Immune regulatory networks coordinated by glycans and glycan-binding proteins in autoimmunity and infection
- Autores
- Pinho, Salomé S.; Alves, Inês; Gaifem, Joana; Rabinovich, Gabriel Adrián
- Año de publicación
- 2023
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- The immune system is coordinated by an intricate network of stimulatory and inhibitory circuits that regulate host responses against endogenous and exogenous insults. Disruption of these safeguard and homeostatic mechanisms can lead to unpredictable inflammatory and autoimmune responses, whereas deficiency of immune stimulatory pathways may orchestrate immunosuppressive programs that contribute to perpetuate chronic infections, but also influence cancer development and progression. Glycans have emerged as essential components of homeostatic circuits, acting as fine-tuners of immunological responses and potential molecular targets for manipulation of immune tolerance and activation in a wide range of pathologic settings. Cell surface glycans, present in cells, tissues and the extracellular matrix, have been proposed to serve as “self-associated molecular patterns” that store structurally relevant biological data. The responsibility of deciphering this information relies on different families of glycan-binding proteins (including galectins, siglecs and C-type lectins) which, upon recognition of specific carbohydrate structures, can recalibrate the magnitude, nature and fate of immune responses. This process is tightly regulated by the diversity of glycan structures and the establishment of multivalent interactions on cell surface receptors and the extracellular matrix. Here we review the spatiotemporal regulation of selected glycan-modifying processes including mannosylation, complex N-glycan branching, core 2 O-glycan elongation, LacNAc extension, as well as terminal sialylation and fucosylation. Moreover, we illustrate examples that highlight the contribution of these processes to the control of immune responses and their integration with canonical tolerogenic pathways. Finally, we discuss the power of glycans and glycan-binding proteins as a source of immunomodulatory signals that could be leveraged for the treatment of autoimmune inflammation and chronic infection.
Fil: Pinho, Salomé S.. Universidad de Porto; Portugal
Fil: Alves, Inês. Universidad de Porto; Portugal
Fil: Gaifem, Joana. Universidad de Porto; Portugal
Fil: Rabinovich, Gabriel Adrián. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Biología y Medicina Experimental. Fundación de Instituto de Biología y Medicina Experimental. Instituto de Biología y Medicina Experimental; Argentina - Materia
-
GLYCOSYLATION
INFECTION
AUTOIMMUNITY
GLYCAN-BINDING PROTEINS - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- https://creativecommons.org/licenses/by/2.5/ar/
- Repositorio
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/249634
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Immune regulatory networks coordinated by glycans and glycan-binding proteins in autoimmunity and infectionPinho, Salomé S.Alves, InêsGaifem, JoanaRabinovich, Gabriel AdriánGLYCOSYLATIONINFECTIONAUTOIMMUNITYGLYCAN-BINDING PROTEINShttps://purl.org/becyt/ford/3.1https://purl.org/becyt/ford/3The immune system is coordinated by an intricate network of stimulatory and inhibitory circuits that regulate host responses against endogenous and exogenous insults. Disruption of these safeguard and homeostatic mechanisms can lead to unpredictable inflammatory and autoimmune responses, whereas deficiency of immune stimulatory pathways may orchestrate immunosuppressive programs that contribute to perpetuate chronic infections, but also influence cancer development and progression. Glycans have emerged as essential components of homeostatic circuits, acting as fine-tuners of immunological responses and potential molecular targets for manipulation of immune tolerance and activation in a wide range of pathologic settings. Cell surface glycans, present in cells, tissues and the extracellular matrix, have been proposed to serve as “self-associated molecular patterns” that store structurally relevant biological data. The responsibility of deciphering this information relies on different families of glycan-binding proteins (including galectins, siglecs and C-type lectins) which, upon recognition of specific carbohydrate structures, can recalibrate the magnitude, nature and fate of immune responses. This process is tightly regulated by the diversity of glycan structures and the