Quantitative proteomic analysis of plasmodium vivax UIS3-induced proteome by label-free LC-MS
Issued Date
2014
Resource Type
Language
eng
Rights
Mahidol University
Suggested Citation
Peerut Chienwichai, พีรุทย์ เชียรวิชัย, Wang Nguitragool, Jetsumon Prachumsri, เจตสุมน ประจำศรี, Supachai Topanurak, ศุภชัย โตภาณุรักษ์ (2014). Quantitative proteomic analysis of plasmodium vivax UIS3-induced proteome by label-free LC-MS. Retrieved from: https://repository.li.mahidol.ac.th/handle/20.500.14594/63147
Title
Quantitative proteomic analysis of plasmodium vivax UIS3-induced proteome by label-free LC-MS
Other Contributor(s)
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.
Description
Joint International Tropical Medicine Meeting 2014: 3D perspectives on tropical medicine: drivers, diversity and determination the 8th seminar on food-and water-borne parasitic zoonoses: 2-4 December 2014: Centara Grand Bangkok Convention Center at Central World, Bangkok, Thailand. Bangkok: Faculty of Tropical Medicine, Mahidol University; 2014. p. 224.