The interaction of Galectin-8 C -terminal domain with cell surface glycoconjugates modulates membrane elasticity to stimulate antigen uptake and presentation to CD4 T cells

Autores
Prato, Cecilia Arahi; Borbolla, Laura Victoria; Lizarraga, Leonardo; Campetella, Oscar Eduardo; Tribulatti, María Virginia
Año de publicación
2024
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Galectins constitute a family of soluble lectins with unique capacity to induce macroscale rearrangements upon interacting with cell membrane glycoconjugates. Galectin-8 is acknowledged for its role in facilitating antigen uptake and processing upon engaging with cell surface glycoconjugates on antigen-presenting cells. Galectin-8 consists of two covalently fused N- and C-terminal carbohydrate recognition domains, each exhibiting distinct glycan specificity. In this study, we utilized single N- and C-carbohydrate recognition domains recombinant proteins to dissect the nature of Galectin-8-glycan interactions during antigen internalization enhancement. Single C-carbohydrate recognition domain was able to replicate the effect of full-length Galectin-8 on antigen internalization in bone marrow-derived dendritic cells. Antigen uptake enhancement was diminished in the presence of lactose or when N-glycosylation-deficient macrophages served as antigen-presenting cells, underscoring the significance of glycan recognition. Measurement of the elastic modulus using Atomic Force Microscopy unveiled that full-length Galectin-8- and C-carbohydrate recognition domain-stimulated macrophages exhibited heightened membrane stiffness compared to untreated cells, providing a plausible mechanism for their involvement in endocytosis. C-carbohydrate recognition domain proved to be as efficient as full-length Galectin-8 in promoting antigen degradation, suggesting its implication in antigen-processing induction. Lastly, C-carbohydrate recognition domain was able to replicate full-length Galectin-8-induced antigen presentation in the major histocompatibility complex class II (MHC-II) context both in vitro and in vivo. Our findings support the notion that Galectin-8 binds through its C-carbohydrate recognition domain to cell surface N-glycans, thereby altering membrane mechanical forces conducive to soluble antigen endocytosis, processing, and presentation to cognate CD4 T cells. These findings contribute to a deeper comprehension of Galectin-8 and its mechanisms of action, paving the way for the development of more efficacious immunotherapies.
Fil: Prato, Cecilia Arahi. Universidad Nacional de San Martín. Instituto de Investigaciones Biotecnológicas. - Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Biotecnológicas; Argentina
Fil: Borbolla, Laura Victoria. Universidad Nacional de San Martín. Instituto de Investigaciones Biotecnológicas. - Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Biotecnológicas; Argentina
Fil: Lizarraga, Leonardo. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Centro de Investigaciones en Bionanociencias "Elizabeth Jares Erijman"; Argentina
Fil: Campetella, Oscar Eduardo. Universidad Nacional de San Martín. Instituto de Investigaciones Biotecnológicas. - Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Biotecnológicas; Argentina
Fil: Tribulatti, María Virginia. Universidad Nacional de San Martín. Instituto de Investigaciones Biotecnológicas. - Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Biotecnológicas; Argentina
Materia
MEMBRANE ELASTICITY
ENDOCYTOSIS
ANTIGEN UPTAKE
GALECTIN-8
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:11336/264172
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/264172
