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Role of a 49 kDa Trypanosoma cruzi Mucin-Associated Surface Protein (MASP49) during the Infection Process and Identification of a Mammalian Cell Surface Receptor
Trypanosoma cruzi is the etiologic agent of Chagas disease, a parasitic disease of great medical importance on the American continent. Trypomastigote infection’s initial step in a mammalian host is vital for the parasite’s life cycle. A trypomastigote’s surface presents many molecules, some of which...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2023
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9865002/ https://www.ncbi.nlm.nih.gov/pubmed/36678452 http://dx.doi.org/10.3390/pathogens12010105 |
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author | Espinoza, Bertha Martínez, Ignacio Martínez-Velasco, María Luisa Rodríguez-Sosa, Miriam González-Canto, Augusto Vázquez-Mendoza, Alicia Terrazas, Luis I. |
author_facet | Espinoza, Bertha Martínez, Ignacio Martínez-Velasco, María Luisa Rodríguez-Sosa, Miriam González-Canto, Augusto Vázquez-Mendoza, Alicia Terrazas, Luis I. |
author_sort | Espinoza, Bertha |
collection | PubMed |
description | Trypanosoma cruzi is the etiologic agent of Chagas disease, a parasitic disease of great medical importance on the American continent. Trypomastigote infection’s initial step in a mammalian host is vital for the parasite’s life cycle. A trypomastigote’s surface presents many molecules, some of which have been proposed to be involved in the infection process, including a glycoprotein family called mucin-associated surface proteins (MASPs). This work describes a 49-kDa molecule (MASP49) that belongs to this family and is expressed mainly on the surfaces of amastigotes and trypomastigotes but can be found in extracts and the membrane-enriched fractions of epimastigotes. This protein is partially GPI-anchored to the surface and has a role during the internalization process, since its blockade with specific antibodies decreases parasite entry into Vero cells by 62%. This work shows that MASP49 binds to peritoneal macrophages and rat cardiomyocytes, undergoes glycosylation via galactose N-acetylgalactosamine, and can attach to the macrophage murine C-type lectin receptor (mMGL). These results suggest that MASP49 can be considered a virulence factor in T. cruzi, and a better understanding of its role in the infection process is necessary. |
format | Online Article Text |
id | pubmed-9865002 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-98650022023-01-22 Role of a 49 kDa Trypanosoma cruzi Mucin-Associated Surface Protein (MASP49) during the Infection Process and Identification of a Mammalian Cell Surface Receptor Espinoza, Bertha Martínez, Ignacio Martínez-Velasco, María Luisa Rodríguez-Sosa, Miriam González-Canto, Augusto Vázquez-Mendoza, Alicia Terrazas, Luis I. Pathogens Article Trypanosoma cruzi is the etiologic agent of Chagas disease, a parasitic disease of great medical importance on the American continent. Trypomastigote infection’s initial step in a mammalian host is vital for the parasite’s life cycle. A trypomastigote’s surface presents many molecules, some of which have been proposed to be involved in the infection process, including a glycoprotein family called mucin-associated surface proteins (MASPs). This work describes a 49-kDa molecule (MASP49) that belongs to this family and is expressed mainly on the surfaces of amastigotes and trypomastigotes but can be found in extracts and the membrane-enriched fractions of epimastigotes. This protein is partially GPI-anchored to the surface and has a role during the internalization process, since its blockade with specific antibodies decreases parasite entry into Vero cells by 62%. This work shows that MASP49 binds to peritoneal macrophages and rat cardiomyocytes, undergoes glycosylation via galactose N-acetylgalactosamine, and can attach to the macrophage murine C-type lectin receptor (mMGL). These results suggest that MASP49 can be considered a virulence factor in T. cruzi, and a better understanding of its role in the infection process is necessary. MDPI 2023-01-07 /pmc/articles/PMC9865002/ /pubmed/36678452 http://dx.doi.org/10.3390/pathogens12010105 Text en © 2023 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Espinoza, Bertha Martínez, Ignacio Martínez-Velasco, María Luisa Rodríguez-Sosa, Miriam González-Canto, Augusto Vázquez-Mendoza, Alicia Terrazas, Luis I. Role of a 49 kDa Trypanosoma cruzi Mucin-Associated Surface Protein (MASP49) during the Infection Process and Identification of a Mammalian Cell Surface Receptor |
title | Role of a 49 kDa Trypanosoma cruzi Mucin-Associated Surface Protein (MASP49) during the Infection Process and Identification of a Mammalian Cell Surface Receptor |
title_full | Role of a 49 kDa Trypanosoma cruzi Mucin-Associated Surface Protein (MASP49) during the Infection Process and Identification of a Mammalian Cell Surface Receptor |
title_fullStr | Role of a 49 kDa Trypanosoma cruzi Mucin-Associated Surface Protein (MASP49) during the Infection Process and Identification of a Mammalian Cell Surface Receptor |
title_full_unstemmed | Role of a 49 kDa Trypanosoma cruzi Mucin-Associated Surface Protein (MASP49) during the Infection Process and Identification of a Mammalian Cell Surface Receptor |
title_short | Role of a 49 kDa Trypanosoma cruzi Mucin-Associated Surface Protein (MASP49) during the Infection Process and Identification of a Mammalian Cell Surface Receptor |
title_sort | role of a 49 kda trypanosoma cruzi mucin-associated surface protein (masp49) during the infection process and identification of a mammalian cell surface receptor |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9865002/ https://www.ncbi.nlm.nih.gov/pubmed/36678452 http://dx.doi.org/10.3390/pathogens12010105 |
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