Identification of phosphorylated proteins in erythrocytes infected by the human malaria parasite Plasmodium falciparum.

ABSTRACT:

Background

Previous comparative proteomic analysis on Plasmodium falciparum isolates of different adhesion properties suggested that protein phosphorylation varies between isolates with different cytoadherence properties. But the extent and dynamic changes in phosphorylation have not been systematically studied. As a baseline for these future studies, this paper examined changes in the phosphoproteome of parasitized red blood cells (pRBC).

Methods

Metabolic labelling with [35S] methionine on pRBC and 2D gel electrophoresis (2-DE) has previously been used to show the expression of parasite proteins and changes in protein iso-electric point (PI). 2-DE of different parasite strains was combined with immunoblotting using monoclonal antibodies specifically to phosphorylated serin

SUBMITTER: Wu Y 

PROVIDER: S-EPMC2696463 | biostudies-literature | 2009 May

REPOSITORIES: biostudies-literature