Involvement of sulfates from cruzipain, a major antigen of Trypanosoma cruzi, in the interaction with immunomodulatory molecule Siglec-E

Autores
Ferrero, Maximiliano R; Heins, Anja M; Soprano, Luciana L; Acosta, Diana M; Esteva, Monica I; Jacobs, Thomas; Duschak, Vilma G
Año de publicación
2016
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Fil: Ferrero, Maximiliano R. ANLIS Dr.C.G.Malbrán. Instituto Nacional de Parasitología. Departamento de Investigación y Docencia; Argentina.
Fil: Heins, Anja M. Bernhard Nocht Institute for Tropical Medicine, Hamburgo; Alemania.
Fil: Soprano, Luciana L. ANLIS Dr.C.G.Malbrán. Instituto Nacional de Parasitología. Departamento de Investigación y Docencia; Argentina.
Fil: Acosta, Diana M. ANLIS Dr.C.G.Malbrán. Instituto Nacional de Parasitología. Departamento de Investigación y Docencia; Argentina.
Fil: Esteva, Monica I. ANLIS Dr.C.G.Malbrán. Instituto Nacional de Parasitología. Departamento de Investigación y Docencia; Argentina.
Fil: Jacobs, Thomas. Bernhard Nocht Institute for Tropical Medicine, Hamburgo; Alemania.
Fil: Duschak, Vilma G. ANLIS Dr.C.G.Malbrán. Instituto Nacional de Parasitología. Departamento de Investigación y Docencia; Argentina.
In order to investigate the involvement of sulfated groups in the Trypanosoma cruzi host-parasite relationship, we studied the interaction between the major cysteine proteinase of T. cruzi, cruzipain (Cz), a sulfate-containing sialylated molecule and the sialic acid-binding immunoglobulin like lectin-E (Siglec-E). To this aim, ELISA, indirect immunofluorescence assays and flow cytometry, using mouse Siglec-E-Fc fusion molecules and glycoproteins of parasites, were performed. Competition assays verified that the lectins, Maackia amurensis II (Mal II) and Siglec-E-Fc, compete for the same binding sites. Taking into account that Mal II binding remains unaltered by sulfation, we established this lectin as sialylation degree control. Proteins of an enriched microsomal fraction showed the highest binding to Siglec-E as compared with those from the other parasite subcellular fractions. ELISA assays and the affinity purification of Cz by a Siglec-E column confirmed the interaction between both molecules. The significant decrease in binding of Siglec-E-Fc to Cz and to its C-terminal domain (C-T) after desulfation of these molecules suggests that sulfates contribute to the interaction between Siglec-E-Fc and these glycoproteins. Competitive ELISA assays confirmed the involvement of sulfated epitopes in the affinity between Siglec-E and Cz, probably modified by natural protein environment. Interestingly, data from flow cytometry of untreated and chlorate-treated parasites suggested that sulfates are not primary receptors, but enhance the binding of Siglec-E to trypomastigotic forms. Altogether, our findings support the notion that sulfate-containing sialylated glycoproteins interact with Siglec-E, an ortholog protein of human Siglec-9, and might modulate the immune response of the host, favoring parasitemia and persistence of the parasite.
Fuente
Medical Microbiology and Immunology 2016:205(1):21-35
Materia
Trypanosoma cruzi
Inmunomodulación
Ácido N-Acetilneuramínico
Lectinas Similares a la Inmunoglobulina de Unión a Ácido Siálico
Sulfatos
Nivel de accesibilidad
acceso abierto
Condiciones de uso
Repositorio
Sistema de Gestión del Conocimiento ANLIS MALBRÁN
Institución
Administración Nacional de Laboratorios e Institutos de Salud "Dr. Carlos G. Malbrán"
OAI Identificador
oai:sgc.anlis.gob.ar:123456789/1430

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network_acronym_str SGCANLIS
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network_name_str Sistema de Gestión del Conocimiento ANLIS MALBRÁN
spelling Involvement of sulfates from cruzipain, a major antigen of Trypanosoma cruzi, in the interaction with immunomodulatory molecule Siglec-EFerrero, Maximiliano RHeins, Anja MSoprano, Luciana LAcosta, Diana MEsteva, Monica IJacobs, ThomasDuschak, Vilma GTrypanosoma cruziInmunomodulaciónÁcido N-AcetilneuramínicoLectinas Similares a la Inmunoglobulina de Unión a Ácido SiálicoSulfatosFil: Ferrero, Maximiliano R. ANLIS Dr.C.G.Malbrán. Instituto Nacional de Parasitología. Departamento de Investigación y Docencia; Argentina.Fil: Heins, Anja M. Bernhard Nocht Institute for Tropical Medicine, Hamburgo; Alemania.Fil: Soprano, Luciana L. ANLIS Dr.C.G.Malbrán. Instituto Nacional de Parasitología. Departamento de Investigación y Docencia; Argentina.Fil: Acosta, Diana M. ANLIS Dr.C.G.Malbrán. Instituto Nacional de Parasitología. Departamento de Investigación y Docencia; Argentina.Fil: Esteva, Monica I. ANLIS Dr.C.G.Malbrán. Instituto Nacional de Parasitología. Departamento de Investigación y Docencia; Argentina.Fil: Jacobs, Thomas. Bernhard Nocht Institute for Tropical Medicine, Hamburgo; Alemania.Fil: Duschak, Vilma G. ANLIS Dr.C.G.Malbrán. Instituto Nacional de Parasitología. Departamento de Investigación y Docencia; Argentina.In order to investigate the involvement of