establishment of multivalent interactions on cell surface receptors and the extracellular matrix. Here we review the spatiotemporal regulation of selected glycan-modifying processes including mannosylation, complex N-glycan branching, core 2 O-glycan elongation, LacNAc extension, as well as terminal sialylation and fucosylation. Moreover, we illustrate examples that highlight the contribution of these processes to the control of immune responses and their integration with canonical tolerogenic pathways. Finally, we discuss the power of glycans and glycan-binding proteins as a source of immunomodulatory signals that could be leveraged for the treatment of autoimmune inflammation and chronic infection.Fil: Pinho, Salomé S.. Universidad de Porto; PortugalFil: Alves, Inês. Universidad de Porto; PortugalFil: Gaifem, Joana. Universidad de Porto; PortugalFil: Rabinovich, Gabriel Adrián. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Biología y Medicina Experimental. Fundación de Instituto de Biología y Medicina Experimental. Instituto de Biología y Medicina Experimental; ArgentinaNature2023-08info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/249634Pinho, Salomé S.; Alves, Inês; Gaifem, Joana; Rabinovich, Gabriel Adrián; Immune regulatory networks coordinated by glycans and glycan-binding proteins in autoimmunity and infection; Nature; Cellular & Molecular Immunology; 20; 10; 8-2023; 1101-11132042-0226CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.nature.com/articles/s41423-023-01074-1info:eu-repo/semantics/altIdentifier/doi/10.1038/s41423-023-01074-1info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T09:47:05Zoai:ri.conicet.gov.ar:11336/249634instacron: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:34982025-09-03 09:47:05.493CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
dc.title.none.fl_str_mv |
Immune regulatory networks coordinated by glycans and glycan-binding proteins in autoimmunity and infection |
title |
Immune regulatory networks coordinated by glycans and glycan-binding proteins in autoimmunity and infection |
spellingShingle |
Immune regulatory networks coordinated by glycans and glycan-binding proteins in autoimmunity and infection Pinho, Salomé S. GLYCOSYLATION INFECTION AUTOIMMUNITY GLYCAN-BINDING PROTEINS |
title_short |
Immune regulatory networks coordinated by glycans and glycan-binding proteins in autoimmunity and infection |
title_full |
Immune regulatory networks coordinated by glycans and glycan-binding proteins in autoimmunity and infection |
title_fullStr |
Immune regulatory networks coordinated by glycans and glycan-binding proteins in autoimmunity and infection |
title_full_unstemmed |
Immune regulatory networks coordinated by glycans and glycan-binding proteins in autoimmunity and infection |
title_sort |
Immune regulatory networks coordinated by glycans and glycan-binding proteins in autoimmunity and infection |
dc.creator.none.fl_str_mv |
Pinho, Salomé S. Alves, Inês Gaifem, Joana Rabinovich, Gabriel Adrián |
author |
Pinho, Salomé S. |
author_facet |
Pinho, Salomé S. Alves, Inês Gaifem, Joana Rabinovich, Gabriel Adrián |
author_role |
author |
author2 |
Alves, Inês Gaifem, Joana Rabinovich, Gabriel Adrián |
author2_role |
author author author |
dc.subject.none.fl_str_mv |
GLYCOSYLATION INFECTION AUTOIMMUNITY GLYCAN-BINDING PROTEINS |
topic |
GLYCOSYLATION INFECTION AUTOIMMUNITY GLYCAN-BINDING PROTEINS |
purl_subject.fl_str_mv |
https://purl.org/becyt/ford/3.1 https://purl.org/becyt/ford/3 |
dc.description.none.fl_txt_mv |
The immune system is coordinated by an intricate network of stimulatory and inhibitory circuits that regulate host responses against endogenous and exogenous insults. Disruption of these safeguard and homeostatic mechanisms can lead to unpredictable inflammatory and autoimmune responses, whereas deficiency of immune stimulatory pathways may orchestrate immunosuppressive programs that contribute to perpetuate chronic infections, but also influence cancer development and progression. Glycans have emerged as essential components of homeostatic circuits, acting as fine-tuners of immunological responses and potential molecular targets for manipulation of immune tolerance and activation in a wide range of pathologic settings. Cell surface glycans, present in cells, tissues and the extracellular matrix, have been proposed to serve as “self-associated molecular patterns” that store structurally relevant biological data. The responsibility of deciphering this information relies on different families of