Research
Identification of phosphorylated proteins in erythrocytes infected by the human malaria parasite Plasmodium falciparum
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* Corresponding authors: Yang Wu ywu@liverpool.ac.uk - Alister Craig agcraig@liverpool.ac.uk
1 Liverpool School of Tropical Medicine, Pembroke Place, Liverpool L3 5QA, UK
2 Faculty of Veterinary Science, University of Liverpool, Crown Street, Liverpool L69 7ZJ, UK
Malaria Journal 2009, 8:105 doi:10.1186/1475-2875-8-105
Published: 18 May 2009Additional files
Additional file 1:
PI changes of pRBC from different parasite lines. Fluorography of proteins from trophozoite stage pRBC infected with 3D7 and ItG. At 20 hours after invasion, parasites were metabolically labelled with 50 μCi/ml [35S] methionine for 4 hours. Tris-insoluble pellets of pRBC were separated run on pH 4–7 IEF strips followed by 12% SDS-PAGE. Gels were stained with Coomassie blue, dried and exposed to X-ray film. Marked boxes show proteins with at least three fold changes between 3D7 and ItG. Enlarged images of corresponding boxes showing significant changes in the protein profiles. Arrows indicate the relative positions of the spots in different lines.
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Additional file 2:
Immunoblot of normal RBC and secondary antibody control. Immunoblot of normal RBC separated by 2DE (using the same conditions as for Figures 2 &3) and probed with antibodies to phosphorylated serine/threonine (A) or tyrosine (B). Part C is an immunoblot of Tris-insoluble pellet of ItG-infected RBC probed with the secondary antibody only and developed by ECL.
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Additional file 3:
Plasmodium falciparum phosphorylated proteins from ItG infected erythrocytes. Phosphorylated proteins purified/enriched by affinity chromatography techniques were separated by 1D SDS-PAGE and identified by nano-flow LC/MS/MS. Additional file 4 contains P. falciparum proteins from ItG-pRBC identified using searches including the phosphorylation modifications.
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Additional file 4:
Host phosphorylated proteins from ItG infected erythrocytes. Phosphorylated proteins purified/enriched by affinity chromatography techniques were separated by 1D SDS-PAGE and identified by nano-flow LC/MS/MS. Additional file 5 contains human phosphorylated proteins from ItG-pRBC identified using searches including the phosphorylation modifications.
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Additional file 5:
Phosphorylated proteins of non-infected erythrocytes purified from phospho-affinity column. Phosphorylated proteins purified/enriched by affinity chromatography techniques were separated by 1D SDS-PAGE and identified by nano-flow LC/MS/MS. Additional file 6 contains human phosphorylated proteins from normal RBC identified using searches including the phosphorylation modifications.
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Additional file 6:
Gene ontology analysis of serine/threonine and tyrosine phosphorylated proteins. Gene ontology analysis of the serine/threonine and tyrosine phosphorylated proteins. A. Functional categories; B. Cellular components; C. Biological processes. The different colours indicate human (blue) or parasite (red) proteins.
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