Novel, sensitive, in vitro radiolabeling assays allow the monitoring of cytosolic vimentin proteoforms by SDS-page in non-infected, mycobacterial-infected and TLR2-ligated THP-1 ce...

Autores
Asensio, Cristian Jorge Alejandro; Zampieri, Stefania; Zuppan, Karim; Guarnaccia, Corrado; Vindigni, Alessandro; Oliveira, Renato A.S.; Saklatvala, Jerry; Baralle, Francisco E.; García, Rodolfo C.
Año de publicación
2023
Idioma
inglés
Tipo de recurso
documento de conferencia
Estado
versión publicada
Descripción
Discovering low-abundant macrophage proteins/proteoforms, altered in level/PTMs during intracellular bacterial infection and innate immune responses, needs sensitive proteome screening tools in electrophoretic gels, but outperforming dyes. AIMS: to search for, in human THP1 macrophage-like cells, cytosolic proteins reproducibly altered in a time-dependent and sustained manner, at days 1-4 post-infection with mycobacteria (live or killed). METHODS: The cytosolic fraction was obtained and used in novel, post-cell harvest, cell-free, in vitro radiolabeling (IVR) assays, allowing the covalent labeling of cytosolic proteomes with P-32. Labeled proteomes were separated in 1D/2D gels to detect bands/spots with altered labeling, normalizing them against total stained and total labeled proteomes. Proteins of interest were identified by MS and characterized. Bibliometric and bioinformatic studies were initiated to interpret findings in terms of PTMs, protein-protein interactions and possible roles of altered proteins and to plan how IVR might help future studies. RESULTS: in all 12 time-course infection experiments, cytosolic vimentin (VIM) was upregulated by infection in a timedependent manner. In 3 monocytic- to-macrophage differentiation experiments (PMA-treated, non-infected), the VIM IVR increased during 4 days. We identified cytosolic kinases allowing detection of VIM with cleaved forms. Metabolic labeling in cell culture detected VIM profiles different to IVR. In WB, different antibodies and sera against other proteins often did bind non-specifically to VIM. So, to monitor minor cleavage/expression changes in VIM, IVR was more sensitive, quantitative and robust than WB. The literature indicated that VIM: a) is emerging as a multifunctional protein located in the perinuclear area, cytosol, endosomes, viral factories, cell surface, extracellular space and blood; b) has roles in auto- /xeno-/aggre-phagy, apoptosis, scaffolding of signaling complexes and in binding to DNA, RNA, phospholipids, O-GlcNAc, Rab7a, p62, HDAC6, MTOC, NFκB, NOD2, NLRP3, ERK; c) is a modulator of infectious, immune, autoimmune, inflammatory, cell stress, and fibrotic responses and is a target of toxins from many bacteria; d) has roles other than the cytoskeletal/mechanical by using different PTMs and by assembling as 1-, 2- and 4-mers, cages, and filamentous networks; e) Surface VIM binds many bacteria and viruses including SARS-Cov2; f) Non-specific WB signals might depend on VIM-Fc and/or on citrullinated VIM-Ab interactions; g) VIM can be cleaved in cells. CONCLUSIONS: IVR helped detecting dynamic changes in cytosolic VIM levels, complementing WB. IVR would help to study VIM functional diversity, to correlate VIM alterations with those in binding partners, and to study VIM as biomarker or drug-target in cell infection and/or differentiation. Dissecting pro-infection and infection-restricting VIM roles will improve our knowledge of host–pathogen interaction complexity.