sulfated groups in the Trypanosoma cruzi host-parasite relationship, we studied the interaction between the major cysteine proteinase of T. cruzi, cruzipain (Cz), a sulfate-containing sialylated molecule and the sialic acid-binding immunoglobulin like lectin-E (Siglec-E). To this aim, ELISA, indirect immunofluorescence assays and flow cytometry, using mouse Siglec-E-Fc fusion molecules and glycoproteins of parasites, were performed. Competition assays verified that the lectins, Maackia amurensis II (Mal II) and Siglec-E-Fc, compete for the same binding sites. Taking into account that Mal II binding remains unaltered by sulfation, we established this lectin as sialylation degree control. Proteins of an enriched microsomal fraction showed the highest binding to Siglec-E as compared with those from the other parasite subcellular fractions. ELISA assays and the affinity purification of Cz by a Siglec-E column confirmed the interaction between both molecules. The significant decrease in binding of Siglec-E-Fc to Cz and to its C-terminal domain (C-T) after desulfation of these molecules suggests that sulfates contribute to the interaction between Siglec-E-Fc and these glycoproteins. Competitive ELISA assays confirmed the involvement of sulfated epitopes in the affinity between Siglec-E and Cz, probably modified by natural protein environment. Interestingly, data from flow cytometry of untreated and chlorate-treated parasites suggested that sulfates are not primary receptors, but enhance the binding of Siglec-E to trypomastigotic forms. Altogether, our findings support the notion that sulfate-containing sialylated glycoproteins interact with Siglec-E, an ortholog protein of human Siglec-9, and might modulate the immune response of the host, favoring parasitemia and persistence of the parasite.2016-02info:ar-repo/semantics/articuloinfo:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionapplication/pdf1432-1831http://sgc.anlis.gob.ar/handle/123456789/143010.1007/s00430-015-0421-2Medical Microbiology and Immunology 2016:205(1):21-35reponame:Sistema de Gestión del Conocimiento ANLIS MALBRÁNinstname:Administración Nacional de Laboratorios e Institutos de Salud "Dr. Carlos G. Malbrán"instacron:ANLISMedical microbiology and immunologyenginfo:eu-repo/semantics/openAccess2025-09-04T11:16:50Zoai:sgc.anlis.gob.ar:123456789/1430Institucionalhttp://sgc.anlis.gob.ar/Organismo científico-tecnológicoNo correspondehttp://sgc.anlis.gob.ar/oai/biblioteca@anlis.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:a2025-09-04 11:16:50.874Sistema de Gestión del Conocimiento ANLIS MALBRÁN - Administración Nacional de Laboratorios e Institutos de Salud "Dr. Carlos G. Malbrán"false
dc.title.none.fl_str_mv Involvement of sulfates from cruzipain, a major antigen of Trypanosoma cruzi, in the interaction with immunomodulatory molecule Siglec-E
title Involvement of sulfates from cruzipain, a major antigen of Trypanosoma cruzi, in the interaction with immunomodulatory molecule Siglec-E
spellingShingle Involvement of sulfates from cruzipain, a major antigen of Trypanosoma cruzi, in the interaction with immunomodulatory molecule Siglec-E
Ferrero, Maximiliano R
Trypanosoma cruzi
Inmunomodulación
Ácido N-Acetilneuramínico
Lectinas Similares a la Inmunoglobulina de Unión a Ácido Siálico
Sulfatos
title_short Involvement of sulfates from cruzipain, a major antigen of Trypanosoma cruzi, in the interaction with immunomodulatory molecule Siglec-E
title_full Involvement of sulfates from cruzipain, a major antigen of Trypanosoma cruzi, in the interaction with immunomodulatory molecule Siglec-E
title_fullStr Involvement of sulfates from cruzipain, a major antigen of Trypanosoma cruzi, in the interaction with immunomodulatory molecule Siglec-E
title_full_unstemmed Involvement of sulfates from cruzipain, a major antigen of Trypanosoma cruzi, in the interaction with immunomodulatory molecule Siglec-E
title_sort Involvement of sulfates from cruzipain, a major antigen of Trypanosoma cruzi, in the interaction with immunomodulatory molecule Siglec-E
dc.creator.none.fl_str_mv Ferrero, Maximiliano R
Heins, Anja M
Soprano, Luciana L
Acosta, Diana M
Esteva, Monica I
Jacobs, Thomas
Duschak, Vilma G
author Ferrero, Maximiliano R
author_facet Ferrero, Maximiliano R
Heins, Anja M
Soprano, Luciana L
Acosta, Diana M
Esteva, Monica I
Jacobs, Thomas
Duschak, Vilma G
author_role author
author2 Heins, Anja M
Soprano, Luciana L
Acosta, Diana M
Esteva, Monica I
Jacobs, Thomas
Duschak, Vilma G
author2_role author
author
author
author
author
author
dc.subject.none.fl_str_mv Trypanosoma cruzi
Inmunomodulación
Ácido N-Acetilneuramínico
Lectinas Similares a la Inmunoglobulina de Unión a Ácido Siálico
Sulfatos
topic Trypanosoma cruzi
Inmunomodulación
Ácido N-Acetilneuramínico
Lectinas Similares a la Inmunoglobulina de Unión a Ácido Siálico
Sulfatos
dc.description.none.fl_txt_mv Fil: Ferrero, Maximiliano R. ANLIS Dr.C.G.Malbrán. Instituto Nacional de Parasitología. Departamento de Investigación y Docencia; Argentina.
