Global proteomic analysis of the oocyst/sporozoite of Toxoplasma gondii reveals commitment to a host-independent lifestyle
- Equal contributors
1 Department of Infectious, Parasitic and Immunomediated Diseases, Istituto Superiore di Sanità, Viale Regina Elena 299, Rome 00161, Italy
2 United States Department of Agriculture, Agricultural Research Service, Animal Parasitic Diseases Laboratory, Animal and Natural Resources Institute, Beltsville, MD, 20705, USA
3 Present address: Agenzia Regionale per la Protezione Ambientale del Lazio, Sezione di Rieti, Via Salaria per l'Aquila 8, Rieti, 02100, Italy
BMC Genomics 2013, 14:183 doi:10.1186/1471-2164-14-183Published: 15 March 2013
Additional file 1: Figure S1:
Electrophoretic profiles of fractionated oocyst/sporozoite proteins of T. gondii. In experiment 3, Tris-soluble and Tris-insoluble protein samples were resolved by SDS-PAGE on a 10% acrylamide gel under reducing conditions and processed for LC-MS/MS analysis. Protein bands were visualized by staining with colloidal Coomassie. The arrows indicate the positions of representative gel slices.
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Additional file 2: Table S1:
Complete dataset of T. gondii oocyst/sporozoite proteins identified in this study. The table includes the list of the 1615 VEG oocyst proteins identified in the present study. Each protein is identified by the gene ID (column A) and annotation (column B) provided by ToxoDB 7.1. Columns C-E report Bioworks Browser 3.3.1 parameters, the number of peptides indicated in column E refers to the best identification. Column F reports the number of experiments in which each protein was identified. Column G indicates the predicted molecular weight of full length polypeptides. Asterisks indicate two proteins (TGGT1_064110 and TGGT1_064850) identified with a single peptide shared by other T. gondii proteins, whose IDs and annotations are reported at the bottom of the table.
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