Coupling pathogen recognition to innate immunity through glycan-dependent mechanisms

Autores
Davicino, Roberto Carlos; Eliçabe, Ricardo Javier; Di Genaro, Maria Silvia; Rabinovich, Gabriel Adrian
Año de publicación
2011
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Innate immune cells have evolved to sense microbial pathogens through pattern recognition receptors (PRRs), which interact with conserved pathogen-associated molecular patterns (PAMPs) to convey microbial information into immune cell signaling and activation events. PRRs also recognize endogenous damage-associated molecular patterns (DAMPs), including alarmins released during microbial invasion, initiation of autoimmune inflammation or tumor growth. In spite of the well-established role of Toll-like receptors (TLRs) in mediating these recognition events, compelling evidence supports a central function for lectin-glycan interactions in promoting microbial sensing and evoking immune responses. Here we discuss the role of glycans and lectins (particularly galectins) in mediating microbial recognition and initiation of innate immune responses. Both microbes and host cells are sources of glycan-containing information which is, at least in part, decoded by endogenous glycan-binding proteins or lectins, including C-type lectins, siglecs and galectins. Although C-type lectins and siglecs can recognize microbial glycans when expressed on the cell surface of innate immune cells, galectins mainly function as soluble mediators that bridge microbial or host glycans to amplify or attenuate immune responses. Galectins are widely expressed in host cells and play important roles during different steps of infection such as pathogen recognition, invasion and resolution. In addition, recent studies report the presence of conserved 'galectin-like' domains in certain pathogens including helminths and protistan parasites, suggesting that they could also serve as potential virulence factors that influence the outcome and course of infection. Understanding the role of lectin-glycan interactions and the relevance of PRR or PAMP glycosylation in microbial recognition might contribute to the design of novel prophylactic and therapeutic strategies.
Fil: Davicino, Roberto Carlos. Universidad Nacional de San Luis; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico San Luis. Instituto Multidisciplinario de Investigaciones Biológicas de San Luis; Argentina
Fil: Eliçabe, Ricardo Javier. Universidad Nacional de San Luis; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico San Luis. Instituto Multidisciplinario de Investigaciones Biológicas de San Luis; Argentina
Fil: Di Genaro, Maria Silvia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico San Luis. Instituto Multidisciplinario de Investigaciones Biológicas de San Luis; Argentina. Universidad Nacional de San Luis; Argentina
Fil: Rabinovich, Gabriel Adrian. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Biológica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Biología y Medicina Experimental (i); Argentina
Materia
Lectins
Galectins
Toll Like Receptors
Infection
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/11533
Acceder
id CONICETDig_ded10250efae2f30db0174874a310f5d
oai_identifier_str oai:ri.conicet.gov.ar:11336/11533
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Coupling pathogen recognition to innate immunity through glycan-dependent mechanismsDavicino, Roberto CarlosEliçabe, Ricardo JavierDi Genaro, Maria SilviaRabinovich, Gabriel AdrianLectinsGalectinsToll Like ReceptorsInfectionhttps://purl.org/becyt/ford/3.3https://purl.org/becyt/ford/3Innate immune cells have evolved to sense microbial pathogens through pattern recognition receptors (PRRs), which interact with conserved pathogen-associated molecular patterns (PAMPs) to convey microbial information into immune cell signaling and activation events. PRRs also recognize endogenous damage-associated molecular patterns (DAMPs), including alarmins released during microbial invasion, initiation of autoimmune inflammation or tumor growth. In spite of the well-established role of Toll-like receptors (TLRs) in mediating these recognition events, compelling evidence supports a central function for lectin-glycan interactions in promoting microbial sensing and evoking immune responses. Here we discuss the role of glycans and lectins (particularly galectins) in mediating microbial recognition and initiation of innate immune responses. Both microbes and host cells are sources of glycan-containing information which is, at least in part, decoded by endogenous glycan-binding proteins or lectins, including C-type lectins, siglecs and galectins. Although C-type lectins and siglecs can recognize microbial glycans when expressed on the cell surface of innate immune cells, galectins mainly function as soluble mediators that bridge microbial or host glycans to amplify or attenuate immune responses. Galectins are widely expressed in host cells and play important roles during different steps of infection such as pathogen recognition, invasion and resolution. In addition, recent studies report the presence of conserved 'galectin-like' domains in certain pathogens including helminths and protistan parasites, suggesting that they could also serve as potential virulence factors that influence the