¿Procesamiento de proteínas en Plasmodium falciparum?

Resumen

human and animal malaria, are characterized by an extreme high A+T content and an associated abundant low complexity inserts within their proteins. The enzyme glucose-6-phosphate dehydrogenase-6-phosphogluconolactonase (G6PD- 6PGL) found in Plasmodium species has unique structural and bifunctional characteristics. Here, we report the expression analysis of P. faciparum G6PD- 6PGL along the intraerythrocytic cycle by immunological analysis with antibodies raised against its N- and C- terminal domains. The pattern modification of band sizes at the different stages of parasite development suggest intracellular protein processing involving the cleavage of the native bifunctional form to produce two main fragments. In vitro RNA-mediated PfG6PD-6PGL gene silencing, studied along short-term parasite development also revealed the apparent intracellular protein modification dependent on the parasite stage. Fragment sizes were consistent with separating both catalytic functions of the enzyme. The proteolytic machinery underlying this specific PfG6PD-6PGL proccesing is still unknown in P. falciparum but suggests the existence of distinctive mechanisms in the parasite to deal with unique protein structures of essential function resulting from its genome evolution.