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Identification of a fibronectin binding protein from Streptococcus mutans.
1Graduate Institute of Microbiology, College of Medicine, National Taiwan University, Taipei, Taiwan, Republic of China. chiajs@ha.mc.edu.tw
Infection and Immunity
|March 18, 2000
Summary
Researchers identified a Streptococcus mutans protein, FBP-130, that binds fibronectin (Fn) and mediates bacterial adherence to endothelial cells, impacting infective endocarditis pathogenesis.
Area of Science:
- Microbiology
- Pathogenesis
- Extracellular Matrix Interactions
Background:
- Viridans streptococci interactions with the extracellular matrix (ECM) are crucial in infective endocarditis.
- Streptococcus mutans utilizes ECM components for adhesion and colonization.
Purpose of the Study:
- To identify and characterize a fibronectin (Fn)-binding protein from Streptococcus mutans.
- To elucidate the role of this protein in bacterial adherence to host cells.
Main Methods:
- Enzyme-linked immunosorbent assay (ELISA) to assess Fn binding.
- Far-Western immunoblotting to detect Fn-binding proteins.
- Affinity chromatography for protein purification.
- In vitro adherence assays using endothelial cells.
Main Results:
- A 130 kDa protein (FBP-130) from S. mutans was identified as a specific fibronectin binder.
- FBP-130 is present in both cell wall and extracellular fractions, with higher abundance in the cell wall.
- Purified FBP-130 and anti-FBP antibodies inhibited S. mutans adherence to Fn and endothelial cells.
Conclusions:
- FBP-130 mediates the specific adherence of Streptococcus mutans to fibronectin and endothelial cells.
- This mechanism is significant in the pathogenesis of infective endocarditis.
- Viridans streptococci employ diverse strategies for ECM interaction.