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling The interaction of Galectin-8 C -terminal domain with cell surface glycoconjugates modulates membrane elasticity to stimulate antigen uptake and presentation to CD4 T cellsPrato, Cecilia ArahiBorbolla, Laura VictoriaLizarraga, LeonardoCampetella, Oscar EduardoTribulatti, María VirginiaMEMBRANE ELASTICITYENDOCYTOSISANTIGEN UPTAKEGALECTIN-8https://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1https://purl.org/becyt/ford/1.4https://purl.org/becyt/ford/1Galectins constitute a family of soluble lectins with unique capacity to induce macroscale rearrangements upon interacting with cell membrane glycoconjugates. Galectin-8 is acknowledged for its role in facilitating antigen uptake and processing upon engaging with cell surface glycoconjugates on antigen-presenting cells. Galectin-8 consists of two covalently fused N- and C-terminal carbohydrate recognition domains, each exhibiting distinct glycan specificity. In this study, we utilized single N- and C-carbohydrate recognition domains recombinant proteins to dissect the nature of Galectin-8-glycan interactions during antigen internalization enhancement. Single C-carbohydrate recognition domain was able to replicate the effect of full-length Galectin-8 on antigen internalization in bone marrow-derived dendritic cells. Antigen uptake enhancement was diminished in the presence of lactose or when N-glycosylation-deficient macrophages served as antigen-presenting cells, underscoring the significance of glycan recognition. Measurement of the elastic modulus using Atomic Force Microscopy unveiled that full-length Galectin-8- and C-carbohydrate recognition domain-stimulated macrophages exhibited heightened membrane stiffness compared to untreated cells, providing a plausible mechanism for their involvement in endocytosis. C-carbohydrate recognition domain proved to be as efficient as full-length Galectin-8 in promoting antigen degradation, suggesting its implication in antigen-processing induction. Lastly, C-carbohydrate recognition domain was able to replicate full-length Galectin-8-induced antigen presentation in the major histocompatibility complex class II (MHC-II) context both in vitro and in vivo. Our findings support the notion that Galectin-8 binds through its C-carbohydrate recognition domain to cell surface N-glycans, thereby altering membrane mechanical forces conducive to soluble antigen endocytosis, processing, and presentation to cognate CD4 T cells. These findings contribute to a deeper comprehension of Galectin-8 and its mechanisms of action, paving the way for the development of more efficacious immunotherapies.Fil: Prato, Cecilia Arahi. Universidad Nacional de San Martín. Instituto de Investigaciones Biotecnológicas. - Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Biotecnológicas; ArgentinaFil: Borbolla, Laura Victoria. Universidad Nacional de San Martín. Instituto de Investigaciones Biotecnológicas. - Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Biotecnológicas; ArgentinaFil: Lizarraga, Leonardo. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Centro de Investigaciones en Bionanociencias "Elizabeth Jares Erijman"; ArgentinaFil: Campetella, Oscar Eduardo. Universidad Nacional de San Martín. Instituto de Investigaciones Biotecnológicas. - Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Biotecnológicas; ArgentinaFil: Tribulatti, María Virginia. Universidad Nacional de San Martín. Instituto de Investigaciones Biotecnológicas. - Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Biotecnológicas; ArgentinaOxford University Press2024-10info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/264172Prato, Cecilia Arahi; Borbolla, Laura Victoria; Lizarraga, Leonardo; Campetella, Oscar Eduardo; Tribulatti, María Virginia; The interaction of Galectin-8 C -terminal domain with cell surface glycoconjugates modulates membrane elasticity to stimulate antigen uptake and presentation to CD4 T cells; Oxford University Press; Journal of Leukocyte Biology; 117; 2; 10-2024; 1-131938-3673CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://academic.oup.com/jleukbio/advance-article/doi/10.1093/jleuko/qiae214/7811061info:eu-repo/semantics/altIdentifier/doi/10.1093/jleuko/qiae214info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-22T11:06:53Zoai:ri.conicet.gov.ar:11336/264172instacron: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:34982025-10-22 11:06:54.073CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv The interaction of Galectin-8 C -terminal domain with cell surface glycoconjugates modulates membrane elasticity to stimulate antigen uptake and presentation to CD4 T cells
