Mutation of the surface layer protein SlpB has pleiotropic effects in the probiotic propionibacterium freudenreichii CIRM-BIA 129

Autores
do Carmo, Fillipe L. R.; Marques Da Silva, Wanderson; Tavares, Guilherme C.; Ibraim, Izabela C.; Cordeiro, Barbara F.; Oliveira, Emiliano R.; Rabah, Houem; Cauty, Chantal; da Silva, Sara H.; Canário Viana, Marcus V.; Caetano, Ana C. B.; dos Santos, Roselane G.; de Oliveira Carvalho, Rodrigo D.; Jardin, Julien; Pereira, Felipe L.; Folador, Edson L.; Le Loir, Yves; Figueiredo, Henrique C. P.; Jan, Gwénaël; Azevedo, Vasco
Año de publicación
2018
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Propionibacterium freudenreichii is a beneficial Gram-positive bacterium, traditionally used as a cheese-ripening starter, and currently considered as an emerging probiotic. As an example, the P. freudenreichii CIRM-BIA 129 strain recently revealed promising immunomodulatory properties. Its consumption accordingly exerts healing effects in different animal models of colitis, suggesting a potent role in the context of inflammatory bowel diseases. This anti-inflammatory effect depends on surface layer proteins (SLPs). SLPs may be involved in key functions in probiotics, such as persistence within the gut, adhesion to host cells and mucus, or immunomodulation. Several SLPs coexist in P. freudenreichii CIRM-BIA 129 and mediate immunomodulation and adhesion. A mutant P. freudenreichii CIRM-BIA 129ΔslpB (CB129ΔslpB) strain was shown to exhibit decreased adhesion to intestinal epithelial cells. In the present study, we thoroughly analyzed the impact of this mutation on cellular properties. Firstly, we investigated alterations of surface properties in CB129ΔslpB. Surface extractable proteins, surface charges (ζ-potential) and surface hydrophobicity were affected by the mutation. Whole-cell proteomics, using high definition mass spectrometry, identified 1,288 quantifiable proteins in the wild-type strain, i.e., 53% of the theoretical proteome predicted according to P. freudenreichii CIRM-BIA 129 genome sequence. In the mutant strain, we detected 1,252 proteins, including 1,227 proteins in common with the wild-type strain. Comparative quantitative analysis revealed 97 proteins with significant differences between wild-type and mutant strains. These proteins are involved in various cellular process like signaling, metabolism, and DNA repair and replication. Finally, in silico analysis predicted that slpB gene is not part of an operon, thus not affecting the downstream genes after gene knockout. This study, in accordance with the various roles attributed in the literature to SLPs, revealed a pleiotropic effect of a single slpB mutation, in the probiotic P. freudenreichii. This suggests that SlpB may be at a central node of cellular processes and confirms that both nature and amount of SLPs, which are highly variable within the P. freudenreichii species, determine the probiotic abilities of strains.