Fil: Asensio, Cristian Jorge Alejandro. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tandil. Centro de Investigación Veterinaria de Tandil. Universidad Nacional del Centro de la Provincia de Buenos Aires. Centro de Investigación Veterinaria de Tandil. Provincia de Buenos Aires. Gobernación. Comision de Investigaciones Científicas. Centro de Investigación Veterinaria de Tandil; Argentina. International Centre for Genetic Engineering and Biotechnology; Italia. Kennedy Institute of Rheumatology; Reino Unido
Fil: Zampieri, Stefania. International Centre for Genetic Engineering and Biotechnology; Italia
Fil: Zuppan, Karim. International Centre for Genetic Engineering and Biotechnology; Italia
Fil: Guarnaccia, Corrado. International Centre for Genetic Engineering and Biotechnology; Italia
Fil: Vindigni, Alessandro. International Centre for Genetic Engineering and Biotechnology; Italia
Fil: Oliveira, Renato A.S.. International Centre for Genetic Engineering and Biotechnology; Italia
Fil: Saklatvala, Jerry. Kennedy Institute of Rheumatology; Reino Unido
Fil: Baralle, Francisco E.. International Centre for Genetic Engineering and Biotechnology; Italia
Fil: García, Rodolfo C.. International Centre for Genetic Engineering and Biotechnology; Italia
LXXI Reunión Científica Anual de la Sociedad Argentina de Inmunología
San Luis
Argentina
Sociedad Argentina de Inmunología
Universidad Nacional de San Luis
Materia
MACROPHAGE
BACTERIAL
INFECTION
IMMUNE
THP1
PROTEOMES
CYTOSOLIC
VIMENTIN
PATHOGEN
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:11336/245529
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/245529
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Novel, sensitive, in vitro radiolabeling assays allow the monitoring of cytosolic vimentin proteoforms by SDS-page in non-infected, mycobacterial-infected and TLR2-ligated THP-1 cells: possible vimentin roles in monocyte to macrophage differentiation, inflammationAsensio, Cristian Jorge AlejandroZampieri, StefaniaZuppan, KarimGuarnaccia, CorradoVindigni, AlessandroOliveira, Renato A.S.Saklatvala, JerryBaralle, Francisco E.García, Rodolfo C.MACROPHAGEBACTERIALINFECTIONIMMUNETHP1PROTEOMESCYTOSOLICVIMENTINPATHOGENhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Discovering low-abundant macrophage proteins/proteoforms, altered in level/PTMs during intracellular bacterial infection and innate immune responses, needs sensitive proteome screening tools in electrophoretic gels, but outperforming dyes. AIMS: to search for, in human THP1 macrophage-like cells, cytosolic proteins reproducibly altered in a time-dependent and sustained manner, at days 1-4 post-infection with mycobacteria (live or killed). METHODS: The cytosolic fraction was obtained and used in novel, post-cell harvest, cell-free, in vitro radiolabeling (IVR) assays, allowing the covalent labeling of cytosolic proteomes with P-32. Labeled proteomes were separated in 1D/2D gels to detect bands/spots with altered labeling, normalizing them against total stained and total labeled proteomes. Proteins of interest were identified by MS and characterized. Bibliometric and bioinformatic studies were initiated to interpret findings in terms of PTMs, protein-protein interactions and possible roles of altered proteins and to plan how IVR might help future studies. RESULTS: in all 12 time-course infection experiments, cytosolic vimentin (VIM) was upregulated by infection in a timedependent manner. In 3 monocytic- to-macrophage differentiation experiments (PMA-treated, non-infected), the VIM IVR increased during 4 days. We identified cytosolic kinases allowing detection of VIM with cleaved forms. Metabolic labeling in cell culture detected VIM profiles different to IVR. In WB, different antibodies and sera against other proteins often did bind non-specifically to VIM. So, to monitor minor cleavage/expression changes in VIM, IVR was more sensitive, quantitative and robust than WB. The literature indicated that VIM: a) is emerging as a multifunctional protein located in the