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Plasminogen binding and activation by Mycoplasma fermentans
A Yavlovich1, A A Higazi, S Rottem
1Department of Membrane and Ultrastructure Research, The Hebrew University-Hadassah Medical School, Jerusalem, Israel.
Infection and Immunity
|March 20, 2001
Summary
Mycoplasma fermentans binds plasminogen, enhancing its activation to plasmin by urokinase-type plasminogen activator (uPA) and promoting host cell invasion.
Area of Science:
- Microbiology
- Biochemistry
- Molecular Biology
Background:
- Mycoplasma fermentans is a pathogen known to interact with host cells.
- Plasminogen is a key protein in the fibrinolytic system, involved in tissue remodeling and degradation.
Purpose of the Study:
- To investigate the binding of plasminogen to Mycoplasma fermentans.
- To determine the functional consequences of plasminogen binding on bacterial invasion and plasminogen activation.
Main Methods:
- Immunoblot analysis and binding assays using iodine-labeled plasminogen.
- Scatchard analysis to characterize binding kinetics.
- Ligand blotting to identify plasminogen-binding proteins.
- Assays to measure plasminogen activation and bacterial invasion.
Main Results:
- Mycoplasma fermentans binds plasminogen with high affinity (kd 0.5 microM) and lower affinity (kd 7.5 microM).
- Two plasminogen-binding proteins of approximately 32 and 55 kDa were identified.
- Plasminogen binding enhances plasminogen activation by urokinase-type plasminogen activator (uPA).
- Bacterial invasion of HeLa cells was promoted by plasminogen binding and further enhanced by uPA.
Conclusions:
- Mycoplasma fermentans possesses specific binding sites for plasminogen.
- The binding of plasminogen facilitates bacterial invasion through enhanced plasminogen activation to plasmin.