| Primary Identifier | IPR035310 | Type | Family |
| Short Name | Gal_GalNac_35kDa |
| description | In Entamoeba histolytica, the Gal/GalNAc lectin contributes to its virulence by establishing adhesion to host cell []. The Gal/GalNAc lectin is a heterodimeric molecule composed of a transmembrane heavy (170kDa) subunit and glycosylphosphatidylinositol-anchored light 31kDa and 35kDa subunits, which are non-covalently associated with an intermediate subunit of 150kDa [, ]. Inhibition of expression of 35kDa subunit of Gal/GalNAc lectin inhibits the cytotoxic and cytopathic activity of E. histolytica, but no decrease in adherence capacity to mammalian cells was evident. Interestingly, a carbohydrate-binding activity has been reported for the 35kDa light subunit of the lectin molecules of the closely related Entamoeba invadens []. Proteins in this entry are related to the light subunit. The light subunit consists of several polypeptide chains with considerable antigenic homology. The two light (31/35kDa) subunits of the lectinare present in two isoforms: the 31kDa isoform is glycerolphosphatidylinositol (GPI) anchored; and the 35kDa isoform is more highly glycosylated []. |