perinuclear area, cytosol, endosomes, viral factories, cell surface, extracellular space and blood; b) has roles in auto- /xeno-/aggre-phagy, apoptosis, scaffolding of signaling complexes and in binding to DNA, RNA, phospholipids, O-GlcNAc, Rab7a, p62, HDAC6, MTOC, NFκB, NOD2, NLRP3, ERK; c) is a modulator of infectious, immune, autoimmune, inflammatory, cell stress, and fibrotic responses and is a target of toxins from many bacteria; d) has roles other than the cytoskeletal/mechanical by using different PTMs and by assembling as 1-, 2- and 4-mers, cages, and filamentous networks; e) Surface VIM binds many bacteria and viruses including SARS-Cov2; f) Non-specific WB signals might depend on VIM-Fc and/or on citrullinated VIM-Ab interactions; g) VIM can be cleaved in cells. CONCLUSIONS: IVR helped detecting dynamic changes in cytosolic VIM levels, complementing WB. IVR would help to study VIM functional diversity, to correlate VIM alterations with those in binding partners, and to study VIM as biomarker or drug-target in cell infection and/or differentiation. Dissecting pro-infection and infection-restricting VIM roles will improve our knowledge of host–pathogen interaction complexity.Fil: Asensio, Cristian Jorge Alejandro. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tandil. Centro de Investigación Veterinaria de Tandil. Universidad Nacional del Centro de la Provincia de Buenos Aires. Centro de Investigación Veterinaria de Tandil. Provincia de Buenos Aires. Gobernación. Comision de Investigaciones Científicas. Centro de Investigación Veterinaria de Tandil; Argentina. International Centre for Genetic Engineering and Biotechnology; Italia. Kennedy Institute of Rheumatology; Reino UnidoFil: Zampieri, Stefania. International Centre for Genetic Engineering and Biotechnology; ItaliaFil: Zuppan, Karim. International Centre for Genetic Engineering and Biotechnology; ItaliaFil: Guarnaccia, Corrado. International Centre for Genetic Engineering and Biotechnology; ItaliaFil: Vindigni, Alessandro. International Centre for Genetic Engineering and Biotechnology; ItaliaFil: Oliveira, Renato A.S.. International Centre for Genetic Engineering and Biotechnology; ItaliaFil: Saklatvala, Jerry. Kennedy Institute of Rheumatology; Reino UnidoFil: Baralle, Francisco E.. International Centre for Genetic Engineering and Biotechnology; ItaliaFil: García, Rodolfo C.. International Centre for Genetic Engineering and Biotechnology; ItaliaLXXI Reunión Científica Anual de la Sociedad Argentina de InmunologíaSan LuisArgentinaSociedad Argentina de InmunologíaUniversidad Nacional de San LuisUniversidad Nacional de San Luis2023info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/conferenceObjectReuniónBookhttp://purl.org/coar/resource_type/c_5794info:ar-repo/semantics/documentoDeConferenciaapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/245529Novel, sensitive, in vitro radiolabeling assays allow the monitoring of cytosolic vimentin proteoforms by SDS-page in non-infected, mycobacterial-infected and TLR2-ligated THP-1 cells: possible vimentin roles in monocyte to macrophage differentiation, inflammation; LXXI Reunión Científica Anual de la Sociedad Argentina de Inmunología; San Luis; Argentina; 2023; 128-128978-987-733-386-2CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://inmunologia.org.ar/wp-content/uploads/2023/11/Libro-de-Resumenes-LXXI-Reunion-SAI-2023.pdfNacionalinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:26:44Zoai:ri.conicet.gov.ar:11336/245529instacron: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 10:26:44.603CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Novel, sensitive, in vitro radiolabeling assays allow the monitoring of cytosolic vimentin proteoforms by SDS-page in non-infected, mycobacterial-infected and TLR2-ligated THP-1 cells: possible vimentin roles in monocyte to macrophage differentiation, inflammation
title Novel, sensitive, in vitro radiolabeling assays allow the monitoring of cytosolic vimentin proteoforms by SDS-page in non-infected, mycobacterial-infected and TLR2-ligated THP-1 cells: possible vimentin roles in monocyte to macrophage differentiation, inflammation