Fil: do Carmo, Fillipe L. R.. Institut National de la Recherche Agronomique; Francia. Universidade Federal de Minas Gerais. Instituto de Ciências Biológicas; Brasil
Fil: Marques Da Silva, Wanderson. Instituto Nacional de Tecnología Agropecuaria. Centro de Investigación en Ciencias Veterinarias y Agronómicas. Instituto de Biotecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Tavares, Guilherme C.. Universidade Federal de Minas Gerais; Brasil
Fil: Ibraim, Izabela C.. Universidade Federal de Minas Gerais. Instituto de Ciências Biológicas; Brasil
Fil: Cordeiro, Barbara F.. Universidade Federal de Minas Gerais. Instituto de Ciências Biológicas; Brasil
Fil: Oliveira, Emiliano R.. Universidade Federal de Minas Gerais. Instituto de Ciências Biológicas; Brasil
Fil: Rabah, Houem. Institut National de la Recherche Agronomique; Francia
Fil: Cauty, Chantal. Institut National de la Recherche Agronomique; Francia
Fil: da Silva, Sara H.. Universidade Federal de Minas Gerais. Instituto de Ciências Biológicas; Brasil
Fil: Canário Viana, Marcus V.. Universidade Federal de Minas Gerais. Instituto de Ciências Biológicas; Brasil
Fil: Caetano, Ana C. B.. Universidade Federal de Minas Gerais. Instituto de Ciências Biológicas; Brasil
Fil: dos Santos, Roselane G.. Universidade Federal de Minas Gerais. Instituto de Ciências Biológicas; Brasil
Fil: de Oliveira Carvalho, Rodrigo D.. Instituto de Ciencias Da Saúde; Brasil
Fil: Jardin, Julien. Institut National de la Recherche Agronomique; Francia
Fil: Pereira, Felipe L.. Universidade Federal de Minas Gerais; Brasil
Fil: Folador, Edson L.. Universidade Estadual da Paraiba; Brasil
Fil: Le Loir, Yves. Institut National de la Recherche Agronomique; Francia
Fil: Figueiredo, Henrique C. P.. Universidade Federal de Minas Gerais; Brasil
Fil: Jan, Gwénaël. Institut National de la Recherche Agronomique; Francia
Fil: Azevedo, Vasco. Universidade Federal de Minas Gerais. Instituto de Ciências Biológicas; Brasil
Materia
BACTERIA GENOMIC
BACTERIA PROTEOMIC
HDMSE
SHOTGUN PROTEOMIC
SURFACE LAYER PROTEIN
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/177751
Acceder
id CONICETDig_bbe789ccc1b306b3f0254b938b39ed04
oai_identifier_str oai:ri.conicet.gov.ar:11336/177751
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Mutation of the surface layer protein SlpB has pleiotropic effects in the probiotic propionibacterium freudenreichii CIRM-BIA 129do Carmo, Fillipe L. R.Marques Da Silva, WandersonTavares, Guilherme C.Ibraim, Izabela C.Cordeiro, Barbara F.Oliveira, Emiliano R.Rabah, HouemCauty, Chantalda Silva, Sara H.Canário Viana, Marcus V.Caetano, Ana C. B.dos Santos, Roselane G.de Oliveira Carvalho, Rodrigo D.Jardin, JulienPereira, Felipe L.Folador, Edson L.Le Loir, YvesFigueiredo, Henrique C. P.Jan, GwénaëlAzevedo, VascoBACTERIA GENOMICBACTERIA PROTEOMICHDMSESHOTGUN PROTEOMICSURFACE LAYER PROTEINhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Propionibacterium freudenreichii is a beneficial Gram-positive bacterium, traditionally used as a cheese-ripening starter, and currently considered as an emerging probiotic. As an example, the P. freudenreichii CIRM-BIA 129 strain recently revealed promising immunomodulatory properties. Its consumption accordingly exerts healing effects in different animal models of colitis, suggesting a potent role in the context of inflammatory bowel diseases. This anti-inflammatory effect depends on surface layer proteins (SLPs). SLPs may be involved in key functions in probiotics, such as persistence within the gut, adhesion to host cells and mucus, or immunomodulation. Several SLPs coexist in P. freudenreichii CIRM-BIA 129 and mediate immunomodulation and adhesion. A mutant P. freudenreichii CIRM-BIA 129ΔslpB (CB129ΔslpB) strain was shown to exhibit decreased adhesion to intestinal epithelial cells. In the present study, we thoroughly analyzed the impact of this mutation on cellular properties. Firstly, we investigated alterations of surface properties in CB129ΔslpB. Surface extractable proteins, surface charges (ζ-potential) and surface hydrophobicity were affected by the mutation. Whole-cell proteomics, using high definition mass spectrometry, identified 1,288 quantifiable proteins in the