A striking common O-linked N-acetylglucosaminyl moiety between cruzipain and myosin

Autores
Acosta, Diana M; Soprano, Luciana L; Ferrero, Maximiliano R; Landoni, Malena; Esteva, Monica I; Couto, Alicia S; Duschak, Vilma G
Año de publicación
2011
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Fil: Acosta, D. M. ANLIS Dr. C. G. Malbrán. Instituto Nacional de Parasitologia Dr. Mario Fatala Chaben (INP); Argentina.
Fil: Soprano, L. L. ANLIS Dr. C. G. Malbrán. Instituto Nacional de Parasitologia Dr. Mario Fatala Chaben (INP); Argentina.
Fil: Ferrero, M. ANLIS Dr. C. G. Malbrán. Instituto Nacional de Parasitologia Dr. Mario Fatala Chaben (INP); Argentina.
Fil: Landoni, M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Orgánica. Centro de Investigaciones en Hidratos de Carbono (CIHIDECAR); Argentina.
Fil: Esteva, Mónica Inés. ANLIS Dr. C. G. Malbrán. Instituto Nacional de Parasitologia Dr. Mario Fatala Chaben (INP); Argentina.
Fil: Couto, A. S. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Orgánica. Centro de Investigaciones en Hidratos de Carbono (CIHIDECAR); Argentina.
Fil: Duschak, V. G. ANLIS Dr. C. G. Malbrán. Instituto Nacional de Parasitologia Dr. Mario Fatala Chaben (INP); Argentina.
Single units of O-linked N-acetylglucosamine (GlcNAc), usually components of nuclear and cytoplasmatic proteins, are present at the C-terminal domain of cruzipain (Cz), a lysosomal major antigen from Trypanosoma cruzi. On the other hand, antibodies directed against some self-antigens like myosin are associated with Chagas heart disease. The participation of O-GlcNAc moieties in the molecular antigenicity of Cz was determined using GlcNAc linked to aprotinin by ELISA. The immune cross-reactivity between Cz and myosin is mainly focused in the C-T domain. ELISA inhibition assays using rabbit sera specific for Cz and C-T in conjunction with immune-gold electron microscopy analysis of heart tissues from mice immunized with C-T confronted with polyclonal rabbit sera specific for Cz and C-T prior and after myosin adsorption provided evidence which indicates that O-GlcNAc moieties constitute a common epitope between Cz and either myosin or other cardiac O-GlcNAc-containing proteins, showing a new insight into the molecular immune pathogenesis of Chagas heart disease.
Fuente
Parasite immunology, 2011, 33(7), 363-370.
Materia
Enfermedad de Chagas
Miosina
Trypanosoma cruzi
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:Publications/123456789/534
Acceder
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network_acronym_str SGCANLIS
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network_name_str Sistema de Gestión del Conocimiento ANLIS MALBRÁN
spelling A striking common O-linked N-acetylglucosaminyl moiety between cruzipain and myosinAcosta, Diana MSoprano, Luciana LFerrero, Maximiliano RLandoni, MalenaEsteva, Monica ICouto, Alicia SDuschak, Vilma GEnfermedad de ChagasMiosinaTrypanosoma cruziFil: Acosta, D. M. ANLIS Dr. C. G. Malbrán. Instituto Nacional de Parasitologia Dr. Mario Fatala Chaben (INP); Argentina.Fil: Soprano, L. L. ANLIS Dr. C. G. Malbrán. Instituto Nacional de Parasitologia Dr. Mario Fatala Chaben (INP); Argentina.Fil: Ferrero, M. ANLIS Dr. C. G. Malbrán. Instituto Nacional de Parasitologia Dr. Mario Fatala Chaben (INP); Argentina.Fil: Landoni, M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Orgánica. Centro de Investigaciones en Hidratos de Carbono (CIHIDECAR); Argentina.Fil: Esteva, Mónica Inés. ANLIS Dr. C. G. Malbrán. Instituto Nacional de Parasitologia Dr. Mario Fatala Chaben (INP); Argentina.Fil: Couto, A. S. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Orgánica. Centro de Investigaciones en Hidratos de Carbono (CIHIDECAR); Argentina.Fil: Duschak, V. G. ANLIS Dr. C. G. Malbrán. Instituto Nacional de Parasitologia Dr. Mario Fatala Chaben (INP); Argentina.Single units of O-linked N-acetylglucosamine (GlcNAc), usually components of nuclear and cytoplasmatic proteins, are present at the C-terminal domain of cruzipain (Cz), a lysosomal major antigen from Trypanosoma cruzi. On the other hand, antibodies directed against some self-antigens like myosin are associated with Chagas heart disease. The participation of O-GlcNAc moieties in the molecular antigenicity of Cz was determined using GlcNAc linked to aprotinin by ELISA. The immune cross-reactivity between Cz and myosin is mainly focused in the C-T domain. ELISA inhibition assays using rabbit sera specific for Cz and C-T in conjunction with immune-gold electron microscopy analysis of heart tissues from mice immunized with C-T confronted with polyclonal rabbit sera specific for Cz and C-T prior and after myosin adsorption provided evidence which indicates that O-GlcNAc moieties constitute a common epitope between Cz and either myosin or other cardiac O-GlcNAc-containing proteins, showing a new insight into the molecular immune pathogenesis of Chagas heart disease.2011info:ar-repo/semantics/articuloinfo:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionapplication/pdfhttp://sgc.anlis.gob.ar/handle/123456789/53410.1111/j.1365-3024.2011.01291.xParasite immunology, 2011, 33(7), 363-370.reponame:Sistema de Gestión del Conocimiento ANLIS MALBRÁNinstname:Administración Nacional de Laboratorios e Institutos de Salud "Dr. Carlos G. Malbrán"instacron:ANLISParasite immunologyhttps://creativecommons.org/licenses/by-nc-nd/4.0/enginfo:eu-repo/semantics/openAccess2025-09-04T11:15:54Zoai:sgc.anlis.gob.ar:Publications/123456789/534Institucionalhttp://sgc.anlis.gob.ar/Organismo científico-tecnológicoNo correspondehttp://sgc.anlis.gob.ar/oai/biblioteca@anlis.