An anionic synthetic sugar containing 6-SO3 -NAcGlc mimics the sulfated cruzipain epitope that plays a central role in immune recognition
- Autores
- Couto, Alicia S; Soprano, Luciana L; Landoni, Malena; Pourcelot, Marilyne; Acosta, Diana M; Bultel, Laurent; Parente, Juliana E; Ferrero, Maximiliano R; Barbier, Maximilien; Dussouy, Christophe; Esteva, Monica I; Kovensky, José; Duschak, Vilma G
- Año de publicación
- 2012
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- Fil: Couto, Alicia S. Universidad de Buenos Aires. Centro de Investigaciones en Hidratos de Carbono (CIHIDECAR). Departamento de Química Orgánica; Argentina.
Fil: Soprano, Luciana L. ANLIS Dr. C.G.Malbrán. Intituto Nacional de Parasitología "Dr. Mario Fatala Chaben". Departamento de investigación; Argentina.
Fil: Landoni, Malena. Universidad de Buenos Aires. Centro de Investigaciones en Hidratos de Carbono (CIHIDECAR). Departamento de Química Orgánica; Argentina.
Fil: Pourcelot, Marilyne. Université de Picardie Jules Verne. Laboratoire des Glucides; Francia.
Fil: Acosta, Diana M. ANLIS Dr. C.G.Malbrán. Intituto Nacional de Parasitología "Dr. Mario Fatala Chaben". Departamento de investigación; Argentina.
Fil: Bultel, Laurent. Université de Picardie Jules Verne. Laboratoire des Glucides; Francia.
Fil: Parente, Juliana E. Universidad de Buenos Aires. Centro de Investigaciones en Hidratos de Carbono (CIHIDECAR). Departamento de Química Orgánica; Argentina.
Fil: Ferrero, Maximiliano R. ANLIS Dr. C.G.Malbrán. Intituto Nacional de Parasitología "Dr. Mario Fatala Chaben". Departamento de investigación; Argentina.
Fil: Barbier, Maximilien. Université de Picardie Jules Verne. Laboratoire des Glucides; Francia.
Fil: Dussouy, Christophe. Université de Picardie Jules Verne. Laboratoire des Glucides; Francia.
Fil: Esteva, Monica I. ANLIS Dr. C.G.Malbrán. Intituto Nacional de Parasitología "Dr. Mario Fatala Chaben". Departamento de investigación; Argentina.
Fil: Kovensky, José. Université de Picardie Jules Verne. Laboratoire des Glucides; Francia.
Fil: Duschak, Vilma G. ANLIS Dr. C.G.Malbrán. Intituto Nacional de Parasitología "Dr. Mario Fatala Chaben". Departamento de investigación; Argentina.
Cruzipain (Cz), the major cysteine proteinase of Trypanosoma cruzi, is a glycoprotein that contains sulfated high-mannose-type oligosaccharides. We have previously determined that these sulfate groups are targets of specific immune responses. In order to evaluate the structural requirements for antibody recognition of Cz, a systematic structure-activity study of the chemical characteristics needed for antibody binding to the Cz sulfated epitope was performed by immunoassays. With this aim, different synthesized molecules were coupled to the proteins BSA and aprotinin and confronted with (a) mouse sera specific for Cz and its carboxy-terminal (C-T) domain, (b) antibodies raised in rabbits immunized with Cz and its C-terminal domain and (c) IgGs purified from human Chagas disease sera. Our results indicate that a glucosamine containing an esterifying sulfate group in position O-6 and an N-acetyl group was the preferred epitope for the immune recognition of sera specific for Cz and its C-T domain. Although to a minor extent, other anionic compounds bearing sulfate groups in different positions and number as well as different anionic charged groups including carboxylated or phosphorylated monosaccharides, disaccharides and oligosaccharides were recognized. In conclusion, we found that synthetic anionic sugar conjugates containing N-acetyl d-glucosamine-6-sulfate sodium salt (GlcNAc6S) competitively inhibit the binding of affinity purified rabbit anti-C-T IgG to the C-T extension of Cz. Extending these findings to the context of natural infection, immune assays performed with Chagas disease serum confirmed that the structure of synthetic GlcNAc6S mimics the N-glycan-linked sulfated epitope displayed in the C-T domain of Cz. - Materia
-
Enfermedad de Chagas
Sitios de Unión de Anticuerpos
Glucosamina - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- Repositorio
