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Enolase as a plasminogen binding protein in Leishmania mexicana

Vanegas, Gilmer, Quiñones, Wilfredo, Carrasco-López, Cesar, Concepción, Juan Luis, Albericio, Fernando, Avilán, Luisana
Parasitology research 2007 v.101 no.6 pp. 1511-1516
Leishmania mexicana, Streptococcus pneumoniae, antibodies, binding proteins, glycolysis, leishmaniasis, parasites, plasma membrane, plasminogen, prokaryotic cells, receptors, therapeutics
Enolase is a glycolytic and gluconeogenic enzyme also found on the surface of several eukaryotic and prokaryotic cells where it acts as plasminogen binding protein. Leishmania mexicana, one of the causative agents of Leishmaniasis, binds plasminogen and, in this parasite, enolase has been previously found associated with the external face of the plasma membrane. In this work, we show that the purified recombinant enolase has plasminogen binding activity indicating that, at the surface of the parasite, the protein may function as one of the plasminogen receptors. An internal motif ₂₄₉AYDAERKMY₂₅₇, similar to the nine amino-acid internal plasminogen-binding motif in Streptococcus pneumoniae enolase, is responsible for plasminogen interaction with the parasite enolase. Anti-enolase antibodies inhibited up to 60% of plasminogen binding on live parasites indicating that enolase act as a plasminogen receptor on the parasite. The fact that enolase acts as a possible plasminogen receptor in vivo makes this protein a promising target for therapy.