Surface-displayed glyceraldehyde 3-phosphate dehydrogenase and galectin

Surface-displayed glyceraldehyde 3-phosphate dehydrogenase and galectin from Dirofilaria immitis enhance the activation of the fibrinolytic system of the host.

González-Miguel J, Morchón R, Siles-Lucas M, Oleaga A, Simón F.

Acta Trop. 2015 May;145:8-16. doi: 10.1016/j.actatropica.2015.01.010. Epub 2015 Feb 7.

Cardiopulmonary dirofilariosis is a cosmopolitan disease caused by Dirofilaria immitis. This study includes the cloning, sequencing and expression of the recombinant forms of the GAPDH and GAL of D. immitis (rDiGAPDH and rDiGAL) and the analysis of their capacity as plasminogen-binding proteins. The results indicate that rDiGAPDH and rDiGAL bind plasminogen and stimulate plasmin generation by tissue plasminogen activator (tPA).

In addition, we show that rDiGAPDH and rDiGAL enhance the expression of the urokinase-type plasminogen activator (uPA) on canine endothelial cells in culture and that both proteins are expressed on the surface of D. immitis in close contact with the blood of the host. These data suggest that D. immitis could use the associated surface GAPDH and GAL as physiological plasminogen receptors to shift the fibrinolytic balance towards the generation of plasmin, which might constitute a survival mechanism to avoid the clot formation in its intravascular habitat.