outcome and course of infection. Understanding the role of lectin-glycan interactions and the relevance of PRR or PAMP glycosylation in microbial recognition might contribute to the design of novel prophylactic and therapeutic strategies.Fil: Davicino, Roberto Carlos. Universidad Nacional de San Luis; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico San Luis. Instituto Multidisciplinario de Investigaciones Biológicas de San Luis; ArgentinaFil: Eliçabe, Ricardo Javier. Universidad Nacional de San Luis; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico San Luis. Instituto Multidisciplinario de Investigaciones Biológicas de San Luis; ArgentinaFil: Di Genaro, Maria Silvia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico San Luis. Instituto Multidisciplinario de Investigaciones Biológicas de San Luis; Argentina. Universidad Nacional de San Luis; ArgentinaFil: Rabinovich, Gabriel Adrian. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Biológica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Biología y Medicina Experimental (i); ArgentinaElsevier Science2011-10info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/11533Davicino, Roberto Carlos; Eliçabe, Ricardo Javier; Di Genaro, Maria Silvia; Rabinovich, Gabriel Adrian; Coupling pathogen recognition to innate immunity through glycan-dependent mechanisms; Elsevier Science; International Immunopharmacology; 11; 10; 10-2011; 1457-14631567-57691878-1705enginfo:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S156757691100213Xinfo:eu-repo/semantics/altIdentifier/url/http://dx.doi.org/10.1016/j.intimp.2011.05.002info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-nd/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T10:09:20Zoai:ri.conicet.gov.ar:11336/11533instacron: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 10:09:20.849CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Coupling pathogen recognition to innate immunity through glycan-dependent mechanisms
title Coupling pathogen recognition to innate immunity through glycan-dependent mechanisms
spellingShingle Coupling pathogen recognition to innate immunity through glycan-dependent mechanisms
Davicino, Roberto Carlos
Lectins
Galectins
Toll Like Receptors
Infection
title_short Coupling pathogen recognition to innate immunity through glycan-dependent mechanisms
title_full Coupling pathogen recognition to innate immunity through glycan-dependent mechanisms
title_fullStr Coupling pathogen recognition to innate immunity through glycan-dependent mechanisms
title_full_unstemmed Coupling pathogen recognition to innate immunity through glycan-dependent mechanisms
title_sort Coupling pathogen recognition to innate immunity through glycan-dependent mechanisms
dc.creator.none.fl_str_mv Davicino, Roberto Carlos
Eliçabe, Ricardo Javier
Di Genaro, Maria Silvia
Rabinovich, Gabriel Adrian
author Davicino, Roberto Carlos
author_facet Davicino, Roberto Carlos
Eliçabe, Ricardo Javier
Di Genaro, Maria Silvia
Rabinovich, Gabriel Adrian
author_role author
author2 Eliçabe, Ricardo Javier
Di Genaro, Maria Silvia
Rabinovich, Gabriel Adrian
author2_role author
author
author
dc.subject.none.fl_str_mv Lectins
Galectins
Toll Like Receptors
Infection
topic Lectins
Galectins
Toll Like Receptors
Infection
purl_subject.fl_str_mv https://purl.org/becyt/ford/3.3
https://purl.org/becyt/ford/3
dc.description.none.fl_txt_mv Innate immune cells have evolved to sense microbial pathogens through pattern recognition receptors (PRRs), which interact with conserved pathogen-associated molecular patterns (PAMPs) to convey microbial information into immune cell signaling and activation events. PRRs also recognize endogenous damage-associated molecular patterns (DAMPs), including alarmins released during microbial invasion, initiation of autoimmune inflammation or tumor growth. In spite of the well-established role of Toll-like receptors (TLRs) in mediating these recognition events, compelling evidence supports a central function for lectin-glycan interactions in promoting microbial sensing and evoking immune responses. Here we discuss the role of glycans and lectins (particularly galectins) in mediating microbial recognition and initiation of innate immune responses. Both microbes and host cells are sources of glycan-containing information which is, at least in part, decoded by endogenous glycan-binding proteins or lectins, including C-type lectins, siglecs and galectins. Although C-type lectins and siglecs can recognize microbial glycans when expressed on the cell surface of innate immune cells, galectins mainly function as soluble mediators that bridge microbial or host glycans to amplify or attenuate immune responses. Galectins are widely expressed in host cells and play important roles during different steps of infection such as pathogen recognition, invasion and resolution. In addition, recent studies report the presence of conserved 'galectin-like' domains in certain pathogens including helminths and protistan parasites, suggesting that they could also serve as potential virulence factors that influence the outcome and course of infection. Understanding the role of lectin-glycan interactions and the relevance of PRR or PAMP glycosylation in microbial recognition might contribute to the design of novel prophylactic and therapeutic strategies.