glycan-binding proteins (including galectins, siglecs and C-type lectins) which, upon recognition of specific carbohydrate structures, can recalibrate the magnitude, nature and fate of immune responses. This process is tightly regulated by the diversity of glycan structures and the establishment of multivalent interactions on cell surface receptors and the extracellular matrix. Here we review the spatiotemporal regulation of selected glycan-modifying processes including mannosylation, complex N-glycan branching, core 2 O-glycan elongation, LacNAc extension, as well as terminal sialylation and fucosylation. Moreover, we illustrate examples that highlight the contribution of these processes to the control of immune responses and their integration with canonical tolerogenic pathways. Finally, we discuss the power of glycans and glycan-binding proteins as a source of immunomodulatory signals that could be leveraged for the treatment of autoimmune inflammation and chronic infection. Fil: Pinho, Salomé S.. Universidad de Porto; Portugal Fil: Alves, Inês. Universidad de Porto; Portugal Fil: Gaifem, Joana. Universidad de Porto; Portugal Fil: Rabinovich, Gabriel Adrián. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Biología y Medicina Experimental. Fundación de Instituto de Biología y Medicina Experimental. Instituto de Biología y Medicina Experimental; Argentina |
description |
The immune system is coordinated by an intricate network of stimulatory and inhibitory circuits that regulate host responses against endogenous and exogenous insults. Disruption of these safeguard and homeostatic mechanisms can lead to unpredictable inflammatory and autoimmune responses, whereas deficiency of immune stimulatory pathways may orchestrate immunosuppressive programs that contribute to perpetuate chronic infections, but also influence cancer development and progression. Glycans have emerged as essential components of homeostatic circuits, acting as fine-tuners of immunological responses and potential molecular targets for manipulation of immune tolerance and activation in a wide range of pathologic settings. Cell surface glycans, present in cells, tissues and the extracellular matrix, have been proposed to serve as “self-associated molecular patterns” that store structurally relevant biological data. The responsibility of deciphering this information relies on different families of glycan-binding proteins (including galectins, siglecs and C-type lectins) which, upon recognition of specific carbohydrate structures, can recalibrate the magnitude, nature and fate of immune responses. This process is tightly regulated by the diversity of glycan structures and the establishment of multivalent interactions on cell surface receptors and the extracellular matrix. Here we review the spatiotemporal regulation of selected glycan-modifying processes including mannosylation, complex N-glycan branching, core 2 O-glycan elongation, LacNAc extension, as well as terminal sialylation and fucosylation. Moreover, we illustrate examples that highlight the contribution of these processes to the control of immune responses and their integration with canonical tolerogenic pathways. Finally, we discuss the power of glycans and glycan-binding proteins as a source of immunomodulatory signals that could be leveraged for the treatment of autoimmune inflammation and chronic infection. |
publishDate |
2023 |
dc.date.none.fl_str_mv |
2023-08 |
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/11336/249634 Pinho, Salomé S.; Alves, Inês; Gaifem, Joana; Rabinovich, Gabriel Adrián; Immune regulatory networks coordinated by glycans and glycan-binding proteins in autoimmunity and infection; Nature; Cellular & Molecular Immunology; 20; 10; 8-2023; 1101-1113 2042-0226 CONICET Digital CONICET |
url |
http://hdl.handle.net/11336/249634 |
identifier_str_mv |
Pinho, Salomé S.; Alves, Inês; Gaifem, Joana; Rabinovich, Gabriel Adrián; Immune regulatory networks coordinated by glycans and glycan-binding proteins in autoimmunity and infection; Nature; Cellular & Molecular Immunology; 20; 10; 8-2023; 1101-1113 2042-0226 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.nature.com/articles/s41423-023-01074-1 info:eu-repo/semantics/altIdentifier/doi/10.1038/s41423-023-01074-1 |
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 application/pdf |
dc.publisher.none.fl_str_mv |
Nature |
publisher.none.fl_str_mv |
Nature |
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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13.13397 |