spellingShingle Novel, sensitive, in vitro radiolabeling assays allow the monitoring of cytosolic vimentin proteoforms by SDS-page in non-infected, mycobacterial-infected and TLR2-ligated THP-1 cells: possible vimentin roles in monocyte to macrophage differentiation, inflammation
Asensio, Cristian Jorge Alejandro
MACROPHAGE
BACTERIAL
INFECTION
IMMUNE
THP1
PROTEOMES
CYTOSOLIC
VIMENTIN
PATHOGEN
title_short Novel, sensitive, in vitro radiolabeling assays allow the monitoring of cytosolic vimentin proteoforms by SDS-page in non-infected, mycobacterial-infected and TLR2-ligated THP-1 cells: possible vimentin roles in monocyte to macrophage differentiation, inflammation
title_full Novel, sensitive, in vitro radiolabeling assays allow the monitoring of cytosolic vimentin proteoforms by SDS-page in non-infected, mycobacterial-infected and TLR2-ligated THP-1 cells: possible vimentin roles in monocyte to macrophage differentiation, inflammation
title_fullStr Novel, sensitive, in vitro radiolabeling assays allow the monitoring of cytosolic vimentin proteoforms by SDS-page in non-infected, mycobacterial-infected and TLR2-ligated THP-1 cells: possible vimentin roles in monocyte to macrophage differentiation, inflammation
title_full_unstemmed Novel, sensitive, in vitro radiolabeling assays allow the monitoring of cytosolic vimentin proteoforms by SDS-page in non-infected, mycobacterial-infected and TLR2-ligated THP-1 cells: possible vimentin roles in monocyte to macrophage differentiation, inflammation
title_sort Novel, sensitive, in vitro radiolabeling assays allow the monitoring of cytosolic vimentin proteoforms by SDS-page in non-infected, mycobacterial-infected and TLR2-ligated THP-1 cells: possible vimentin roles in monocyte to macrophage differentiation, inflammation
dc.creator.none.fl_str_mv Asensio, Cristian Jorge Alejandro
Zampieri, Stefania
Zuppan, Karim
Guarnaccia, Corrado
Vindigni, Alessandro
Oliveira, Renato A.S.
Saklatvala, Jerry
Baralle, Francisco E.
García, Rodolfo C.
author Asensio, Cristian Jorge Alejandro
author_facet Asensio, Cristian Jorge Alejandro
Zampieri, Stefania
Zuppan, Karim
Guarnaccia, Corrado
Vindigni, Alessandro
Oliveira, Renato A.S.
Saklatvala, Jerry
Baralle, Francisco E.
García, Rodolfo C.
author_role author
author2 Zampieri, Stefania
Zuppan, Karim
Guarnaccia, Corrado
Vindigni, Alessandro
Oliveira, Renato A.S.
Saklatvala, Jerry
Baralle, Francisco E.
García, Rodolfo C.
author2_role author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv MACROPHAGE
BACTERIAL
INFECTION
IMMUNE
THP1
PROTEOMES
CYTOSOLIC
VIMENTIN
PATHOGEN
topic MACROPHAGE
BACTERIAL
INFECTION
IMMUNE
THP1
PROTEOMES
CYTOSOLIC
VIMENTIN
PATHOGEN
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Discovering low-abundant macrophage proteins/proteoforms, altered in level/PTMs during intracellular bacterial infection and innate immune responses, needs sensitive proteome screening tools in electrophoretic gels, but outperforming dyes. AIMS: to search for, in human THP1 macrophage-like cells, cytosolic proteins reproducibly altered in a time-dependent and sustained manner, at days 1-4 post-infection with mycobacteria (live or killed). METHODS: The cytosolic fraction was obtained and used in novel, post-cell harvest, cell-free, in vitro radiolabeling (IVR) assays, allowing the covalent labeling of cytosolic proteomes with P-32. Labeled proteomes were separated in 1D/2D gels to detect bands/spots with altered labeling, normalizing them against total stained and total labeled proteomes. Proteins of interest were identified by MS and characterized. Bibliometric and bioinformatic studies were initiated to interpret findings in terms of PTMs, protein-protein interactions and possible roles of altered proteins and to plan how IVR might help future studies. RESULTS: in all 12 time-course infection experiments, cytosolic vimentin (VIM) was upregulated by infection in a timedependent