ArticleInfection and immunity2001
Intermediate subunit of the Gal/GalNAc lectin of Entamoeba histolytica is a member of a gene family containing multiple CXXC sequence motifs.
Article in Infection and immunity, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed, 81 citations in OpenAlex.
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- Using MUC2 mucin producing tumorigenic human goblet-like cells to uncover functional properties of the mucus barrier.Gut microbes · 2025Article
- Host-specific targets of Histomonas meleagridis antigens revealed by immunoprecipitation.Scientific reports · 2025Article
- Molecular characterisation of Entamoeba histolytica UDP-glucose 4-epimerase, an enzyme able to provide building blocks for cyst wall formation.PLoS neglected tropical diseases · 2023Article
- The Gal/GalNac lectin as a possible acetylcholine receptor inFrontiers in cellular and infection microbiology · 2023Article
- Review
- Identification of Multiple Domains ofInternational journal of molecular sciences · 2022Article
- Interaction between human mucins and parasite glycoproteins: the role of lectins and glycosidases in colonization by intestinal protozoa.Revista do Instituto de Medicina Tropical de Sao Paulo · 2020Article
- Article
- Comparison of hemolytic activity of the intermediate subunit of Entamoeba histolytica and Entamoeba dispar lectins.PloS one · 2017Article
- Endoplasmic reticulum-resident Rab8A GTPase is involved in phagocytosis in the protozoan parasite Entamoeba histolytica.Cellular microbiology · 2016Article
- Evaluation of the C-Terminal Fragment of Entamoeba histolytica Gal/GalNAc Lectin Intermediate Subunit as a Vaccine Candidate against Amebic Liver Abscess.PLoS neglected tropical diseases · 2016Article
- Novel hemagglutinating, hemolytic and cytotoxic activities of the intermediate subunit of Entamoeba histolytica lectin.Scientific reports · 2015Article
- Entamoeba histolytica: adhesins and lectins in the trophozoite surface.Molecules (Basel, Switzerland) · 2015Review
- Expression, purification, and evaluation of recombinant LecA as a candidate for an amebic colitis vaccine.Vaccine · 2014Article
- An integrated microfluidic device for rapid serodiagnosis of amebiasis.Biomicrofluidics · 2013Article
- A Multilocus Sequence Typing System (MLST) reveals a high level of diversity and a genetic component to Entamoeba histolytica virulence.BMC microbiology · 2012Article
- Seroprevalence of Entamoeba histolytica infection in China.The American journal of tropical medicine and hygiene · 2012Article
- Common pathways for receptor-mediated ingestion of Escherichia coli and LDL cholesterol by Entamoeba histolytica regulated in part by transmembrane kinase 39.International journal for parasitology · 2012Article
- Localisation to lipid rafts correlates with increased function of the Gal/GalNAc lectin in the human protozoan parasite, Entamoeba histolytica.International journal for parasitology · 2011Article
Corrections and comments
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Authors and funding
11 authors at 2 institutions in 2 countries.
Funding
Abstract
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.
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