Multifunctional glyceraldehyde-3-phosphate dehydrogenase (GAPDH) of parasites.

Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is an enzyme involved in glycolysis. However, non-glycolytic activities of this enzyme were subsequently discovered including DNA repair, cell death, membrane fusion and transport. Recent studies have identified additional functions of this enzyme in parasites such as modulating host immune responses. For example, Haemonchus contortus GAPDH binds to complement C3 and also interacts with peripheral blood mononuclear cells. The enzyme from Leishmania major inhibits TNF-α production in host macrophages. Further, GAPDH of Schistosoma bovis, Dirofilaria immitis and Babesia microti binds to plasminogen that may facilitate parasite migration by preventing clot formation in its vicinity. Trichomonas vaginalis GAPDH interacts with many extracellular matrix proteins that may support initial adhesion of the organism to the host tissues. Surface associated GAPDH of Plasmodium berghei interacts with CD68 of Kupffer cells; a prerequisite for hepatocyte infection. This review discusses the general features of the enzyme and its significance in host-parasite relationships.