wild-type strain, i.e., 53% of the theoretical proteome predicted according to P. freudenreichii CIRM-BIA 129 genome sequence. In the mutant strain, we detected 1,252 proteins, including 1,227 proteins in common with the wild-type strain. Comparative quantitative analysis revealed 97 proteins with significant differences between wild-type and mutant strains. These proteins are involved in various cellular process like signaling, metabolism, and DNA repair and replication. Finally, in silico analysis predicted that slpB gene is not part of an operon, thus not affecting the downstream genes after gene knockout. This study, in accordance with the various roles attributed in the literature to SLPs, revealed a pleiotropic effect of a single slpB mutation, in the probiotic P. freudenreichii. This suggests that SlpB may be at a central node of cellular processes and confirms that both nature and amount of SLPs, which are highly variable within the P. freudenreichii species, determine the probiotic abilities of strains.Fil: do Carmo, Fillipe L. R.. Institut National de la Recherche Agronomique; Francia. Universidade Federal de Minas Gerais. Instituto de Ciências Biológicas; BrasilFil: Marques Da Silva, Wanderson. Instituto Nacional de Tecnología Agropecuaria. Centro de Investigación en Ciencias Veterinarias y Agronómicas. Instituto de Biotecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Tavares, Guilherme C.. Universidade Federal de Minas Gerais; BrasilFil: Ibraim, Izabela C.. Universidade Federal de Minas Gerais. Instituto de Ciências Biológicas; BrasilFil: Cordeiro, Barbara F.. Universidade Federal de Minas Gerais. Instituto de Ciências Biológicas; BrasilFil: Oliveira, Emiliano R.. Universidade Federal de Minas Gerais. Instituto de Ciências Biológicas; BrasilFil: Rabah, Houem. Institut National de la Recherche Agronomique; FranciaFil: Cauty, Chantal. Institut National de la Recherche Agronomique; FranciaFil: da Silva, Sara H.. Universidade Federal de Minas Gerais. Instituto de Ciências Biológicas; BrasilFil: Canário Viana, Marcus V.. Universidade Federal de Minas Gerais. Instituto de Ciências Biológicas; BrasilFil: Caetano, Ana C. B.. Universidade Federal de Minas Gerais. Instituto de Ciências Biológicas; BrasilFil: dos Santos, Roselane G.. Universidade Federal de Minas Gerais. Instituto de Ciências Biológicas; BrasilFil: de Oliveira Carvalho, Rodrigo D.. Instituto de Ciencias Da Saúde; BrasilFil: Jardin, Julien. Institut National de la Recherche Agronomique; FranciaFil: Pereira, Felipe L.. Universidade Federal de Minas Gerais; BrasilFil: Folador, Edson L.. Universidade Estadual da Paraiba; BrasilFil: Le Loir, Yves. Institut National de la Recherche Agronomique; FranciaFil: Figueiredo, Henrique C. P.. Universidade Federal de Minas Gerais; BrasilFil: Jan, Gwénaël. Institut National de la Recherche Agronomique; FranciaFil: Azevedo, Vasco. Universidade Federal de Minas Gerais. Instituto de Ciências Biológicas; BrasilFrontiers Media2018-08info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/177751do Carmo, Fillipe L. R.; Marques Da Silva, Wanderson; Tavares, Guilherme C.; Ibraim, Izabela C.; Cordeiro, Barbara F.; et al.; Mutation of the surface layer protein SlpB has pleiotropic effects in the probiotic propionibacterium freudenreichii CIRM-BIA 129; Frontiers Media; Frontiers in Microbiology; 9; AUG; 8-2018; 1-221664-302XCONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.frontiersin.org/article/10.3389/fmicb.2018.01807/fullinfo:eu-repo/semantics/altIdentifier/doi/10.3389/fmicb.2018.01807info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:30:14Zoai:ri.conicet.gov.ar:11336/177751instacron: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 10:30:14.908CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Mutation of the surface layer protein SlpB has pleiotropic effects in the probiotic propionibacterium freudenreichii CIRM-BIA 129
title Mutation of the surface layer protein SlpB has pleiotropic effects in the probiotic propionibacterium freudenreichii CIRM-BIA 129
spellingShingle Mutation of the surface layer protein SlpB has pleiotropic effects in the probiotic propionibacterium freudenreichii CIRM-BIA 129
do Carmo, Fillipe L. R.
