<i>Entamoeba histolytica</i> Trophozoites Interact with the c-Met Receptor at the Surface of Liver Origin Cells through the Gal/GalNAc Amoebic Lectin
Amoebiasis in humans is caused by the protozoan parasite <i>Entamoeba histolytica,</i> 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 le...
| Main Authors: | , , , , , , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
MDPI AG
2021-09-01
|
| Series: | Life |
| Subjects: | |
| Online Access: | https://www.mdpi.com/2075-1729/11/9/923 |
| _version_ | 1829092065934311424 |
|---|---|
| author | 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 |
| author_facet | 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 |
| author_sort | Jesus Pérez-Hernández |
| collection | DOAJ |
| description | Amoebiasis in humans is caused by the protozoan parasite <i>Entamoeba histolytica,</i> 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. |
| first_indexed | 2024-03-10T07:30:08Z |
| format | Article |
| id | doaj.art-982683c34650415682b1ccae8b1facd4 |
| institution | Directory Open Access Journal |
| issn | 2075-1729 |
| language | English |
| last_indexed | 2024-03-10T07:30:08Z |
| publishDate | 2021-09-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Life |
| spelling | doaj.art-982683c34650415682b1ccae8b1facd42023-11-22T13:55:58ZengMDPI AGLife2075-17292021-09-0111992310.3390/life11090923<i>Entamoeba histolytica</i> Trophozoites Interact with the c-Met Receptor at the Surface of Liver Origin Cells through the Gal/GalNAc Amoebic LectinJesus Pérez-Hernández0Clarisa Retana-González1Espiridión Ramos-Martínez2José Cruz-Colín3Andrés Saralegui-Amaro4Gabriela Baltazar-Rosario5Concepción Gutiérrez-Ruíz6Gerardo Aristi-Urista7Rosario López-Vancell8Experimental Pathology Laboratory, Research Unit in Experimental Medicine, School of Medicine, National Autonomous University of Mexico, Mexico City 04519, MexicoExperimental Pathology Laboratory, Research Unit in Experimental Medicine, School of Medicine, National Autonomous University of Mexico, Mexico City 04519, MexicoExperimental Pathology Laboratory, Research Unit in Experimental Medicine, School of Medicine, National Autonomous University of Mexico, Mexico City 04519, MexicoNational Institute of Genomic Medicine, Mexico City 14610, MexicoNational Laboratory for Advanced Microscopy, Institute of Biotechnology, National Autonomous University of Mexico, Cuernavaca, Morelos 62210, MexicoExperimental Pathology Laboratory, Research Unit in Experimental Medicine, School of Medicine, National Autonomous University of Mexico, Mexico City 04519, MexicoCellular Physiology Laboratory, Biological and Health Sciences Division, Metropolitan Autonomous University, Mexico City 09340, MexicoPathology Service, General Hospital of Mexico “Dr. Eduardo Liceaga”, School of Medicine, UNAM (National Autonomous University of Mexico), Mexico City 06720, MexicoExperimental Pathology Laboratory, Research Unit in Experimental Medicine, School of Medicine, National Autonomous University of Mexico, Mexico City 04519, MexicoAmoebiasis in humans is caused by the protozoan parasite <i>Entamoeba histolytica,</i> 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.https://www.mdpi.com/2075-1729/11/9/923Gal/GalNAc lectin<i>Entamoeba histolytica</i> cytotoxicityc-Met receptor |
| spellingShingle | 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 <i>Entamoeba histolytica</i> Trophozoites Interact with the c-Met Receptor at the Surface of Liver Origin Cells through the Gal/GalNAc Amoebic Lectin Life Gal/GalNAc lectin <i>Entamoeba histolytica</i> cytotoxicity c-Met receptor |
| title | <i>Entamoeba histolytica</i> Trophozoites Interact with the c-Met Receptor at the Surface of Liver Origin Cells through the Gal/GalNAc Amoebic Lectin |
| title_full | <i>Entamoeba histolytica</i> Trophozoites Interact with the c-Met Receptor at the Surface of Liver Origin Cells through the Gal/GalNAc Amoebic Lectin |
| title_fullStr | <i>Entamoeba histolytica</i> Trophozoites Interact with the c-Met Receptor at the Surface of Liver Origin Cells through the Gal/GalNAc Amoebic Lectin |
| title_full_unstemmed | <i>Entamoeba histolytica</i> Trophozoites Interact with the c-Met Receptor at the Surface of Liver Origin Cells through the Gal/GalNAc Amoebic Lectin |
| title_short | <i>Entamoeba histolytica</i> Trophozoites Interact with the c-Met Receptor at the Surface of Liver Origin Cells through the Gal/GalNAc Amoebic Lectin |
| title_sort | i entamoeba histolytica i trophozoites interact with the c met receptor at the surface of liver origin cells through the gal galnac amoebic lectin |
| topic | Gal/GalNAc lectin <i>Entamoeba histolytica</i> cytotoxicity c-Met receptor |
| url | https://www.mdpi.com/2075-1729/11/9/923 |
| work_keys_str_mv | AT jesusperezhernandez ientamoebahistolyticaitrophozoitesinteractwiththecmetreceptoratthesurfaceofliverorigincellsthroughthegalgalnacamoebiclectin AT clarisaretanagonzalez ientamoebahistolyticaitrophozoitesinteractwiththecmetreceptoratthesurfaceofliverorigincellsthroughthegalgalnacamoebiclectin AT espiridionramosmartinez ientamoebahistolyticaitrophozoitesinteractwiththecmetreceptoratthesurfaceofliverorigincellsthroughthegalgalnacamoebiclectin AT josecruzcolin ientamoebahistolyticaitrophozoitesinteractwiththecmetreceptoratthesurfaceofliverorigincellsthroughthegalgalnacamoebiclectin AT andressaraleguiamaro ientamoebahistolyticaitrophozoitesinteractwiththecmetreceptoratthesurfaceofliverorigincellsthroughthegalgalnacamoebiclectin AT gabrielabaltazarrosario ientamoebahistolyticaitrophozoitesinteractwiththecmetreceptoratthesurfaceofliverorigincellsthroughthegalgalnacamoebiclectin AT concepciongutierrezruiz ientamoebahistolyticaitrophozoitesinteractwiththecmetreceptoratthesurfaceofliverorigincellsthroughthegalgalnacamoebiclectin AT gerardoaristiurista ientamoebahistolyticaitrophozoitesinteractwiththecmetreceptoratthesurfaceofliverorigincellsthroughthegalgalnacamoebiclectin AT rosariolopezvancell ientamoebahistolyticaitrophozoitesinteractwiththecmetreceptoratthesurfaceofliverorigincellsthroughthegalgalnacamoebiclectin |