Quantitative proteomic analysis of plasmodium vivax UIS3-induced proteome by label-free LC-MS

Abstract

Apicomplexans lack the ability to synthesize fatty acids de novo because it is different from human fatty acid synthesis. Plasmodium has an essential unique protein on its parasitovacuole membrane (PVM) called UIS3 (upregulated infective sporozoite 3). UIS3 binds to host L-FABP (liver-fatty binding protein) in order to convey essential lipids through PVM. L-FABP plays an important role in lipid synthesis, it has been hypothesized that interaction between UIS3 and L-FABP interfere in the overall fatty acid metabolism of hepatocytes. Quantitative proteomics have been used for analysis of the protein expression level of hepatocytes. Mass spectrometry data were analyzed by Skyline software with MS1 filtering label free technique. It has been found that the protein involving in glycolytic pathway and fatty acid synthesis pathway such as citrate synthase, fatty acid synthase are up-regulated. This will be analyzed in a further study.