BACTERIA GENOMIC
BACTERIA PROTEOMIC
HDMSE
SHOTGUN PROTEOMIC
SURFACE LAYER PROTEIN
title_short Mutation of the surface layer protein SlpB has pleiotropic effects in the probiotic propionibacterium freudenreichii CIRM-BIA 129
title_full Mutation of the surface layer protein SlpB has pleiotropic effects in the probiotic propionibacterium freudenreichii CIRM-BIA 129
title_fullStr Mutation of the surface layer protein SlpB has pleiotropic effects in the probiotic propionibacterium freudenreichii CIRM-BIA 129
title_full_unstemmed Mutation of the surface layer protein SlpB has pleiotropic effects in the probiotic propionibacterium freudenreichii CIRM-BIA 129
title_sort Mutation of the surface layer protein SlpB has pleiotropic effects in the probiotic propionibacterium freudenreichii CIRM-BIA 129
dc.creator.none.fl_str_mv do Carmo, Fillipe L. R.
Marques Da Silva, Wanderson
Tavares, Guilherme C.
Ibraim, Izabela C.
Cordeiro, Barbara F.
Oliveira, Emiliano R.
Rabah, Houem
Cauty, Chantal
da Silva, Sara H.
Canário Viana, Marcus V.
Caetano, Ana C. B.
dos Santos, Roselane G.
de Oliveira Carvalho, Rodrigo D.
Jardin, Julien
Pereira, Felipe L.
Folador, Edson L.
Le Loir, Yves
Figueiredo, Henrique C. P.
Jan, Gwénaël
Azevedo, Vasco
author do Carmo, Fillipe L. R.
author_facet do Carmo, Fillipe L. R.
Marques Da Silva, Wanderson
Tavares, Guilherme C.
Ibraim, Izabela C.
Cordeiro, Barbara F.
Oliveira, Emiliano R.
Rabah, Houem
Cauty, Chantal
da Silva, Sara H.
Canário Viana, Marcus V.
Caetano, Ana C. B.
dos Santos, Roselane G.
de Oliveira Carvalho, Rodrigo D.
Jardin, Julien
Pereira, Felipe L.
Folador, Edson L.
Le Loir, Yves
Figueiredo, Henrique C. P.
Jan, Gwénaël
Azevedo, Vasco
author_role author
author2 Marques Da Silva, Wanderson
Tavares, Guilherme C.
Ibraim, Izabela C.
Cordeiro, Barbara F.
Oliveira, Emiliano R.
Rabah, Houem
Cauty, Chantal
da Silva, Sara H.
Canário Viana, Marcus V.
Caetano, Ana C. B.
dos Santos, Roselane G.
de Oliveira Carvalho, Rodrigo D.
Jardin, Julien
Pereira, Felipe L.
Folador, Edson L.
Le Loir, Yves
Figueiredo, Henrique C. P.
