An anionic synthetic sugar containing 6-SO3-NAcGlc mimics the sulfated cruzipain epitope that plays a central role in immune recognition

Autores
Couto, Alicia Susana; Soprano, Luciana Lía; Landoni, Malena; Pourcelot, Marilyne; Acosta, Diana Maria; Bultel, Laurent; Parente, Juliana Elena; Ferrero, Maximiliano Ruben; Barbier, Maximilien; Dussouy, Christophe; Esteva, Mónica Inés; Kovensky, Jose Eduardo; Duschak, Vilma Gladys
Año de publicación
2012
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
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.
Fil: Couto, Alicia Susana. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Centro de Investigaciones en Hidratos de Carbono. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Centro de Investigaciones en Hidratos de Carbono; Argentina
Fil: Soprano, Luciana Lía. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Dirección Nacional de Instituto de Investigación. Administración Nacional de Laboratorio e Instituto de Salud "Dr. C. G. Malbrán". Instituto Nacional de Parasitología "Dr. Mario Fatala Chaben"; Argentina
Fil: Landoni, Malena. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Centro de Investigaciones en Hidratos de Carbono. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Centro de Investigaciones en Hidratos de Carbono; Argentina
Fil: Pourcelot, Marilyne. Universite de Picardie Jules Verne (universite de Picardie Jules V);
Fil: Acosta, Diana Maria. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Dirección Nacional de Instituto de Investigación. Administración Nacional de Laboratorio e Instituto de Salud "Dr. C. G. Malbrán". Instituto Nacional de Parasitología "Dr. Mario Fatala Chaben"; Argentina
Fil: Bultel, Laurent. Universite de Picardie Jules Verne (universite de Picardie Jules V);
Fil: Parente, Juliana Elena. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Centro de Investigaciones en Hidratos de Carbono. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Centro de Investigaciones en Hidratos de Carbono; Argentina
Fil: Ferrero, Maximiliano Ruben. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Dirección Nacional de Instituto de Investigación. Administración Nacional de Laboratorio e Instituto de Salud "Dr. C. G. Malbrán". Instituto Nacional de Parasitología "Dr. Mario Fatala Chaben"; Argentina
Fil: Barbier, Maximilien. Universite de Picardie Jules Verne (universite de Picardie Jules V);
Fil: Dussouy, Christophe. Universite de Picardie Jules Verne (universite de Picardie Jules V);
Fil: Esteva, Mónica Inés. Dirección Nacional de Instituto de Investigación. Administración Nacional de Laboratorio e Instituto de Salud "Dr. C. G. Malbrán". Instituto Nacional de Parasitología "Dr. Mario Fatala Chaben"; Argentina
Fil: Kovensky, Jose Eduardo. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universite de Picardie Jules Verne (universite de Picardie Jules V);
Fil: Duschak, Vilma Gladys. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Dirección Nacional de Instituto de Investigación. Administración Nacional de Laboratorio e Instituto de Salud "Dr. C. G. Malbrán". Instituto Nacional de Parasitología "Dr. Mario Fatala Chaben"; Argentina
Materia
CRUZIPAIN
GLYCOPROTEIN
SULFATED GLCNAC
TRYPANOSOMA CRUZI
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/236663
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/236663
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling An anionic synthetic sugar containing 6-SO3-NAcGlc mimics the sulfated cruzipain epitope that plays a central role in immune recognitionCouto, Alicia SusanaSoprano, Luciana LíaLandoni, MalenaPourcelot, MarilyneAcosta, Diana MariaBultel, LaurentParente, Juliana ElenaFerrero, Maximiliano RubenBarbier, MaximilienDussouy, ChristopheEsteva, Mónica InésKovensky, Jose EduardoDuschak, Vilma GladysCRUZIPAINGLYCOPROTEINSULFATED GLCNACTRYPANOSOMA CRUZIhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Cruzipain (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.Fil: Couto, Alicia Susana. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Centro de Investigaciones en Hidratos de Carbono. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Centro de Investigaciones en Hidratos de Carbono; ArgentinaFil: Soprano, Luciana Lía. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Dirección Nacional de Instituto de Investigación. Administración Nacional de Laboratorio e Instituto de Salud "Dr. C. G. Malbrán". Instituto Nacional de Parasitología "Dr. Mario Fatala Chaben"; ArgentinaFil: Landoni, Malena. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Centro de Investigaciones en Hidratos de Carbono. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Centro de Investigaciones en Hidratos de Carbono; ArgentinaFil: Pourcelot, Marilyne. Universite de Picardie Jules Verne (universite de Picardie Jules V);Fil: Acosta, Diana Maria. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Dirección Nacional de Instituto de Investigación. Administración Nacional de Laboratorio e Instituto de Salud "Dr. C. G. Malbrán". Instituto Nacional de Parasitología "Dr. Mario Fatala Chaben"; ArgentinaFil: Bultel, Laurent. Universite de Picardie Jules Verne (universite de Picardie Jules V);Fil: Parente, Juliana Elena. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Centro de Investigaciones en Hidratos de Carbono. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Centro de Investigaciones en Hidratos de Carbono; ArgentinaFil: Ferrero, Maximiliano Ruben. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Dirección Nacional de Instituto de Investigación. Administración Nacional de Laboratorio e Instituto de Salud "Dr. C. G. Malbrán". Instituto Nacional de Parasitología "Dr. Mario Fatala Chaben"; ArgentinaFil: Barbier, Maximilien. Universite de Picardie Jules Verne (universite de Picardie Jules V);Fil: Dussouy, Christophe. Universite de Picardie Jules Verne (universite de Picardie Jules V);Fil: Esteva, Mónica Inés. Dirección Nacional de Instituto de Investigación. Administración Nacional de Laboratorio e Instituto de Salud "Dr. C. G. Malbrán". Instituto Nacional de Parasitología "Dr. Mario Fatala Chaben"; ArgentinaFil: Kovensky, Jose Eduardo. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universite de Picardie Jules Verne (universite de Picardie Jules V);Fil: Duschak, Vilma Gladys. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Dirección Nacional de Instituto de Investigación. Administración Nacional de Laboratorio e Instituto de Salud "Dr. C. G. Malbrán". Instituto Nacional de Parasitología "Dr. Mario Fatala Chaben"; ArgentinaWiley Blackwell Publishing, Inc2012-10info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/236663Couto, Alicia Susana; Soprano, Luciana Lía; Landoni, Malena; Pourcelot, Marilyne; Acosta, Diana Maria; et al.; An anionic synthetic sugar containing 6-SO3-NAcGlc mimics the sulfated cruzipain epitope that plays a central role in immune recognition; Wiley Blackwell Publishing, Inc; Febs Journal; 279; 19; 10-2012; 3665-36791742-464XCONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://febs.onlinelibrary.wiley.com/doi/full/10.1111/j.1742-4658.2012.08728.xinfo:eu-repo/semantics/altIdentifier/doi/10.1111/j.1742-4658.2012.08728.xinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T09:34:37Zoai:ri.conicet.gov.ar:11336/236663instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-29 09:34:37.474CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
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 Susana
CRUZIPAIN
GLYCOPROTEIN
SULFATED GLCNAC
TRYPANOSOMA CRUZI
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 Susana
Soprano, Luciana Lía
Landoni, Malena
Pourcelot, Marilyne
Acosta, Diana Maria
Bultel, Laurent
Parente, Juliana Elena
Ferrero, Maximiliano Ruben
Barbier, Maximilien
Dussouy, Christophe
Esteva, Mónica Inés
Kovensky, Jose Eduardo
Duschak, Vilma Gladys
author Couto, Alicia Susana
author_facet Couto, Alicia Susana
Soprano, Luciana Lía
Landoni, Malena
Pourcelot, Marilyne
Acosta, Diana Maria
Bultel, Laurent
Parente, Juliana Elena
Ferrero, Maximiliano Ruben
Barbier, Maximilien
Dussouy, Christophe
Esteva, Mónica Inés
Kovensky, Jose Eduardo
Duschak, Vilma Gladys
author_role author
author2 Soprano, Luciana Lía
Landoni, Malena
Pourcelot, Marilyne
Acosta, Diana Maria
Bultel, Laurent
Parente, Juliana Elena
Ferrero, Maximiliano Ruben
Barbier, Maximilien
Dussouy, Christophe
Esteva, Mónica Inés
Kovensky, Jose Eduardo
Duschak, Vilma Gladys
author2_role author
author
author
author
author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv CRUZIPAIN
GLYCOPROTEIN
SULFATED GLCNAC
TRYPANOSOMA CRUZI
topic CRUZIPAIN
GLYCOPROTEIN
SULFATED GLCNAC
TRYPANOSOMA CRUZI
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv 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.