Fil: Heins, Anja M. Bernhard Nocht Institute for Tropical Medicine, Hamburgo; Alemania.
Fil: Soprano, Luciana L. ANLIS Dr.C.G.Malbrán. Instituto Nacional de Parasitología. Departamento de Investigación y Docencia; Argentina.
Fil: Acosta, Diana M. ANLIS Dr.C.G.Malbrán. Instituto Nacional de Parasitología. Departamento de Investigación y Docencia; Argentina.
Fil: Esteva, Monica I. ANLIS Dr.C.G.Malbrán. Instituto Nacional de Parasitología. Departamento de Investigación y Docencia; Argentina.
Fil: Jacobs, Thomas. Bernhard Nocht Institute for Tropical Medicine, Hamburgo; Alemania.
Fil: Duschak, Vilma G. ANLIS Dr.C.G.Malbrán. Instituto Nacional de Parasitología. Departamento de Investigación y Docencia; Argentina.
In order to investigate the involvement of sulfated groups in the Trypanosoma cruzi host-parasite relationship, we studied the interaction between the major cysteine proteinase of T. cruzi, cruzipain (Cz), a sulfate-containing sialylated molecule and the sialic acid-binding immunoglobulin like lectin-E (Siglec-E). To this aim, ELISA, indirect immunofluorescence assays and flow cytometry, using mouse Siglec-E-Fc fusion molecules and glycoproteins of parasites, were performed. Competition assays verified that the lectins, Maackia amurensis II (Mal II) and Siglec-E-Fc, compete for the same binding sites. Taking into account that Mal II binding remains unaltered by sulfation, we established this lectin as sialylation degree control. Proteins of an enriched microsomal fraction showed the highest binding to Siglec-E as compared with those from the other parasite subcellular fractions. ELISA assays and the affinity purification of Cz by a Siglec-E column confirmed the interaction between both molecules. The significant decrease in binding of Siglec-E-Fc to Cz and to its C-terminal domain (C-T) after desulfation of these molecules suggests that sulfates contribute to the interaction between Siglec-E-Fc and these glycoproteins. Competitive ELISA assays confirmed the involvement of sulfated epitopes in the affinity between Siglec-E and Cz, probably modified by natural protein environment. Interestingly, data from flow cytometry of untreated and chlorate-treated parasites suggested that sulfates are not primary receptors, but enhance the binding of Siglec-E to trypomastigotic forms. Altogether, our findings support the notion that sulfate-containing sialylated glycoproteins interact with Siglec-E, an ortholog protein of human Siglec-9, and might modulate the immune response of the host, favoring parasitemia and persistence of the parasite.
description Fil: Ferrero, Maximiliano R. ANLIS Dr.C.G.Malbrán. Instituto Nacional de Parasitología. Departamento de Investigación y Docencia; Argentina.
publishDate 2016
dc.date.none.fl_str_mv 2016-02
dc.type.none.fl_str_mv info:ar-repo/semantics/articulo
info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv 1432-1831
http://sgc.anlis.gob.ar/handle/123456789/1430
10.1007/s00430-015-0421-2
identifier_str_mv 1432-1831
10.1007/s00430-015-0421-2
url http://sgc.anlis.gob.ar/handle/123456789/1430
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv Medical microbiology and immunology
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.source.none.fl_str_mv Medical Microbiology and Immunology 2016:205(1):21-35
reponame:Sistema de Gestión del Conocimiento ANLIS MALBRÁN
instname:Administración Nacional de Laboratorios e Institutos de Salud "Dr. Carlos G. Malbrán"
instacron:ANLIS
reponame_str Sistema de Gestión del Conocimiento ANLIS MALBRÁN
collection Sistema de Gestión del Conocimiento ANLIS MALBRÁN
instname_str Administración Nacional de Laboratorios e Institutos de Salud "Dr. Carlos G. Malbrán"
instacron_str ANLIS
institution ANLIS
repository.name.fl_str_mv Sistema de Gestión del Conocimiento ANLIS MALBRÁN - Administración Nacional de Laboratorios e Institutos de Salud "Dr. Carlos G. Malbrán"
repository.mail.fl_str_mv biblioteca@anlis.gov.ar
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