manner. In 3 monocytic- to-macrophage differentiation experiments (PMA-treated, non-infected), the VIM IVR increased during 4 days. We identified cytosolic kinases allowing detection of VIM with cleaved forms. Metabolic labeling in cell culture detected VIM profiles different to IVR. In WB, different antibodies and sera against other proteins often did bind non-specifically to VIM. So, to monitor minor cleavage/expression changes in VIM, IVR was more sensitive, quantitative and robust than WB. The literature indicated that VIM: a) is emerging as a multifunctional protein located in the perinuclear area, cytosol, endosomes, viral factories, cell surface, extracellular space and blood; b) has roles in auto- /xeno-/aggre-phagy, apoptosis, scaffolding of signaling complexes and in binding to DNA, RNA, phospholipids, O-GlcNAc, Rab7a, p62, HDAC6, MTOC, NFκB, NOD2, NLRP3, ERK; c) is a modulator of infectious, immune, autoimmune, inflammatory, cell stress, and fibrotic responses and is a target of toxins from many bacteria; d) has roles other than the cytoskeletal/mechanical by using different PTMs and by assembling as 1-, 2- and 4-mers, cages, and filamentous networks; e) Surface VIM binds many bacteria and viruses including SARS-Cov2; f) Non-specific WB signals might depend on VIM-Fc and/or on citrullinated VIM-Ab interactions; g) VIM can be cleaved in cells. CONCLUSIONS: IVR helped detecting dynamic changes in cytosolic VIM levels, complementing WB. IVR would help to study VIM functional diversity, to correlate VIM alterations with those in binding partners, and to study VIM as biomarker or drug-target in cell infection and/or differentiation. Dissecting pro-infection and infection-restricting VIM roles will improve our knowledge of host–pathogen interaction complexity.
Fil: Asensio, Cristian Jorge Alejandro. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tandil. Centro de Investigación Veterinaria de Tandil. Universidad Nacional del Centro de la Provincia de Buenos Aires. Centro de Investigación Veterinaria de Tandil. Provincia de Buenos Aires. Gobernación. Comision de Investigaciones Científicas. Centro de Investigación Veterinaria de Tandil; Argentina. International Centre for Genetic Engineering and Biotechnology; Italia. Kennedy Institute of Rheumatology; Reino Unido
Fil: Zampieri, Stefania. International Centre for Genetic Engineering and Biotechnology; Italia
Fil: Zuppan, Karim. International Centre for Genetic Engineering and Biotechnology; Italia
Fil: Guarnaccia, Corrado. International Centre for Genetic Engineering and Biotechnology; Italia
Fil: Vindigni, Alessandro. International Centre for Genetic Engineering and Biotechnology; Italia
Fil: Oliveira, Renato A.S.. International Centre for Genetic Engineering and Biotechnology; Italia
Fil: Saklatvala, Jerry. Kennedy Institute of Rheumatology; Reino Unido
Fil: Baralle, Francisco E.. International Centre for Genetic Engineering and Biotechnology; Italia
Fil: García, Rodolfo C.. International Centre for Genetic Engineering and Biotechnology; Italia
LXXI Reunión Científica Anual de la Sociedad Argentina de Inmunología
San Luis
Argentina
Sociedad Argentina de Inmunología
Universidad Nacional de San Luis
description Discovering low-abundant macrophage proteins/proteoforms, altered in level/PTMs during intracellular bacterial infection and innate immune responses, needs sensitive proteome screening tools in electrophoretic gels, but outperforming dyes. AIMS: to search for, in human THP1 macrophage-like cells, cytosolic proteins reproducibly altered in a time-dependent and sustained manner, at days 1-4 post-infection with mycobacteria (live or killed). METHODS: The cytosolic fraction was obtained and used in novel, post-cell harvest, cell-free, in vitro radiolabeling (IVR) assays, allowing the covalent labeling of cytosolic proteomes with P-32. Labeled proteomes were separated in 1D/2D gels to detect bands/spots with altered labeling, normalizing them against total stained and total labeled proteomes. Proteins of interest were