Membrane protein carbonylation of Plasmodium falciparum infected erythrocytes under conditions of sickle cell trait and G6PD deficiency

Publication date: Available online 22 November 2018Source: Molecular and Biochemical ParasitologyAuthor(s): Neyder Contreras Puentes, Erika Rodríguez Cavallo, Darío Méndez CuadroAbstractDeficiency of glucose-6-phosphate dehydrogenase (G6PD) and sickle cell trait (SCT) are described as the polymorphic disorders prevalent in erythrocytes. Both are considered the result of the selective pressure exerted by Plasmodium parasites over human genome, due to a certain degree of resistance to the clinical symptoms of severe malaria. There exist in both a prooxidant environment that favors the oxidative damage on membrane proteins, which probably is part of molecular protector mechanisms. Nevertheless, mechanisms are not completely understood at molecular level for each polymorphism yet, and even less if are commons for several of them. Here, synchronous cultures at high parasitemia levels of P. falciparum 3D7 were used to quantify oxidative damage in membrane proteins of erythrocytes with G6PD deficient and SCT. Carbonyl index by dot blot assay was used to calculate the variation of oxidative damage during the asexual phases. Besides, protein carbonylation profiles were obtained by Western blot and complemented with mass spectrometry using MALDI-TOF-TOF analysis. Erythrocytes with G6PD deficient and SCT showed higher carbonyl index values than control and similar profiles of carbonylated proteins; moreover, cytoskeletal and stress response proteins were identified as the main target...
Source: Molecular and Biochemical Parasitology - Category: Parasitology Source Type: research