- Institución
- Administración Nacional de Laboratorios e Institutos de Salud "Dr. Carlos G. Malbrán"
- OAI Identificador
- oai:sgc.anlis.gob.ar:123456789/1483
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An anionic synthetic sugar containing 6-SO3 -NAcGlc mimics the sulfated cruzipain epitope that plays a central role in immune recognitionCouto, Alicia SSoprano, Luciana LLandoni, MalenaPourcelot, MarilyneAcosta, Diana MBultel, LaurentParente, Juliana EFerrero, Maximiliano RBarbier, MaximilienDussouy, ChristopheEsteva, Monica IKovensky, JoséDuschak, Vilma GEnfermedad de ChagasSitios de Unión de AnticuerposGlucosaminaFil: Couto, Alicia S. Universidad de Buenos Aires. Centro de Investigaciones en Hidratos de Carbono (CIHIDECAR). Departamento de Química Orgánica; Argentina.Fil: Soprano, Luciana L. ANLIS Dr. C.G.Malbrán. Intituto Nacional de Parasitología "Dr. Mario Fatala Chaben". Departamento de investigación; Argentina.Fil: Landoni, Malena. Universidad de Buenos Aires. Centro de Investigaciones en Hidratos de Carbono (CIHIDECAR). Departamento de Química Orgánica; Argentina.Fil: Pourcelot, Marilyne. Université de Picardie Jules Verne. Laboratoire des Glucides; Francia.Fil: Acosta, Diana M. ANLIS Dr. C.G.Malbrán. Intituto Nacional de Parasitología "Dr. Mario Fatala Chaben". Departamento de investigación; Argentina.Fil: Bultel, Laurent. Université de Picardie Jules Verne. Laboratoire des Glucides; Francia.Fil: Parente, Juliana E. Universidad de Buenos Aires. Centro de Investigaciones en Hidratos de Carbono (CIHIDECAR). Departamento de Química Orgánica; Argentina.Fil: Ferrero, Maximiliano R. ANLIS Dr. C.G.Malbrán. Intituto Nacional de Parasitología "Dr. Mario Fatala Chaben". Departamento de investigación; Argentina.Fil: Barbier, Maximilien. Université de Picardie Jules Verne. Laboratoire des Glucides; Francia.Fil: Dussouy, Christophe. Université de Picardie Jules Verne. Laboratoire des Glucides; Francia.Fil: Esteva, Monica I. ANLIS Dr. C.G.Malbrán. Intituto Nacional de Parasitología "Dr. Mario Fatala Chaben". Departamento de investigación; Argentina.Fil: Kovensky, José. Université de Picardie Jules Verne. Laboratoire des Glucides; Francia.Fil: Duschak, Vilma G. ANLIS Dr. C.G.Malbrán. Intituto Nacional de Parasitología "Dr. Mario Fatala Chaben". Departamento de investigación; Argentina.Cruzipain (Cz), the major cysteine proteinase of Trypanosoma cruzi, is a glycoprotein that contains sulfated high-mannose-type oligosaccharides. We have previously determined that these sulfate groups are targets of specific immune responses. In order to evaluate the structural requirements for antibody recognition of Cz, a systematic structure-activity study of the chemical characteristics needed for antibody binding to the Cz sulfated epitope was performed by immunoassays. With this aim, different synthesized molecules were coupled to the proteins BSA and aprotinin and confronted with (a) mouse sera specific for Cz and its carboxy-terminal (C-T) domain, (b) antibodies raised in rabbits immunized with Cz and its C-terminal domain and (c) IgGs purified from human Chagas disease sera. Our results indicate that a glucosamine containing an esterifying sulfate group in position O-6 and an N-acetyl group was the preferred epitope for the immune recognition of sera specific for Cz and its C-T domain. Although to a minor extent, other anionic compounds bearing sulfate groups in different positions and number as well as different anionic charged groups including carboxylated or phosphorylated monosaccharides, disaccharides and oligosaccharides were recognized. In conclusion, we found that synthetic anionic sugar conjugates containing N-acetyl d-glucosamine-6-sulfate sodium salt (GlcNAc6S) competitively inhibit the binding of affinity purified rabbit anti-C-T IgG to the C-T extension of Cz. Extending these findings to the context of natural infection, immune assays performed with Chagas disease serum confirmed that the structure of synthetic GlcNAc6S mimics the N-glycan-linked sulfated epitope displayed in the C-T domain of