Jan, Gwénaël
Azevedo, Vasco
author2_role author
author
author
author
author
author
author
author
author
author
author
author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv BACTERIA GENOMIC
BACTERIA PROTEOMIC
HDMSE
SHOTGUN PROTEOMIC
SURFACE LAYER PROTEIN
topic BACTERIA GENOMIC
BACTERIA PROTEOMIC
HDMSE
SHOTGUN PROTEOMIC
SURFACE LAYER PROTEIN
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Propionibacterium freudenreichii is a beneficial Gram-positive bacterium, traditionally used as a cheese-ripening starter, and currently considered as an emerging probiotic. As an example, the P. freudenreichii CIRM-BIA 129 strain recently revealed promising immunomodulatory properties. Its consumption accordingly exerts healing effects in different animal models of colitis, suggesting a potent role in the context of inflammatory bowel diseases. This anti-inflammatory effect depends on surface layer proteins (SLPs). SLPs may be involved in key functions in probiotics, such as persistence within the gut, adhesion to host cells and mucus, or immunomodulation. Several SLPs coexist in P. freudenreichii CIRM-BIA 129 and mediate immunomodulation and adhesion. A mutant P. freudenreichii CIRM-BIA 129ΔslpB (CB129ΔslpB) strain was shown to exhibit decreased adhesion to intestinal epithelial cells. In the present study, we thoroughly analyzed the impact of this mutation on cellular properties. Firstly, we investigated alterations of surface properties in CB129ΔslpB. Surface extractable proteins, surface charges (ζ-potential) and surface hydrophobicity were affected by the mutation. Whole-cell proteomics, using high definition mass spectrometry, identified 1,288 quantifiable proteins in the wild-type strain, i.e., 53% of the theoretical proteome predicted according to P. freudenreichii CIRM-BIA 129 genome sequence. In the mutant strain, we detected 1,252 proteins, including 1,227 proteins in common with the wild-type strain. Comparative quantitative analysis revealed 97 proteins with significant differences between wild-type and mutant strains. These proteins are involved in various cellular process like signaling, metabolism, and DNA repair and replication. Finally, in silico analysis predicted that slpB gene is not part of an operon, thus not affecting the downstream genes after gene knockout. This study, in accordance with the various roles attributed in the literature to SLPs, revealed a pleiotropic effect of a single slpB mutation, in the probiotic P. freudenreichii. This suggests that SlpB may be at a central node of cellular processes and confirms that both nature and amount of SLPs, which are highly variable within the P. freudenreichii species, determine the probiotic abilities of strains.
Fil: do Carmo, Fillipe L. R.. Institut National de la Recherche Agronomique; Francia. Universidade Federal de Minas Gerais. Instituto de Ciências Biológicas; Brasil
Fil: Marques Da Silva, Wanderson. Instituto Nacional de Tecnología Agropecuaria. Centro de Investigación en Ciencias Veterinarias y Agronómicas. Instituto de Biotecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Tavares, Guilherme C.. Universidade Federal de Minas Gerais; Brasil
Fil: Ibraim, Izabela C.. Universidade Federal de Minas Gerais. Instituto de Ciências Biológicas; Brasil
Fil: Cordeiro, Barbara F.. Universidade Federal de Minas Gerais. Instituto de Ciências Biológicas; Brasil
Fil: Oliveira, Emiliano R.. Universidade Federal de Minas Gerais. Instituto de Ciências Biológicas; Brasil
Fil: Rabah, Houem. Institut National de la Recherche Agronomique; Francia
Fil: Cauty, Chantal. Institut National de la Recherche Agronomique; Francia
Fil: da Silva, Sara H.. Universidade Federal de Minas Gerais. Instituto de Ciências Biológicas; Brasil
Fil: Canário Viana, Marcus V.. Universidade Federal de Minas Gerais. Instituto de Ciências Biológicas; Brasil
Fil: Caetano, Ana C. B.. Universidade Federal de Minas Gerais. Instituto de Ciências Biológicas; Brasil
Fil: dos Santos, Roselane G.. Universidade Federal de Minas Gerais. Instituto de Ciências Biológicas; Brasil
Fil: de Oliveira Carvalho, Rodrigo D.. Instituto de Ciencias Da Saúde; Brasil
Fil: Jardin, Julien. Institut National de la Recherche Agronomique; Francia
Fil: Pereira, Felipe L.. Universidade Federal de Minas Gerais; Brasil