Fil: Couto, Alicia Susana. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Centro de Investigaciones en Hidratos de Carbono. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Centro de Investigaciones en Hidratos de Carbono; Argentina
Fil: Soprano, Luciana Lía. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Dirección Nacional de Instituto de Investigación. Administración Nacional de Laboratorio e Instituto de Salud "Dr. C. G. Malbrán". Instituto Nacional de Parasitología "Dr. Mario Fatala Chaben"; Argentina
Fil: Landoni, Malena. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Centro de Investigaciones en Hidratos de Carbono. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Centro de Investigaciones en Hidratos de Carbono; Argentina
Fil: Pourcelot, Marilyne. Universite de Picardie Jules Verne (universite de Picardie Jules V);
Fil: Acosta, Diana Maria. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Dirección Nacional de Instituto de Investigación. Administración Nacional de Laboratorio e Instituto de Salud "Dr. C. G. Malbrán". Instituto Nacional de Parasitología "Dr. Mario Fatala Chaben"; Argentina
Fil: Bultel, Laurent. Universite de Picardie Jules Verne (universite de Picardie Jules V);
Fil: Parente, Juliana Elena. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Centro de Investigaciones en Hidratos de Carbono. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Centro de Investigaciones en Hidratos de Carbono; Argentina
Fil: Ferrero, Maximiliano Ruben. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Dirección Nacional de Instituto de Investigación. Administración Nacional de Laboratorio e Instituto de Salud "Dr. C. G. Malbrán". Instituto Nacional de Parasitología "Dr. Mario Fatala Chaben"; Argentina
Fil: Barbier, Maximilien. Universite de Picardie Jules Verne (universite de Picardie Jules V);
Fil: Dussouy, Christophe. Universite de Picardie Jules Verne (universite de Picardie Jules V);
Fil: Esteva, Mónica Inés. Dirección Nacional de Instituto de Investigación. Administración Nacional de Laboratorio e Instituto de Salud "Dr. C. G. Malbrán". Instituto Nacional de Parasitología "Dr. Mario Fatala Chaben"; Argentina
Fil: Kovensky, Jose Eduardo. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universite de Picardie Jules Verne (universite de Picardie Jules V);
Fil: Duschak, Vilma Gladys. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Dirección Nacional de Instituto de Investigación. Administración Nacional de Laboratorio e Instituto de Salud "Dr. C. G. Malbrán". Instituto Nacional de Parasitología "Dr. Mario Fatala Chaben"; Argentina
description 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.
publishDate 2012
dc.date.none.fl_str_mv 2012-10
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/236663
Couto, Alicia Susana; Soprano, Luciana Lía; Landoni, Malena; Pourcelot, Marilyne; Acosta, Diana Maria; et al.; An anionic synthetic sugar containing 6-SO3-NAcGlc mimics the sulfated cruzipain epitope that plays a central role in immune recognition; Wiley Blackwell Publishing, Inc; Febs Journal; 279; 19; 10-2012; 3665-3679
1742-464X
CONICET Digital
CONICET
url http://hdl.handle.net/11336/236663
identifier_str_mv Couto, Alicia Susana; Soprano, Luciana Lía; Landoni, Malena; Pourcelot, Marilyne; Acosta, Diana Maria; et al.; An anionic synthetic sugar containing 6-SO3-NAcGlc mimics the sulfated cruzipain epitope that plays a central role in immune recognition; Wiley Blackwell Publishing, Inc; Febs Journal; 279; 19; 10-2012; 3665-3679
1742-464X
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
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info:eu-repo/semantics/altIdentifier/doi/10.1111/j.1742-4658.2012.08728.x
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
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dc.publisher.none.fl_str_mv Wiley Blackwell Publishing, Inc
publisher.none.fl_str_mv Wiley Blackwell Publishing, Inc
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instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
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repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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