Cz.2012-10info:ar-repo/semantics/articuloinfo:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionapplication/pdfhttp://sgc.anlis.gob.ar/handle/123456789/148310.1111/j.1742-4658.2012.08728.x#PLACEHOLDER_PARENT_METADATA_VALUE#datasetsThe FEBS journalenginfo:eu-repo/semantics/openAccessreponame:Sistema de Gestión del Conocimiento ANLIS MALBRÁNinstname:Administración Nacional de Laboratorios e Institutos de Salud "Dr. Carlos G. Malbrán"instacron:ANLIS2025-09-04T11:17:12Zoai:sgc.anlis.gob.ar:123456789/1483Institucionalhttp://sgc.anlis.gob.ar/Organismo científico-tecnológicoNo correspondehttp://sgc.anlis.gob.ar/oai/biblioteca@anlis.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:a2025-09-04 11:17:12.413Sistema 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 |
An anionic synthetic sugar containing 6-SO3 -NAcGlc mimics the sulfated cruzipain epitope that plays a central role in immune recognition |
title |
An anionic synthetic sugar containing 6-SO3 -NAcGlc mimics the sulfated cruzipain epitope that plays a central role in immune recognition |
spellingShingle |
An anionic synthetic sugar containing 6-SO3 -NAcGlc mimics the sulfated cruzipain epitope that plays a central role in immune recognition Couto, Alicia S Enfermedad de Chagas Sitios de Unión de Anticuerpos Glucosamina |
title_short |
An anionic synthetic sugar containing 6-SO3 -NAcGlc mimics the sulfated cruzipain epitope that plays a central role in immune recognition |
title_full |
An anionic synthetic sugar containing 6-SO3 -NAcGlc mimics the sulfated cruzipain epitope that plays a central role in immune recognition |
title_fullStr |
An anionic synthetic sugar containing 6-SO3 -NAcGlc mimics the sulfated cruzipain epitope that plays a central role in immune recognition |
title_full_unstemmed |
An anionic synthetic sugar containing 6-SO3 -NAcGlc mimics the sulfated cruzipain epitope that plays a central role in immune recognition |
title_sort |
An anionic synthetic sugar containing 6-SO3 -NAcGlc mimics the sulfated cruzipain epitope that plays a central role in immune recognition |
dc.creator.none.fl_str_mv |
Couto, Alicia S Soprano, Luciana L Landoni, Malena Pourcelot, Marilyne Acosta, Diana M Bultel, Laurent Parente, Juliana E Ferrero, Maximiliano R Barbier, Maximilien Dussouy, Christophe Esteva, Monica I Kovensky, José Duschak, Vilma G |
author |
Couto, Alicia S |
author_facet |
Couto, Alicia S Soprano, Luciana L Landoni, Malena Pourcelot, Marilyne Acosta, Diana M Bultel, Laurent Parente, Juliana E Ferrero, Maximiliano R Barbier, Maximilien Dussouy, Christophe Esteva, Monica I Kovensky, José Duschak, Vilma G |
author_role |
author |
author2 |
Soprano, Luciana L Landoni, Malena Pourcelot, Marilyne Acosta, Diana M Bultel, Laurent Parente, Juliana E Ferrero, Maximiliano R Barbier, Maximilien Dussouy, Christophe Esteva, Monica I Kovensky, José Duschak, Vilma G |
author2_role |
author author author author author author author author author author author author |
dc.subject.none.fl_str_mv |
Enfermedad de Chagas Sitios de Unión de Anticuerpos Glucosamina |
topic |
Enfermedad de Chagas Sitios de Unión de Anticuerpos Glucosamina |
dc.description.none.fl_txt_mv |
Fil: Couto, Alicia S. Universidad de Buenos Aires. Centro de Investigaciones en Hidratos de Carbono (CIHIDECAR). Departamento de Química Orgánica; Argentina. Fil: Soprano, Luciana L. ANLIS Dr. C.G.Malbrán. Intituto Nacional de Parasitología "Dr. Mario Fatala Chaben". Departamento de investigación; Argentina. Fil: Landoni, Malena. Universidad de Buenos Aires. Centro de Investigaciones en Hidratos de Carbono (CIHIDECAR). Departamento de Química Orgánica; Argentina. Fil: Pourcelot, Marilyne. Université de Picardie Jules Verne. Laboratoire des Glucides; Francia. Fil: Acosta, Diana M. ANLIS Dr. C.G.Malbrán. Intituto Nacional de Parasitología "Dr. Mario Fatala Chaben". Departamento de investigación; Argentina. Fil: Bultel, Laurent. Université de Picardie Jules Verne. Laboratoire des Glucides; Francia. Fil: Parente, Juliana E. Universidad de Buenos Aires. Centro de Investigaciones en Hidratos de Carbono (CIHIDECAR). Departamento