Abstract
Galactose and N-acetyl-D-galactosamine (Gal/GalNAc) inhibitable lectin of Entamoeba histolytica, a common protozoan parasite, has roles in pathogenicity and induction of protective immunity in mouse models of amoebiasis. The lectin consists of heavy (Hgl), light (Lgl), and intermediate (Igl) subunits. Hgl has lectin activity and Lgl does not, but little is known about the activity of Igl. In this study, we assessed various regions of Igl for hemagglutinating activity using recombinant proteins expressed in Escherichia coli. We identified a weak hemagglutinating activity of the protein. Furthermore, we found novel hemolytic and cytotoxic activities of the lectin, which resided in the carboxy-terminal region of the protein. Antibodies against Igl inhibited the hemolytic activity of Entamoeba histolytica trophozoites. This is the first report showing hemagglutinating, hemolytic and cytotoxic activities of an amoebic molecule, Igl.
Highlights
Galactose and N-acetyl-D-galactosamine (Gal/GalNAc) inhibitable lectin of Entamoeba histolytica, a common protozoan parasite, has roles in pathogenicity and induction of protective immunity in mouse models of amoebiasis
Adherence of E. histolytica trophozoites to colonic mucins and host cells is essential for colonization, invasion and subsequent pathogenesis, and is mediated by a galactose (Gal)- and N-acetyl-D-galactosamine (GalNAc)-inhibitable lectin[2]
Since Igl is a lectin, we first wanted to clarify the region of Igl that is responsible for this activity
Summary
Galactose and N-acetyl-D-galactosamine (Gal/GalNAc) inhibitable lectin of Entamoeba histolytica, a common protozoan parasite, has roles in pathogenicity and induction of protective immunity in mouse models of amoebiasis. Antibodies against Igl inhibited the hemolytic activity of Entamoeba histolytica trophozoites. This is the first report showing hemagglutinating, hemolytic and cytotoxic activities of an amoebic molecule, Igl. Amoebiasis caused by infection with Entamoeba histolytica (E. histolytica) is a problematic parasitic disease in both developing and developed countries. Adherence of E. histolytica trophozoites to colonic mucins and host cells is essential for colonization, invasion and subsequent pathogenesis, and is mediated by a galactose (Gal)- and N-acetyl-D-galactosamine (GalNAc)-inhibitable lectin[2]. The 260-kDa Gal/GalNAc inhibitable lectin is a heterodimer of transmembrane heavy subunit (Hgl, 170 kDa) and glycosylphosphatidylinositol (GPI)-anchored light subunit (Lgl, 35/31 kDa) glycoproteins linked by disulfide bonds. Hgl contains a carbohydrate recognition domain (CRD) and is the key molecule in amebic adherence
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