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Published on: June 11, 2015
The role of streptococcal plasmin(ogen) binding in infective endocarditis
1Department of Biological and Biomedical Sciences, Glasgow Caledonian University, Glasgow, G4 0BA, UK.
Abstract:
The ability of viridans group streptococci (VGS) to bind human plasminogen and its subsequent activation into plasmin may contribute to the pathogenesis of streptococcal endocarditis. The increased proteolytic activity acquired through cell-bound plasmin may lead to a decreased stability of the streptococcal vegetation and possible embolisation. Twenty-two infective endocarditis isolates and 16 non-infective endocarditis isolates were screened for their ability to bind plasminogen through the quantification of its active form plasmin, using the colorimetric substrate D-Val-Leu-Lys p-nitroanilide. The species of the VGS assessed expressed a universal capability to bind human plasminogen, although they did so with differing affinities and independently of the site of isolation.
Insights
Viridans group streptococci (VGS) universally bind human plasminogen. This interaction may enhance streptococcal endocarditis virulence by increasing proteolytic activity and vegetation instability, potentially leading to embolisation.
Area of Science:
- Microbiology
- Infectious Diseases
- Cardiovascular Pathophysiology
Background:
- Viridans group streptococci (VGS) are implicated in infective endocarditis.
- Bacterial interaction with host plasminogen may influence disease pathogenesis.
Purpose of the Study:
- To investigate the capacity of VGS to bind human plasminogen.
- To determine if plasminogen binding correlates with infective endocarditis.
Main Methods:
- Screening of 22 infective endocarditis and 16 non-infective endocarditis VGS isolates.
- Quantification of bound plasmin (active form of plasminogen) using a colorimetric assay.
Main Results:
- All assessed VGS species demonstrated the ability to bind human plasminogen.
- Plasminogen binding affinity varied among isolates.
- Binding capability was independent of the isolation source (infective vs. non-infective endocarditis).
Conclusions:
- VGS possess a universal capacity for human plasminogen binding.
- This interaction may contribute to the pathogenesis of streptococcal endocarditis through enhanced proteolytic activity and vegetation instability.
Related Concept Videos
Endocarditis I: Introduction
Determinants of Bacterial Pathogenicity and Virulence
Endocarditis II: Clinical Features of Infective Endocarditis
Streptococcal Pharyngitis
Endocarditis III: Medical Management
Endocarditis IV: Nursing Management

