Proteomic analysis of phagocytosis in the enteric protozoan parasite Entamoeba histolytica.
Proteomic analysis of phagosomes isolated from Entamoeba histolytica by liquid chromatography and mass spectrometry identified 85 proteins involved in surface recognition, actin cytoskeleton rearrangement, vesicular trafficking, and degradation. Phagosome localization of representative proteins was verified by immunofluorescence assay. This study should provide a basis for molecular identification and characterization of phagosome biogenesis.
Okada
Mami
M
Department of Parasitology, Gunma University Graduate School of Medicine, 3-39-22 Showa-machi, Maebashi, Gunma 371-8511, Japan.
Huston
Christopher D
CD
Mann
Barbara J
BJ
Petri
William A
WA
Kita
Kiyoshi
K
Nozaki
Tomoyoshi
T
D000199:Actins / Q000378:metabolism; D000818:Animals; D015415:Biomarkers / Q000378:metabolism; D004748:Entamoeba histolytica / Q000378:metabolism*; D020558:GTP Phosphohydrolases / Q000378:metabolism; D010587:Phagocytosis; D040901:Proteomics; D015800:Protozoan Proteins / Q000378:metabolism / Q000502:physiology*; D000090802:rab7 GTP-Binding Proteins
D000199:Actins; D015415:Biomarkers; D015800:Protozoan Proteins; D000090802:rab7 GTP-Binding Proteins; D020558:GTP Phosphohydrolases; C464925:Rab7 protein, Entamoeba histolytica