Developmentally regulated glycosylation of the CD8alphabeta coreceptor stalk modulates ligand binding.

The functional consequences of glycan structural changes associated with cellular differentiation are ill defined. Herein, we investigate the role of glycan adducts to the O-glycosylated polypeptide stalk tethering the CD8alphabeta coreceptor to the thymocyte surface. We show that immature CD4(+)CD8...

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Detalles Bibliográficos
Autores: Reche Gallardo, Pedro Antonio, Reinherz, Ellis L, Moody, A M, Chui, D, Priatel, J J, Marth, J D
Tipo de recurso: artículo
Fecha de publicación:2001
País:España
Institución:Universidad Complutense de Madrid (UCM)
Repositorio:Docta Complutense
Idioma:inglés
OAI Identifier:oai:docta.ucm.es:20.500.14352/58251
Acceso en línea:https://hdl.handle.net/20.500.14352/58251
Access Level:acceso abierto
Palabra clave:Inmunología
Biología molecular (Biología)
2412 Inmunología
2415 Biología Molecular
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spelling Developmentally regulated glycosylation of the CD8alphabeta coreceptor stalk modulates ligand binding.Reche Gallardo, Pedro AntonioReinherz, Ellis LMoody, A MChui, DPriatel, J JMarth, J DInmunologíaBiología molecular (Biología)2412 Inmunología2415 Biología MolecularThe functional consequences of glycan structural changes associated with cellular differentiation are ill defined. Herein, we investigate the role of glycan adducts to the O-glycosylated polypeptide stalk tethering the CD8alphabeta coreceptor to the thymocyte surface. We show that immature CD4(+)CD8(+) double-positive thymocytes bind MHCI tetramers more avidly than mature CD8 single-positive thymocytes, and that this differential binding is governed by developmentally programmed O-glycan modification controlled by the ST3Gal-I sialyltransferase. ST3Gal-I induction and attendant core 1 sialic acid addition to CD8beta on mature thymocytes decreases CD8alphabeta-MHCI avidity by altering CD8alphabeta domain-domain association and/or orientation. Hence, glycans on the CD8beta stalk appear to modulate the ability of the distal binding surface of the dimeric CD8 globular head domains to clamp MHCI.Universidad Complutense de Madrid20012001-01-0120012001-01-01journal articlehttp://purl.org/coar/resource_type/c_6501info:eu-repo/semantics/articleapplication/pdfhttps://hdl.handle.net/20.500.14352/58251reponame:Docta Complutenseinstname:Universidad Complutense de Madrid (UCM)Inglésengopen accesshttp://purl.org/coar/access_right/c_abf2info:eu-repo/semantics/openAccessoai:docta.ucm.es:20.500.14352/582512026-06-02T12:44:21Z
dc.title.none.fl_str_mv Developmentally regulated glycosylation of the CD8alphabeta coreceptor stalk modulates ligand binding.
title Developmentally regulated glycosylation of the CD8alphabeta coreceptor stalk modulates ligand binding.
spellingShingle Developmentally regulated glycosylation of the CD8alphabeta coreceptor stalk modulates ligand binding.
Reche Gallardo, Pedro Antonio
Inmunología
Biología molecular (Biología)
2412 Inmunología
2415 Biología Molecular
title_short Developmentally regulated glycosylation of the CD8alphabeta coreceptor stalk modulates ligand binding.
title_full Developmentally regulated glycosylation of the CD8alphabeta coreceptor stalk modulates ligand binding.
title_fullStr Developmentally regulated glycosylation of the CD8alphabeta coreceptor stalk modulates ligand binding.
title_full_unstemmed Developmentally regulated glycosylation of the CD8alphabeta coreceptor stalk modulates ligand binding.
title_sort Developmentally regulated glycosylation of the CD8alphabeta coreceptor stalk modulates ligand binding.
dc.creator.none.fl_str_mv Reche Gallardo, Pedro Antonio
Reinherz, Ellis L
Moody, A M
Chui, D
Priatel, J J
Marth, J D
author Reche Gallardo, Pedro Antonio
author_facet Reche Gallardo, Pedro Antonio
Reinherz, Ellis L
Moody, A M
Chui, D
Priatel, J J
Marth, J D
author_role author
author2 Reinherz, Ellis L
Moody, A M
Chui, D
Priatel, J J
Marth, J D
author2_role author
author
author
author
author
dc.contributor.none.fl_str_mv Universidad Complutense de Madrid
dc.subject.none.fl_str_mv Inmunología
Biología molecular (Biología)
2412 Inmunología
2415 Biología Molecular
topic Inmunología
Biología molecular (Biología)
2412 Inmunología
2415 Biología Molecular
description The functional consequences of glycan structural changes associated with cellular differentiation are ill defined. Herein, we investigate the role of glycan adducts to the O-glycosylated polypeptide stalk tethering the CD8alphabeta coreceptor to the thymocyte surface. We show that immature CD4(+)CD8(+) double-positive thymocytes bind MHCI tetramers more avidly than mature CD8 single-positive thymocytes, and that this differential binding is governed by developmentally programmed O-glycan modification controlled by the ST3Gal-I sialyltransferase. ST3Gal-I induction and attendant core 1 sialic acid addition to CD8beta on mature thymocytes decreases CD8alphabeta-MHCI avidity by altering CD8alphabeta domain-domain association and/or orientation. Hence, glycans on the CD8beta stalk appear to modulate the ability of the distal binding surface of the dimeric CD8 globular head domains to clamp MHCI.
publishDate 2001
dc.date.none.fl_str_mv 2001
2001-01-01
2001
2001-01-01
dc.type.none.fl_str_mv journal article
http://purl.org/coar/resource_type/c_6501
dc.type.openaire.fl_str_mv info:eu-repo/semantics/article
format article
dc.identifier.none.fl_str_mv https://hdl.handle.net/20.500.14352/58251
url https://hdl.handle.net/20.500.14352/58251
dc.language.none.fl_str_mv Inglés
eng
language_invalid_str_mv Inglés
language eng
dc.rights.none.fl_str_mv open access
http://purl.org/coar/access_right/c_abf2
dc.rights.openaire.fl_str_mv info:eu-repo/semantics/openAccess
rights_invalid_str_mv open access
http://purl.org/coar/access_right/c_abf2
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.source.none.fl_str_mv reponame:Docta Complutense
instname:Universidad Complutense de Madrid (UCM)
instname_str Universidad Complutense de Madrid (UCM)
reponame_str Docta Complutense
collection Docta Complutense
repository.name.fl_str_mv
repository.mail.fl_str_mv
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score 15.301603