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Treponema pallidum receptor binding proteins interact with fibronectin
The Journal of Experimental Medicine
|June 1, 1983
Summary
Virulent *T. pallidum* readily binds host fibronectin, mediating tip-oriented attachment to host cells. This specific interaction involves outer envelope proteins and is crucial for *T. pallidum* parasitism.
Area of Science:
- Microbiology
- Cell Biology
- Biochemistry
Background:
- *T. pallidum* is a pathogenic bacterium that causes syphilis.
- Understanding the mechanisms of *T. pallidum* adherence to host cells is crucial for developing effective treatments.
Purpose of the Study:
- To investigate the interaction between *T. pallidum* and host plasma proteins.
- To elucidate the role of fibronectin in *T. pallidum* attachment to host cells.
Main Methods:
- Analysis of plasma proteins bound to *T. pallidum* surfaces.
- Western blotting using antifibronectin serum.
- Assessing *T. pallidum* attachment to fibronectin-coated surfaces and HEp-2 cells.
- Investigating the role of outer envelope proteins.
Main Results:
- Virulent *T. pallidum* avidly binds fibronectin from plasma.
- Specific, tip-oriented attachment of *T. pallidum* to fibronectin was observed.
- Three outer envelope proteins of *T. pallidum* showed avid association with fibronectin.
- Avirulent *T. phagedenis* biotype Reiter did not show similar binding.
Conclusions:
- Surface fibronectin mediates the specific, tip-oriented attachment of *T. pallidum* to host cells.
- This interaction is mediated by a receptor-ligand mechanism involving *T. pallidum* outer envelope proteins.
- Fibronectin binding is a key factor in *T. pallidum* parasitism.