A lysosomal hydrolase receptor, CPBF2, is associated with motility and invasion of the enteric protozoan parasite Entamoeba histolytica.

Proper targeting and secretion of lysosomal hydrolases are regulated by transporting receptors. Entamoeba histolytica, the enteric protozoan parasite responsible for human amebiasis, has a unique family of lysosomal hydrolase receptors, cysteine protease binding protein family, CPBF. CPBFs, consisting of 11 members with conserved domain organization, bind to a wide range of cargos including cysteine proteases and glycosidases, which are also known to be involved in pathogenesis of this parasite. In this study, we characterized one of CPBFs, CPBF2, which is involved in cell motility and extracellular matrix invasion. Unexpectedly, these roles of CPBF were not related to its cargo, α-amylase. This is the first demonstration that a putative hydrolase receptor is involved in cell motility and invasion in parasitic protozoa.