de Química Orgánica; Argentina. Fil: Ferrero, Maximiliano R. ANLIS Dr. C.G.Malbrán. Intituto Nacional de Parasitología "Dr. Mario Fatala Chaben". Departamento de investigación; Argentina. Fil: Barbier, Maximilien. Université de Picardie Jules Verne. Laboratoire des Glucides; Francia. Fil: Dussouy, Christophe. Université de Picardie Jules Verne. Laboratoire des Glucides; Francia. Fil: Esteva, Monica I. ANLIS Dr. C.G.Malbrán. Intituto Nacional de Parasitología "Dr. Mario Fatala Chaben". Departamento de investigación; Argentina. Fil: Kovensky, José. Université de Picardie Jules Verne. Laboratoire des Glucides; Francia. Fil: Duschak, Vilma G. ANLIS Dr. C.G.Malbrán. Intituto Nacional de Parasitología "Dr. Mario Fatala Chaben". Departamento de investigación; Argentina. Cruzipain (Cz), the major cysteine proteinase of Trypanosoma cruzi, is a glycoprotein that contains sulfated high-mannose-type oligosaccharides. We have previously determined that these sulfate groups are targets of specific immune responses. In order to evaluate the structural requirements for antibody recognition of Cz, a systematic structure-activity study of the chemical characteristics needed for antibody binding to the Cz sulfated epitope was performed by immunoassays. With this aim, different synthesized molecules were coupled to the proteins BSA and aprotinin and confronted with (a) mouse sera specific for Cz and its carboxy-terminal (C-T) domain, (b) antibodies raised in rabbits immunized with Cz and its C-terminal domain and (c) IgGs purified from human Chagas disease sera. Our results indicate that a glucosamine containing an esterifying sulfate group in position O-6 and an N-acetyl group was the preferred epitope for the immune recognition of sera specific for Cz and its C-T domain. Although to a minor extent, other anionic compounds bearing sulfate groups in different positions and number as well as different anionic charged groups including carboxylated or phosphorylated monosaccharides, disaccharides and oligosaccharides were recognized. In conclusion, we found that synthetic anionic sugar conjugates containing N-acetyl d-glucosamine-6-sulfate sodium salt (GlcNAc6S) competitively inhibit the binding of affinity purified rabbit anti-C-T IgG to the C-T extension of Cz. Extending these findings to the context of natural infection, immune assays performed with Chagas disease serum confirmed that the structure of synthetic GlcNAc6S mimics the N-glycan-linked sulfated epitope displayed in the C-T domain of Cz. |
description |
Fil: Couto, Alicia S. Universidad de Buenos Aires. Centro de Investigaciones en Hidratos de Carbono (CIHIDECAR). Departamento de Química Orgánica; Argentina. |
publishDate |
2012 |
dc.date.none.fl_str_mv |
2012-10 |
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/123456789/1483 10.1111/j.1742-4658.2012.08728.x |
url |
http://sgc.anlis.gob.ar/handle/123456789/1483 |
identifier_str_mv |
10.1111/j.1742-4658.2012.08728.x |
dc.language.none.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
#PLACEHOLDER_PARENT_METADATA_VALUE# datasets The FEBS journal |
dc.rights.none.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
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application/pdf |
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reponame:Sistema de Gestión del Conocimiento ANLIS MALBRÁN instname:Administración Nacional de Laboratorios e Institutos de Salud "Dr. Carlos G. Malbrán" instacron:ANLIS |
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Sistema de Gestión del Conocimiento ANLIS MALBRÁN |
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Sistema de Gestión del Conocimiento ANLIS MALBRÁN |
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Administración Nacional de Laboratorios e Institutos de Salud "Dr. Carlos G. Malbrán" |
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Sistema de Gestión del Conocimiento ANLIS MALBRÁN - Administración Nacional de Laboratorios e Institutos de Salud "Dr. Carlos G. Malbrán" |
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12.623145 |