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Updated: Sep 22, 2026

Invasion of Human Cells by a Bacterial Pathogen
Published on: March 21, 2011
Staphylococcus saprophyticus hemagglutinin binds fibronectin
1Institut für Medizinische Mikrobiologie, Medizinische Universität zu Lübeck, Germany.
Abstract:
Attachment of microorganisms to host tissue is regarded as an important step in the pathogenesis of infections. Staphylococcus saprophyticus adheres to various epithelial cells and hemagglutinates sheep erythrocytes. The hemagglutinin has been identified, but a human target for this surface protein is still not known. In our report, we show that hemagglutinating strains of S. saprophyticus bind to immobilized fibronectin, whereas nonhemagglutinating strains do not. Bacterial binding was inhibited by antibody to the hemagglutinin but not by antibody to Ssp, another surface protein of S. saprophyticus. The purified hemagglutinin but not other surface proteins bound biotin-labeled fibronectin. Binding was saturable and could be inhibited by unbound hemagglutinin, unlabeled fibronectin, and by antibody to the hemagglutinin. We thus conclude that the hemagglutinin of S. saprophyticus may act as a fibronectin receptor in the human host. Heparin, the D3 peptide, or Arg-Gly-Asp-Ser (RGDS) containing peptides did not inhibit binding of fibronectin to the hemagglutinin, indicating that the binding site is different from that of Staphylococcus aureus or Treponema pallidum.
Insights
Staphylococcus saprophyticus hemagglutinin binds to fibronectin, a human protein. This suggests the hemagglutinin may function as a fibronectin receptor, aiding bacterial attachment during infections.
Area of Science:
- Microbiology
- Pathogenesis
- Molecular Biology
Background:
- Bacterial attachment to host tissues is crucial for infection development.
- Staphylococcus saprophyticus adheres to epithelial cells and causes hemagglutination.
- The specific human target for S. saprophyticus hemagglutinin remains unidentified.
Purpose of the Study:
- To identify the human target of Staphylococcus saprophyticus hemagglutinin.
- To investigate the role of hemagglutinin in bacterial adhesion to host tissues.
Main Methods:
- Testing the binding of S. saprophyticus strains to immobilized fibronectin.
- Using antibodies to inhibit bacterial binding and identify involved surface proteins.
- Assessing the binding of purified hemagglutinin to fibronectin.
Main Results:
- Hemagglutinating S. saprophyticus strains bind to fibronectin; non-hemagglutinating strains do not.
- Antibody against hemagglutinin inhibited binding, while antibody against Ssp did not.
- Purified hemagglutinin specifically bound fibronectin in a saturable manner.
Conclusions:
- The hemagglutinin of S. saprophyticus likely functions as a fibronectin receptor in humans.
- This interaction may mediate bacterial adherence to host tissues.
- The fibronectin binding site on hemagglutinin differs from that of other pathogens.
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