Proteomic analysis of Gal/GalNAc lectin-associated proteins in Entamoeba histolytica.
Contact-dependent killing and phagocytosis of target cells by Entamoeba histolytica trophozoites is mediated by the galactose (Gal) and N-acetyl-d-galactosamine (GalNAc)-inhibitable lectin. Previous work has suggested that this lectin functions as part of a signal transduction complex. To identify proteins that might be part of this complex, amebic trophozoites were bound to GalNAc-BSA-labeled magnetic beads and lysed. Bound proteins were eluted from the beads and analyzed by tandem mass spectrometry. Along with the Gal/GalNAc lectin subunits, several cytoskeletal proteins, potential signaling proteins, and a novel transmembrane protein, consistently purified with the GalNAc-BSA beads.
McCoy
James J
JJ
Department of Internal Medicine, University of Virginia School of Medicine, Charlottesville, VA 22908, USA.
Mann
Barbara J
BJ
D000818:Animals; D002448:Cell Adhesion; D004591:Electrophoresis, Polyacrylamide Gel; D004748:Entamoeba histolytica / Q000737:chemistry* / Q000378:metabolism; D015151:Immunoblotting; D018189:Immunomagnetic Separation; D037102:Lectins / Q000032:analysis / Q000378:metabolism*; D013058:Mass Spectrometry; D008863:Microspheres; D040901:Proteomics; D015800:Protozoan Proteins / Q000032:analysis* / Q000378:metabolism; D015398:Signal Transduction
D037102:Lectins; D015800:Protozoan Proteins; C078014:N-acetylgalactosamine inhibitable lectin 35-kDa subunit, Entamoeba histolytica