<i>Entamoeba histolytica</i> Trophozoites Interact with the c-Met Receptor at the Surface of Liver Origin Cells through the Gal/GalNAc Amoebic Lectin
Jesus Pérez-Hernández,
Clarisa Retana-González,
Espiridión Ramos-Martínez,
José Cruz-Colín,
Andrés Saralegui-Amaro,
Gabriela Baltazar-Rosario,
Concepción Gutiérrez-Ruíz,
Gerardo Aristi-Urista,
Rosario López-Vancell
Affiliations
Jesus Pérez-Hernández
Experimental Pathology Laboratory, Research Unit in Experimental Medicine, School of Medicine, National Autonomous University of Mexico, Mexico City 04519, Mexico
Clarisa Retana-González
Experimental Pathology Laboratory, Research Unit in Experimental Medicine, School of Medicine, National Autonomous University of Mexico, Mexico City 04519, Mexico
Espiridión Ramos-Martínez
Experimental Pathology Laboratory, Research Unit in Experimental Medicine, School of Medicine, National Autonomous University of Mexico, Mexico City 04519, Mexico
José Cruz-Colín
National Institute of Genomic Medicine, Mexico City 14610, Mexico
Andrés Saralegui-Amaro
National Laboratory for Advanced Microscopy, Institute of Biotechnology, National Autonomous University of Mexico, Cuernavaca, Morelos 62210, Mexico
Gabriela Baltazar-Rosario
Experimental Pathology Laboratory, Research Unit in Experimental Medicine, School of Medicine, National Autonomous University of Mexico, Mexico City 04519, Mexico
Concepción Gutiérrez-Ruíz
Cellular Physiology Laboratory, Biological and Health Sciences Division, Metropolitan Autonomous University, Mexico City 09340, Mexico
Gerardo Aristi-Urista
Pathology Service, General Hospital of Mexico “Dr. Eduardo Liceaga”, School of Medicine, UNAM (National Autonomous University of Mexico), Mexico City 06720, Mexico
Rosario López-Vancell
Experimental Pathology Laboratory, Research Unit in Experimental Medicine, School of Medicine, National Autonomous University of Mexico, Mexico City 04519, Mexico
Amoebiasis in humans is caused by the protozoan parasite Entamoeba histolytica, which cytotoxic activity has been demonstrated on a wide variety of target cells. The process involves the adherence of the parasite to the cell, and such adherence is mediated by an amoebic surface lectin, known as Gal/GalNAc lectin. It is composed of heavy, intermediate, and light subunits. The carbohydrate recognition domain (CRD) has been identified within a cysteine-rich region in the lectin heavy subunit and has an amino acid sequence identity to the receptor-binding domain of hepatocyte growth factor (HGF). Recombinant CRD has been previously shown to compete with HGF for binding to the c-Met receptor IgG fusion protein. In the present study, we searched for evidence of interaction between the Gal/GalNAc lectin at the surface of trophozoites with the c-Met receptor expressed at the surface of HepG2 in coculture assays. Immunoprecipitation of the coculture lysate indicated interaction of the c-Met with a 60 kDa peptide recognized by antiamoebic lectin antibody. Colocalization of both molecules was detected by fluorescence confocal microscopy. Incubation of HepG2 cells with HGF before coculture with trophozoites prevents the cytotoxic effect caused by the parasites but not their adherence to the cells. Our results point to Gal/GalNAc lectin as a ligand of the c-Met receptor at the surface of HepG2 cells.