identified by MS and characterized. Bibliometric and bioinformatic studies were initiated to interpret findings in terms of PTMs, protein-protein interactions and possible roles of altered proteins and to plan how IVR might help future studies. RESULTS: in all 12 time-course infection experiments, cytosolic vimentin (VIM) was upregulated by infection in a timedependent manner. In 3 monocytic- to-macrophage differentiation experiments (PMA-treated, non-infected), the VIM IVR increased during 4 days. We identified cytosolic kinases allowing detection of VIM with cleaved forms. Metabolic labeling in cell culture detected VIM profiles different to IVR. In WB, different antibodies and sera against other proteins often did bind non-specifically to VIM. So, to monitor minor cleavage/expression changes in VIM, IVR was more sensitive, quantitative and robust than WB. The literature indicated that VIM: a) is emerging as a multifunctional protein located in the perinuclear area, cytosol, endosomes, viral factories, cell surface, extracellular space and blood; b) has roles in auto- /xeno-/aggre-phagy, apoptosis, scaffolding of signaling complexes and in binding to DNA, RNA, phospholipids, O-GlcNAc, Rab7a, p62, HDAC6, MTOC, NFκB, NOD2, NLRP3, ERK; c) is a modulator of infectious, immune, autoimmune, inflammatory, cell stress, and fibrotic responses and is a target of toxins from many bacteria; d) has roles other than the cytoskeletal/mechanical by using different PTMs and by assembling as 1-, 2- and 4-mers, cages, and filamentous networks; e) Surface VIM binds many bacteria and viruses including SARS-Cov2; f) Non-specific WB signals might depend on VIM-Fc and/or on citrullinated VIM-Ab interactions; g) VIM can be cleaved in cells. CONCLUSIONS: IVR helped detecting dynamic changes in cytosolic VIM levels, complementing WB. IVR would help to study VIM functional diversity, to correlate VIM alterations with those in binding partners, and to study VIM as biomarker or drug-target in cell infection and/or differentiation. Dissecting pro-infection and infection-restricting VIM roles will improve our knowledge of host–pathogen interaction complexity.
publishDate 2023
dc.date.none.fl_str_mv 2023
dc.type.none.fl_str_mv info:eu-repo/semantics/publishedVersion
info:eu-repo/semantics/conferenceObject
Reunión
Book
http://purl.org/coar/resource_type/c_5794
info:ar-repo/semantics/documentoDeConferencia
status_str publishedVersion
format conferenceObject
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/245529
Novel, sensitive, in vitro radiolabeling assays allow the monitoring of cytosolic vimentin proteoforms by SDS-page in non-infected, mycobacterial-infected and TLR2-ligated THP-1 cells: possible vimentin roles in monocyte to macrophage differentiation, inflammation; LXXI Reunión Científica Anual de la Sociedad Argentina de Inmunología; San Luis; Argentina; 2023; 128-128
978-987-733-386-2
CONICET Digital
CONICET
url http://hdl.handle.net/11336/245529
identifier_str_mv Novel, sensitive, in vitro radiolabeling assays allow the monitoring of cytosolic vimentin proteoforms by SDS-page in non-infected, mycobacterial-infected and TLR2-ligated THP-1 cells: possible vimentin roles in monocyte to macrophage differentiation, inflammation; LXXI Reunión Científica Anual de la Sociedad Argentina de Inmunología; San Luis; Argentina; 2023; 128-128
978-987-733-386-2
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://inmunologia.org.ar/wp-content/uploads/2023/11/Libro-de-Resumenes-LXXI-Reunion-SAI-2023.pdf
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
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dc.coverage.none.fl_str_mv Nacional
dc.publisher.none.fl_str_mv Universidad Nacional de San Luis
publisher.none.fl_str_mv Universidad Nacional de San Luis
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reponame_str CONICET Digital (CONICET)
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repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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