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Differential ability of isolated H-2 Kb subsets to serve as TCR ligands for allo-specific CTL clones: potential role for N-linked glycosylation

It is not known whether all forms of cell surface peptide-class I complexes, when bound with relevant peptide antigen, are recognized by T cells. We demonstrate herein that two distinct subsets of the murine H-2 Kb molecule can be separately isolated from H-2b-expressing cell lines using Y3 mAb immu...

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Detalles Bibliográficos
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1995
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2192001/
https://www.ncbi.nlm.nih.gov/pubmed/7722454
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description It is not known whether all forms of cell surface peptide-class I complexes, when bound with relevant peptide antigen, are recognized by T cells. We demonstrate herein that two distinct subsets of the murine H-2 Kb molecule can be separately isolated from H-2b-expressing cell lines using Y3 mAb immunoaffinity chromatography. Although both isolated Kb subsets were found to be strongly reactive with Y3 mAb by ELISA, one Kb subset is S19.8 mAb reactive (Ly-m11+Kb subset) and exhibits low reactivity with the M1/42 antibody, while the other subset is negative for the Ly-m11 epitope and highly reactive with the M1/42 antibody (M1/42high Kb subset). More importantly, whereas the M1/42high Kb subset is a very effective ligand for both TCR and CD8, the Ly-m11+ Kb subset could only function as a CD8 ligand, as determined in allo- specific CD8+ CTL clone adhesion and degranulation assays. Peptides acid-eluted from both Kb subsets sensitized Kb-transfected T2 cells expressing "peptide empty" Kb for lysis to a similar extent by allo-CTL clones, indicating that relevant endogenous peptide antigens are not limiting in the Ly-m11+ Kb subset. The major distinction identified between the two Kb subsets is that they differ substantially in their degree of N-linked glycosylation, with the Ly-m11+ subset containing Kb molecules with larger and more complex carbohydrate modifications than the M1/42high subset. The differences in glycosylation may explain the functional differences observed between the two Kb subsets. It is therefore possible that some forms of glycosylation on class I molecules interfere with TCR recognition and may limit CD8+ T cell responses, perhaps under circumstances where peptide antigen is limiting.
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spelling pubmed-21920012008-04-16 Differential ability of isolated H-2 Kb subsets to serve as TCR ligands for allo-specific CTL clones: potential role for N-linked glycosylation J Exp Med Articles It is not known whether all forms of cell surface peptide-class I complexes, when bound with relevant peptide antigen, are recognized by T cells. We demonstrate herein that two distinct subsets of the murine H-2 Kb molecule can be separately isolated from H-2b-expressing cell lines using Y3 mAb immunoaffinity chromatography. Although both isolated Kb subsets were found to be strongly reactive with Y3 mAb by ELISA, one Kb subset is S19.8 mAb reactive (Ly-m11+Kb subset) and exhibits low reactivity with the M1/42 antibody, while the other subset is negative for the Ly-m11 epitope and highly reactive with the M1/42 antibody (M1/42high Kb subset). More importantly, whereas the M1/42high Kb subset is a very effective ligand for both TCR and CD8, the Ly-m11+ Kb subset could only function as a CD8 ligand, as determined in allo- specific CD8+ CTL clone adhesion and degranulation assays. Peptides acid-eluted from both Kb subsets sensitized Kb-transfected T2 cells expressing "peptide empty" Kb for lysis to a similar extent by allo-CTL clones, indicating that relevant endogenous peptide antigens are not limiting in the Ly-m11+ Kb subset. The major distinction identified between the two Kb subsets is that they differ substantially in their degree of N-linked glycosylation, with the Ly-m11+ subset containing Kb molecules with larger and more complex carbohydrate modifications than the M1/42high subset. The differences in glycosylation may explain the functional differences observed between the two Kb subsets. It is therefore possible that some forms of glycosylation on class I molecules interfere with TCR recognition and may limit CD8+ T cell responses, perhaps under circumstances where peptide antigen is limiting. The Rockefeller University Press 1995-05-01 /pmc/articles/PMC2192001/ /pubmed/7722454 Text en This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).
spellingShingle Articles
Differential ability of isolated H-2 Kb subsets to serve as TCR ligands for allo-specific CTL clones: potential role for N-linked glycosylation
title Differential ability of isolated H-2 Kb subsets to serve as TCR ligands for allo-specific CTL clones: potential role for N-linked glycosylation
title_full Differential ability of isolated H-2 Kb subsets to serve as TCR ligands for allo-specific CTL clones: potential role for N-linked glycosylation
title_fullStr Differential ability of isolated H-2 Kb subsets to serve as TCR ligands for allo-specific CTL clones: potential role for N-linked glycosylation
title_full_unstemmed Differential ability of isolated H-2 Kb subsets to serve as TCR ligands for allo-specific CTL clones: potential role for N-linked glycosylation
title_short Differential ability of isolated H-2 Kb subsets to serve as TCR ligands for allo-specific CTL clones: potential role for N-linked glycosylation
title_sort differential ability of isolated h-2 kb subsets to serve as tcr ligands for allo-specific ctl clones: potential role for n-linked glycosylation
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2192001/
https://www.ncbi.nlm.nih.gov/pubmed/7722454