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:a2025-09-04 11:15:55.174Sistema 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 A striking common O-linked N-acetylglucosaminyl moiety between cruzipain and myosin
title A striking common O-linked N-acetylglucosaminyl moiety between cruzipain and myosin
spellingShingle A striking common O-linked N-acetylglucosaminyl moiety between cruzipain and myosin
Acosta, Diana M
Enfermedad de Chagas
Miosina
Trypanosoma cruzi
title_short A striking common O-linked N-acetylglucosaminyl moiety between cruzipain and myosin
title_full A striking common O-linked N-acetylglucosaminyl moiety between cruzipain and myosin
title_fullStr A striking common O-linked N-acetylglucosaminyl moiety between cruzipain and myosin
title_full_unstemmed A striking common O-linked N-acetylglucosaminyl moiety between cruzipain and myosin
title_sort A striking common O-linked N-acetylglucosaminyl moiety between cruzipain and myosin
dc.creator.none.fl_str_mv Acosta, Diana M
Soprano, Luciana L
Ferrero, Maximiliano R
Landoni, Malena
Esteva, Monica I
Couto, Alicia S
Duschak, Vilma G
author Acosta, Diana M
author_facet Acosta, Diana M
Soprano, Luciana L
Ferrero, Maximiliano R
Landoni, Malena
Esteva, Monica I
Couto, Alicia S
Duschak, Vilma G
author_role author
author2 Soprano, Luciana L
Ferrero, Maximiliano R
Landoni, Malena
Esteva, Monica I
Couto, Alicia S
Duschak, Vilma G
author2_role author
author
author
author
author
author
dc.subject.none.fl_str_mv Enfermedad de Chagas
Miosina
Trypanosoma cruzi
topic Enfermedad de Chagas
Miosina
Trypanosoma cruzi
dc.description.none.fl_txt_mv Fil: Acosta, D. M. ANLIS Dr. C. G. Malbrán. Instituto Nacional de Parasitologia Dr. Mario Fatala Chaben (INP); Argentina.
Fil: Soprano, L. L. ANLIS Dr. C. G. Malbrán. Instituto Nacional de Parasitologia Dr. Mario Fatala Chaben (INP); Argentina.
Fil: Ferrero, M. ANLIS Dr. C. G. Malbrán. Instituto Nacional de Parasitologia Dr. Mario Fatala Chaben (INP); Argentina.
Fil: Landoni, M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Orgánica. Centro de Investigaciones en Hidratos de Carbono (CIHIDECAR); Argentina.
Fil: Esteva, Mónica Inés. ANLIS Dr. C. G. Malbrán. Instituto Nacional de Parasitologia Dr. Mario Fatala Chaben (INP); Argentina.
Fil: Couto, A. S. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Orgánica. Centro de Investigaciones en Hidratos de Carbono (CIHIDECAR); Argentina.
Fil: Duschak, V. G. ANLIS Dr. C. G. Malbrán. Instituto Nacional de Parasitologia Dr. Mario Fatala Chaben (INP); Argentina.
Single units of O-linked N-acetylglucosamine (GlcNAc), usually components of nuclear and cytoplasmatic proteins, are present at the C-terminal domain of cruzipain (Cz), a lysosomal major antigen from Trypanosoma cruzi. On the other hand, antibodies directed against some self-antigens like myosin are associated with Chagas heart disease. The participation of O-GlcNAc moieties in the molecular antigenicity of Cz was determined using GlcNAc linked to aprotinin by ELISA. The immune cross-reactivity between Cz and myosin is mainly focused in the C-T domain. ELISA inhibition assays using rabbit sera specific for Cz and C-T in conjunction with immune-gold electron microscopy analysis of heart tissues from mice immunized with C-T confronted with polyclonal rabbit sera specific for Cz and C-T prior and after myosin adsorption provided evidence which indicates that O-GlcNAc moieties constitute a common epitope between Cz and either myosin or other cardiac O-GlcNAc-containing proteins, showing a new insight into the molecular immune pathogenesis of Chagas heart disease.
description Fil: Acosta, D. M. ANLIS Dr. C. G. Malbrán. Instituto Nacional de Parasitologia Dr. Mario Fatala Chaben (INP); Argentina.
publishDate 2011
dc.date.none.fl_str_mv 2011
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 http://sgc.anlis.gob.ar/handle/123456789/534
10.1111/j.1365-3024.2011.01291.x
url http://sgc.anlis.gob.ar/handle/123456789/534
identifier_str_mv 10.1111/j.1365-3024.2011.01291.x
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv Parasite immunology
https://creativecommons.org/licenses/by-nc-nd/4.0/
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 Parasite immunology, 2011, 33(7), 363-370.
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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score 12.623145

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