Fil: Davicino, Roberto Carlos. Universidad Nacional de San Luis; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico San Luis. Instituto Multidisciplinario de Investigaciones Biológicas de San Luis; Argentina
Fil: Eliçabe, Ricardo Javier. Universidad Nacional de San Luis; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico San Luis. Instituto Multidisciplinario de Investigaciones Biológicas de San Luis; Argentina
Fil: Di Genaro, Maria Silvia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico San Luis. Instituto Multidisciplinario de Investigaciones Biológicas de San Luis; Argentina. Universidad Nacional de San Luis; Argentina
Fil: Rabinovich, Gabriel Adrian. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Biológica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Biología y Medicina Experimental (i); Argentina
description Innate immune cells have evolved to sense microbial pathogens through pattern recognition receptors (PRRs), which interact with conserved pathogen-associated molecular patterns (PAMPs) to convey microbial information into immune cell signaling and activation events. PRRs also recognize endogenous damage-associated molecular patterns (DAMPs), including alarmins released during microbial invasion, initiation of autoimmune inflammation or tumor growth. In spite of the well-established role of Toll-like receptors (TLRs) in mediating these recognition events, compelling evidence supports a central function for lectin-glycan interactions in promoting microbial sensing and evoking immune responses. Here we discuss the role of glycans and lectins (particularly galectins) in mediating microbial recognition and initiation of innate immune responses. Both microbes and host cells are sources of glycan-containing information which is, at least in part, decoded by endogenous glycan-binding proteins or lectins, including C-type lectins, siglecs and galectins. Although C-type lectins and siglecs can recognize microbial glycans when expressed on the cell surface of innate immune cells, galectins mainly function as soluble mediators that bridge microbial or host glycans to amplify or attenuate immune responses. Galectins are widely expressed in host cells and play important roles during different steps of infection such as pathogen recognition, invasion and resolution. In addition, recent studies report the presence of conserved 'galectin-like' domains in certain pathogens including helminths and protistan parasites, suggesting that they could also serve as potential virulence factors that influence the outcome and course of infection. Understanding the role of lectin-glycan interactions and the relevance of PRR or PAMP glycosylation in microbial recognition might contribute to the design of novel prophylactic and therapeutic strategies.
publishDate 2011
dc.date.none.fl_str_mv 2011-10
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/11336/11533
Davicino, Roberto Carlos; Eliçabe, Ricardo Javier; Di Genaro, Maria Silvia; Rabinovich, Gabriel Adrian; Coupling pathogen recognition to innate immunity through glycan-dependent mechanisms; Elsevier Science; International Immunopharmacology; 11; 10; 10-2011; 1457-1463
1567-5769
1878-1705
url http://hdl.handle.net/11336/11533
identifier_str_mv Davicino, Roberto Carlos; Eliçabe, Ricardo Javier; Di Genaro, Maria Silvia; Rabinovich, Gabriel Adrian; Coupling pathogen recognition to innate immunity through glycan-dependent mechanisms; Elsevier Science; International Immunopharmacology; 11; 10; 10-2011; 1457-1463
1567-5769
1878-1705
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S156757691100213X
info:eu-repo/semantics/altIdentifier/url/http://dx.doi.org/10.1016/j.intimp.2011.05.002
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Elsevier Science
publisher.none.fl_str_mv Elsevier Science
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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score 13.13397

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