title The interaction of Galectin-8 C -terminal domain with cell surface glycoconjugates modulates membrane elasticity to stimulate antigen uptake and presentation to CD4 T cells
spellingShingle The interaction of Galectin-8 C -terminal domain with cell surface glycoconjugates modulates membrane elasticity to stimulate antigen uptake and presentation to CD4 T cells
Prato, Cecilia Arahi
MEMBRANE ELASTICITY
ENDOCYTOSIS
ANTIGEN UPTAKE
GALECTIN-8
title_short The interaction of Galectin-8 C -terminal domain with cell surface glycoconjugates modulates membrane elasticity to stimulate antigen uptake and presentation to CD4 T cells
title_full The interaction of Galectin-8 C -terminal domain with cell surface glycoconjugates modulates membrane elasticity to stimulate antigen uptake and presentation to CD4 T cells
title_fullStr The interaction of Galectin-8 C -terminal domain with cell surface glycoconjugates modulates membrane elasticity to stimulate antigen uptake and presentation to CD4 T cells
title_full_unstemmed The interaction of Galectin-8 C -terminal domain with cell surface glycoconjugates modulates membrane elasticity to stimulate antigen uptake and presentation to CD4 T cells
title_sort The interaction of Galectin-8 C -terminal domain with cell surface glycoconjugates modulates membrane elasticity to stimulate antigen uptake and presentation to CD4 T cells
dc.creator.none.fl_str_mv Prato, Cecilia Arahi
Borbolla, Laura Victoria
Lizarraga, Leonardo
Campetella, Oscar Eduardo
Tribulatti, María Virginia
author Prato, Cecilia Arahi
author_facet Prato, Cecilia Arahi
Borbolla, Laura Victoria
Lizarraga, Leonardo
Campetella, Oscar Eduardo
Tribulatti, María Virginia
author_role author
author2 Borbolla, Laura Victoria
Lizarraga, Leonardo
Campetella, Oscar Eduardo
Tribulatti, María Virginia
author2_role author
author
author
author
dc.subject.none.fl_str_mv MEMBRANE ELASTICITY
ENDOCYTOSIS
ANTIGEN UPTAKE
GALECTIN-8
topic MEMBRANE ELASTICITY
ENDOCYTOSIS
ANTIGEN UPTAKE
GALECTIN-8
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
https://purl.org/becyt/ford/1.4
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Galectins constitute a family of soluble lectins with unique capacity to induce macroscale rearrangements upon interacting with cell membrane glycoconjugates. Galectin-8 is acknowledged for its role in facilitating antigen uptake and processing upon engaging with cell surface glycoconjugates on antigen-presenting cells. Galectin-8 consists of two covalently fused N- and C-terminal carbohydrate recognition domains, each exhibiting distinct glycan specificity. In this study, we utilized single N- and C-carbohydrate recognition domains recombinant proteins to dissect the nature of Galectin-8-glycan interactions during antigen internalization enhancement. Single C-carbohydrate recognition domain was able to replicate the effect of full-length Galectin-8 on antigen internalization in bone marrow-derived dendritic cells. Antigen uptake enhancement was diminished in the presence of lactose or when N-glycosylation-deficient macrophages served as antigen-presenting cells, underscoring the significance of glycan recognition. Measurement of the elastic modulus using Atomic Force Microscopy unveiled that full-length Galectin-8- and C-carbohydrate recognition domain-stimulated macrophages exhibited heightened membrane stiffness compared to untreated cells, providing a plausible mechanism for their involvement in endocytosis. C-carbohydrate recognition domain proved to be as efficient as full-length Galectin-8 in promoting antigen degradation, suggesting its implication in antigen-processing induction. Lastly, C-carbohydrate recognition domain was able to replicate full-length Galectin-8-induced antigen presentation in the major histocompatibility complex class II (MHC-II) context both in vitro and in vivo. Our findings support the notion that Galectin-8 binds through its C-carbohydrate recognition domain to cell surface N-glycans, thereby altering membrane mechanical forces conducive to soluble antigen endocytosis, processing, and presentation to cognate CD4 T cells. These findings contribute to a deeper comprehension of Galectin-8 and its mechanisms of action, paving the way for the development of more efficacious immunotherapies.
