays using cell surface extracts and heparin.
Main Results:
- Multiple P. acnes strains, particularly those from infections, demonstrated binding to immobilized fibronectin.
- A specific 80 kDa surface protein was identified as the primary fibronectin-binding molecule.
- Fibronectin binding was sensitive to protease and heat, and could be inhibited by heparin and cell surface extracts.
Conclusions:
- P. acnes possesses a surface-exposed 80 kDa protein that binds fibronectin.
- This fibronectin-binding protein may contribute to the pathogenesis of P. acnes infections.
- Further research into this protein could reveal new therapeutic targets.