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Título:
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Developmentally regulated glycosylation of the CD8alphabeta coreceptor stalk modulates ligand binding.
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Autores:
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Moody, A M ;
Chui, D ;
Reche, Pedro A ;
Priatel, J J ;
Marth, J D ;
Reinherz, Ellis L
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Tipo de documento:
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texto impreso
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Fecha de publicación:
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2001
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Dimensiones:
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application/pdf
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Nota general:
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info:eu-repo/semantics/openAccess
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Idiomas:
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Palabras clave:
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Estado = Publicado
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Materia = Ciencias Biomédicas: Medicina: Inmunología
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Materia = Ciencias Biomédicas: Biología: Biología molecular
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Tipo = Artículo
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Resumen:
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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.
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En línea:
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https://eprints.ucm.es/id/eprint/9344/1/13.Moody_Reche_etal_Cell_2001.pdf
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