Proteomic analysis of Entamoeba histolytica.
In this study, the proteome of axenically grown Entamoeba histolytica parasites was explored by two-dimensional gel electrophoresis (2-DE), employing a practical and effective procedure for the solubilization of E. histolytica proteins. Approximately 900 protein species in the pH range between 4 and 7 were detected by Coomassie Blue staining. Ninety-five spots were excised, trypsinated and subjected to mass spectrometry. The resultant data from peptide mass fingerprints were compared with those available in the E. histolytica genome and the (non-redundant) National Center for Biotechnology Information (NCBI) databases for the identification and categorization of proteins. Sixty-three of the proteins identified were predicted to relate to the cytoskeleton, surface, glycolysis, RNA/DNA metabolism, the ubiquitin-proteasome system, vesicular trafficking and signal transduction. The present study demonstrates, for the first time, that corresponding genes are indeed expressed in E. histolytica and provides a foundation for further proteomic studies of this parasite.
Tolstrup
J
J
Bernhard Nocht Institute for Tropical Medicine, 74 Bernhard Nocht Strasse, 20359 Hamburg, Germany.
Krause
E
E
Tannich
E
E
Bruchhaus
I
I
D000818:Animals; D030562:Databases, Protein; D015180:Electrophoresis, Gel, Two-Dimensional / Q000379:methods*; D004748:Entamoeba histolytica / Q000737:chemistry / Q000235:genetics*; D006863:Hydrogen-Ion Concentration; D013058:Mass Spectrometry / Q000379:methods*; D010449:Peptide Mapping; D020543:Proteome / Q000032:analysis / Q000737:chemistry*; D015800:Protozoan Proteins / Q000032:analysis / Q000737:chemistry*; D015398:Signal Transduction; D012995:Solubility
D020543:Proteome; D015800:Protozoan Proteins