The interaction of pathogenic bacteria with the host fibrinolytic system through the plasminogen molecule has been well documented. It has been shown, using animal models, to be important in invasion into the host and establishment of the infection. From a number of recent observations with parasitic protists and helminths, emerges evidence that also in these organisms the interaction with plasminogen may be important for infection and virulence. A group of molecules that act as plasminogen receptors have been identified in parasites. This group comprises the glycolytic enzymes enolase, glyceraldehyde-3-phosphate dehydrogenase and fructose-1,6-biphosphate aldolase, in common with the plasminogen receptors known in prokaryotic pathogens. The interaction with the fibrinolytic system may arm the parasites with the host protease plasmin, thus helping them to migrate and cross barriers, infect cells and avoid clot formation. In this context, plasminogen receptors on the parasite surface or as secreted molecules, may be considered virulence factors. A possible evolutionary scenario for the recruitment of glycolytic enzymes as plasminogen receptors by widely different pathogens is discussed.
- Host-Parasite Interactions
- Plasminogen Activators/metabolism
- Receptors, Cell Surface/metabolism