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Binding to human extracellular matrix by Neisseria meningitidis
T Eberhard1, R Virkola, T Korhonen
1Department of Laboratory Medicine, Karolinska Hospital, Stockholm, Sweden.
Infection and Immunity
|April 7, 1998
Summary
Neisseria meningitidis strains adhere to extracellular matrix components like fibronectin and collagen. Healthy carrier strains showed better adhesion than patient isolates, binding to a novel site on fibronectin.
Area of Science:
- Microbiology
- Bacterial Pathogenesis
- Extracellular Matrix Biology
Background:
- Neisseria meningitidis is a significant human pathogen.
- Bacterial adhesion to host tissues is crucial for colonization and infection.
- The interaction of N. meningitidis with the extracellular matrix (ECM) is not fully understood.
Purpose of the Study:
- To investigate the adhesion properties of Neisseria meningitidis to various components of the extracellular matrix.
- To identify specific ECM molecules and bacterial binding sites involved in this interaction.
Main Methods:
- Testing adhesion of N. meningitidis strains to subendothelial ECM and purified fibronectin and collagens (types I, III, V).
- Comparing adhesion levels between strains isolated from healthy carriers and patients.
- Mapping the bacterial binding site on fibronectin using specific domains.
Main Results:
- Most N. meningitidis strains adhered to subendothelial ECM, fibronectin, and types I, III, and V collagen.
- Strains isolated from healthy carriers exhibited significantly higher adhesion than those from patients.
- The bacterial binding site was localized to the central 75-kDa cell-binding domain of fibronectin, a previously undescribed interaction.
Conclusions:
- Neisseria meningitidis possesses the ability to bind to key extracellular matrix components.
- Differences in adhesion capabilities may distinguish commensal and pathogenic N. meningitidis strains.
- The central cell-binding domain of fibronectin represents a novel bacterial interaction site for N. meningitidis.