Fil: Prato, Cecilia Arahi. Universidad Nacional de San Martín. Instituto de Investigaciones Biotecnológicas. - Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Biotecnológicas; Argentina
Fil: Borbolla, Laura Victoria. Universidad Nacional de San Martín. Instituto de Investigaciones Biotecnológicas. - Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Biotecnológicas; Argentina
Fil: Lizarraga, Leonardo. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Centro de Investigaciones en Bionanociencias "Elizabeth Jares Erijman"; Argentina
Fil: Campetella, Oscar Eduardo. Universidad Nacional de San Martín. Instituto de Investigaciones Biotecnológicas. - Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Biotecnológicas; Argentina
Fil: Tribulatti, María Virginia. Universidad Nacional de San Martín. Instituto de Investigaciones Biotecnológicas. - Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Biotecnológicas; Argentina
description Galectins constitute a family of soluble lectins with unique capacity to induce macroscale rearrangements upon interacting with cell membrane glycoconjugates. Galectin-8 is acknowledged for its role in facilitating antigen uptake and processing upon engaging with cell surface glycoconjugates on antigen-presenting cells. Galectin-8 consists of two covalently fused N- and C-terminal carbohydrate recognition domains, each exhibiting distinct glycan specificity. In this study, we utilized single N- and C-carbohydrate recognition domains recombinant proteins to dissect the nature of Galectin-8-glycan interactions during antigen internalization enhancement. Single C-carbohydrate recognition domain was able to replicate the effect of full-length Galectin-8 on antigen internalization in bone marrow-derived dendritic cells. Antigen uptake enhancement was diminished in the presence of lactose or when N-glycosylation-deficient macrophages served as antigen-presenting cells, underscoring the significance of glycan recognition. Measurement of the elastic modulus using Atomic Force Microscopy unveiled that full-length Galectin-8- and C-carbohydrate recognition domain-stimulated macrophages exhibited heightened membrane stiffness compared to untreated cells, providing a plausible mechanism for their involvement in endocytosis. C-carbohydrate recognition domain proved to be as efficient as full-length Galectin-8 in promoting antigen degradation, suggesting its implication in antigen-processing induction. Lastly, C-carbohydrate recognition domain was able to replicate full-length Galectin-8-induced antigen presentation in the major histocompatibility complex class II (MHC-II) context both in vitro and in vivo. Our findings support the notion that Galectin-8 binds through its C-carbohydrate recognition domain to cell surface N-glycans, thereby altering membrane mechanical forces conducive to soluble antigen endocytosis, processing, and presentation to cognate CD4 T cells. These findings contribute to a deeper comprehension of Galectin-8 and its mechanisms of action, paving the way for the development of more efficacious immunotherapies.
publishDate 2024
dc.date.none.fl_str_mv 2024-10
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/11336/264172
Prato, Cecilia Arahi; Borbolla, Laura Victoria; Lizarraga, Leonardo; Campetella, Oscar Eduardo; Tribulatti, María Virginia; The interaction of Galectin-8 C -terminal domain with cell surface glycoconjugates modulates membrane elasticity to stimulate antigen uptake and presentation to CD4 T cells; Oxford University Press; Journal of Leukocyte Biology; 117; 2; 10-2024; 1-13
1938-3673
CONICET Digital
CONICET
url http://hdl.handle.net/11336/264172
identifier_str_mv Prato, Cecilia Arahi; Borbolla, Laura Victoria; Lizarraga, Leonardo; Campetella, Oscar Eduardo; Tribulatti, María Virginia; The interaction of Galectin-8 C -terminal domain with cell surface glycoconjugates modulates membrane elasticity to stimulate antigen uptake and presentation to CD4 T cells; Oxford University Press; Journal of Leukocyte Biology; 117; 2; 10-2024; 1-13
1938-3673
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
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info:eu-repo/semantics/altIdentifier/doi/10.1093/jleuko/qiae214
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
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Oxford University Press
publisher.none.fl_str_mv Oxford University Press
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
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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