Entamoeba histolytica: Deletion of the GPI Anchor Signal Sequence on the Gal/GalNAc Lectin Light Subunit Prevents Its Assembly into the Lectin Heterodimer

Abstract

Ramakrishnan, G., Lee, S., Mann, B. J., and Petri, W. A. Jr. 2000. Entamoeba histolytica: Deletion of the GPI anchor signal sequence on the Gal/GalNAc lectin light subunit prevents its assembly into the lectin heterodimer. Experimental Parasitology96, 57–60. Adherence and cytotoxicity of Entamoeba histolytica require the function of a heterodimeric galactose and N-acetylgalactosamine (Gal/GalNAc)-specific lectin. The lectin heavy subunit (Hgl) contains a carbohydrate recognition domain and mediates inside-out cell signaling via its cytoplasmic tail. The function of the lectin light subunit (Lgl) is unknown. The lectin has a unique mechanism of membrane association: Hgl is transmembrane but Lgl is glycosylphosphatidylinositol (GPI) anchored. The role of the GPI anchor signal sequence in heterodimer assembly was tested. Epitope-tagged Lgl with or without the GPI anchor addition signal was expressed in E. histolytica trophozoites. Tagged Lgl did not assemble with Hgl into a lectin heterodimer in the absence of the GPI addition signal. Consistent with previous results that only the Hgl subunit mediates adherence, the monomeric Lgl without the GPI anchor signal lacked Gal/GalNAc-binding activity.