Fil: Folador, Edson L.. Universidade Estadual da Paraiba; Brasil
Fil: Le Loir, Yves. Institut National de la Recherche Agronomique; Francia
Fil: Figueiredo, Henrique C. P.. Universidade Federal de Minas Gerais; Brasil
Fil: Jan, Gwénaël. Institut National de la Recherche Agronomique; Francia
Fil: Azevedo, Vasco. Universidade Federal de Minas Gerais. Instituto de Ciências Biológicas; Brasil
description Propionibacterium freudenreichii is a beneficial Gram-positive bacterium, traditionally used as a cheese-ripening starter, and currently considered as an emerging probiotic. As an example, the P. freudenreichii CIRM-BIA 129 strain recently revealed promising immunomodulatory properties. Its consumption accordingly exerts healing effects in different animal models of colitis, suggesting a potent role in the context of inflammatory bowel diseases. This anti-inflammatory effect depends on surface layer proteins (SLPs). SLPs may be involved in key functions in probiotics, such as persistence within the gut, adhesion to host cells and mucus, or immunomodulation. Several SLPs coexist in P. freudenreichii CIRM-BIA 129 and mediate immunomodulation and adhesion. A mutant P. freudenreichii CIRM-BIA 129ΔslpB (CB129ΔslpB) strain was shown to exhibit decreased adhesion to intestinal epithelial cells. In the present study, we thoroughly analyzed the impact of this mutation on cellular properties. Firstly, we investigated alterations of surface properties in CB129ΔslpB. Surface extractable proteins, surface charges (ζ-potential) and surface hydrophobicity were affected by the mutation. Whole-cell proteomics, using high definition mass spectrometry, identified 1,288 quantifiable proteins in the wild-type strain, i.e., 53% of the theoretical proteome predicted according to P. freudenreichii CIRM-BIA 129 genome sequence. In the mutant strain, we detected 1,252 proteins, including 1,227 proteins in common with the wild-type strain. Comparative quantitative analysis revealed 97 proteins with significant differences between wild-type and mutant strains. These proteins are involved in various cellular process like signaling, metabolism, and DNA repair and replication. Finally, in silico analysis predicted that slpB gene is not part of an operon, thus not affecting the downstream genes after gene knockout. This study, in accordance with the various roles attributed in the literature to SLPs, revealed a pleiotropic effect of a single slpB mutation, in the probiotic P. freudenreichii. This suggests that SlpB may be at a central node of cellular processes and confirms that both nature and amount of SLPs, which are highly variable within the P. freudenreichii species, determine the probiotic abilities of strains.
publishDate 2018
dc.date.none.fl_str_mv 2018-08
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/11336/177751
do Carmo, Fillipe L. R.; Marques Da Silva, Wanderson; Tavares, Guilherme C.; Ibraim, Izabela C.; Cordeiro, Barbara F.; et al.; Mutation of the surface layer protein SlpB has pleiotropic effects in the probiotic propionibacterium freudenreichii CIRM-BIA 129; Frontiers Media; Frontiers in Microbiology; 9; AUG; 8-2018; 1-22
1664-302X
CONICET Digital
CONICET
url http://hdl.handle.net/11336/177751
identifier_str_mv do Carmo, Fillipe L. R.; Marques Da Silva, Wanderson; Tavares, Guilherme C.; Ibraim, Izabela C.; Cordeiro, Barbara F.; et al.; Mutation of the surface layer protein SlpB has pleiotropic effects in the probiotic propionibacterium freudenreichii CIRM-BIA 129; Frontiers Media; Frontiers in Microbiology; 9; AUG; 8-2018; 1-22
1664-302X
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://www.frontiersin.org/article/10.3389/fmicb.2018.01807/full
info:eu-repo/semantics/altIdentifier/doi/10.3389/fmicb.2018.01807
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Frontiers Media
publisher.none.fl_str_mv Frontiers Media
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
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reponame_str CONICET Digital (CONICET)
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instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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score 13.070432

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