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Intermediate Subunit of the Gal/GalNAc Lectin of Entamoeba histolytica Is a Member of a Gene Family Containing Multiple CXXC Sequence Motifs

By Xun-Jia Cheng, Molly A. Hughes, Christopher D. Huston, Brendan Loftus, Carol A. Gilchrist, Lauren A. Lockhart, Salil Ghosh, Vanessa Miller-Sims, Barbara J. Mann, William A. Petri and Hiroshi Tachibana


Killing by Entamoeba histolytica requires parasite adherence to host galactose- and N-acetyl-d-galactosamine (Gal/GalNAc)-containing cell surface receptors. A 260-kDa heterodimeric E. histolytica Gal/GalNAc lectin composed of heavy (Hgl) and light (Lgl) subunits has been previously described. Here we present the cloning and characterization of Igl, a 150-kDa intermediate subunit of the Gal/GalNAc lectin. Igl, Hgl, and Lgl colocalized on the surface membrane of trophozoites. Two unlinked copies of genes encoding Igl shared 81% amino acid sequence identity (GenBank accession no. AF337950 and AF337951). They encoded cysteine-rich proteins with amino- and carboxy-terminal hydrophobic signal sequences characteristic of glycosylphosphatidylinositol (GPI)-anchored membrane proteins. The igl genes lacked carbohydrate recognition domains but were members of a large family of amebic genes containing CXXC and CXC motifs. These data indicate that Igl is part of the parasite's multimolecular Gal/GalNAc adhesin required for host interaction

Topics: Fungal and Parasitic Infections
Publisher: American Society for Microbiology
Year: 2001
DOI identifier: 10.1128/IAI.69.9.5892-5898.2001
OAI identifier:
Provided by: PubMed Central
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