Phospholipase A1 from Trypanosoma cruzi infective stages generates lipid messengers that activate host cell protein kinase c

BELAUNZARÁN, ML; WAINSZELBAUM, MJ; LAMMEL, EM; GIMÉNEZ, G; ALOISE, MM; FLORIN-CHRISTENSEN, J; ISOLA, ELD

PARASITOLOGY

CAMBRIDGE UNIV PRESS

Año: 2007 vol. 134 p. 491 - 502

0031-1820

Here we study Phospholipase A1 (Plase A1) from Trypanosoma cruzi infective stages and its possible role regarding the interaction with mammalian host cells. Plase A1 was mainly detected as a membrane-bound activity in the infective amastigotes and trypomastigotes stages, being remarkably higher with respect to the non-infective epimastigotes. It is noteworthy that only the infective stages secreted Plase A1. Moreover, along the differentiation process from epimastigotes into metacyclic trypomastigotes, the secreted enzyme activity increased, as expected, simultaneously with the appearance of metacyclic forms. Thus, Plase A1 constitutes a new biochemical marker for T. cruzi infective stages. Since this enzyme is predominantly membrane-associated and secreted by the infective stages, Vero cells lipid profile modifications were analyzed after interaction with either intact infective parasites or purified T. cruzi Plase A1. Significant changes in Vero cell lipid composition were observed, with appearance of free fatty acids, diacylglycerol and lysophosphatidylcholine. Concomitantly with the generation of second lipid messengers, host cell Protein Kinase C activation was demonstrated. These results indicate that T. cruzi Plase A1 could play a critical role in the early events of parasite-host cell interaction and improve the understanding of the host cell molecular modifications that precede parasite invasion.