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Binding and Endocytosis of Bovine Hololactoferrin by the Parasite Entamoeba histolytica

Entamoeba histolytica is a human parasite that requires iron (Fe) for its metabolic function and virulence. Bovine lactoferrin (B-Lf) and its peptides can be found in the digestive tract after dairy products are ingested. The aim of this study was to compare virulent trophozoites recently isolated f...

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Autores principales: Ortíz-Estrada, Guillermo, Calderón-Salinas, Víctor, Shibayama-Salas, Mineko, León-Sicairos, Nidia, de la Garza, Mireya
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Hindawi Publishing Corporation 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4450225/
https://www.ncbi.nlm.nih.gov/pubmed/26090404
http://dx.doi.org/10.1155/2015/375836
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author Ortíz-Estrada, Guillermo
Calderón-Salinas, Víctor
Shibayama-Salas, Mineko
León-Sicairos, Nidia
de la Garza, Mireya
author_facet Ortíz-Estrada, Guillermo
Calderón-Salinas, Víctor
Shibayama-Salas, Mineko
León-Sicairos, Nidia
de la Garza, Mireya
author_sort Ortíz-Estrada, Guillermo
collection PubMed
description Entamoeba histolytica is a human parasite that requires iron (Fe) for its metabolic function and virulence. Bovine lactoferrin (B-Lf) and its peptides can be found in the digestive tract after dairy products are ingested. The aim of this study was to compare virulent trophozoites recently isolated from hamster liver abscesses with nonvirulent trophozoites maintained for more than 30 years in cultures in vitro regarding their interaction with iron-charged B-Lf (B-holo-Lf). We performed growth kinetics analyses of trophozoites in B-holo-Lf and throughout several consecutive transfers. The virulent parasites showed higher growth and tolerance to iron than nonvirulent parasites. Both amoeba variants specifically bound B-holo-Lf with a similar K (d). However, averages of 9.45 × 10(5) and 6.65 × 10(6) binding sites/cell were found for B-holo-Lf in nonvirulent and virulent amoebae, respectively. Virulent amoebae bound more efficiently to human and bovine holo-Lf, human holo-transferrin, and human and bovine hemoglobin than nonvirulent amoebae. Virulent amoebae showed two types of B-holo-Lf binding proteins. Although both amoebae endocytosed this glycoprotein through clathrin-coated vesicles, the virulent amoebae also endocytosed B-holo-Lf through a cholesterol-dependent mechanism. Both amoeba variants secreted cysteine proteases cleaving B-holo-Lf. These data demonstrate that the B-Lf endocytosis is more efficient in virulent amoebae.
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spelling pubmed-44502252015-06-18 Binding and Endocytosis of Bovine Hololactoferrin by the Parasite Entamoeba histolytica Ortíz-Estrada, Guillermo Calderón-Salinas, Víctor Shibayama-Salas, Mineko León-Sicairos, Nidia de la Garza, Mireya Biomed Res Int Research Article Entamoeba histolytica is a human parasite that requires iron (Fe) for its metabolic function and virulence. Bovine lactoferrin (B-Lf) and its peptides can be found in the digestive tract after dairy products are ingested. The aim of this study was to compare virulent trophozoites recently isolated from hamster liver abscesses with nonvirulent trophozoites maintained for more than 30 years in cultures in vitro regarding their interaction with iron-charged B-Lf (B-holo-Lf). We performed growth kinetics analyses of trophozoites in B-holo-Lf and throughout several consecutive transfers. The virulent parasites showed higher growth and tolerance to iron than nonvirulent parasites. Both amoeba variants specifically bound B-holo-Lf with a similar K (d). However, averages of 9.45 × 10(5) and 6.65 × 10(6) binding sites/cell were found for B-holo-Lf in nonvirulent and virulent amoebae, respectively. Virulent amoebae bound more efficiently to human and bovine holo-Lf, human holo-transferrin, and human and bovine hemoglobin than nonvirulent amoebae. Virulent amoebae showed two types of B-holo-Lf binding proteins. Although both amoebae endocytosed this glycoprotein through clathrin-coated vesicles, the virulent amoebae also endocytosed B-holo-Lf through a cholesterol-dependent mechanism. Both amoeba variants secreted cysteine proteases cleaving B-holo-Lf. These data demonstrate that the B-Lf endocytosis is more efficient in virulent amoebae. Hindawi Publishing Corporation 2015 2015-05-18 /pmc/articles/PMC4450225/ /pubmed/26090404 http://dx.doi.org/10.1155/2015/375836 Text en Copyright © 2015 Guillermo Ortíz-Estrada et al. https://creativecommons.org/licenses/by/3.0/ This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research Article
Ortíz-Estrada, Guillermo
Calderón-Salinas, Víctor
Shibayama-Salas, Mineko
León-Sicairos, Nidia
de la Garza, Mireya
Binding and Endocytosis of Bovine Hololactoferrin by the Parasite Entamoeba histolytica
title Binding and Endocytosis of Bovine Hololactoferrin by the Parasite Entamoeba histolytica
title_full Binding and Endocytosis of Bovine Hololactoferrin by the Parasite Entamoeba histolytica
title_fullStr Binding and Endocytosis of Bovine Hololactoferrin by the Parasite Entamoeba histolytica
title_full_unstemmed Binding and Endocytosis of Bovine Hololactoferrin by the Parasite Entamoeba histolytica
title_short Binding and Endocytosis of Bovine Hololactoferrin by the Parasite Entamoeba histolytica
title_sort binding and endocytosis of bovine hololactoferrin by the parasite entamoeba histolytica
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4450225/
https://www.ncbi.nlm.nih.gov/pubmed/26090404
http://dx.doi.org/10.1155/2015/375836
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