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The specific binding of peptide ligand to Ld class I major histocompatibility complex molecules determines their antigenic structure

To better understand the biological implications of the association of ligand with major histocompatibility complex class I molecules, we have studied the Ld molecule of the mouse. The culturing of various nonselected cell lines with three different known Ld peptide ligands resulted in a two- to fou...

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Detalles Bibliográficos
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1991
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2118782/
https://www.ncbi.nlm.nih.gov/pubmed/1703208
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description To better understand the biological implications of the association of ligand with major histocompatibility complex class I molecules, we have studied the Ld molecule of the mouse. The culturing of various nonselected cell lines with three different known Ld peptide ligands resulted in a two- to fourfold specific increase in surface Ld expression as detected by 10 of 11 different monoclonal antibodies (mAbs) recognizing Ld epitopes. These findings suggest that Ld molecules are not saturated with endogenous peptide ligands and thus have accessible binding sites. Exploiting this feature of Ld we demonstrate that the physical association of Ld with ligand is exquisitely specific, indicating that they function in determinant selection. In addition, a non-peptide-bound antigenic variant of Ld was specifically detected with an exceptional mAb designated 64-3-7. In comparison with other Ld molecules, 64-3-7+ Ld molecules are not peptide ligand inducible, are more susceptible to proteolysis, lack beta 2 microglobulin association, and display a slower rate of oligosaccharide maturation. In spite of their deficiencies, the non- ligand-associated 64-3-7 Ld molecules were detected on the surface of all cell types tested; however, they appear not to be recognized by alloreactive cytotoxic T lymphocytes.
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spelling pubmed-21187822008-04-17 The specific binding of peptide ligand to Ld class I major histocompatibility complex molecules determines their antigenic structure J Exp Med Articles To better understand the biological implications of the association of ligand with major histocompatibility complex class I molecules, we have studied the Ld molecule of the mouse. The culturing of various nonselected cell lines with three different known Ld peptide ligands resulted in a two- to fourfold specific increase in surface Ld expression as detected by 10 of 11 different monoclonal antibodies (mAbs) recognizing Ld epitopes. These findings suggest that Ld molecules are not saturated with endogenous peptide ligands and thus have accessible binding sites. Exploiting this feature of Ld we demonstrate that the physical association of Ld with ligand is exquisitely specific, indicating that they function in determinant selection. In addition, a non-peptide-bound antigenic variant of Ld was specifically detected with an exceptional mAb designated 64-3-7. In comparison with other Ld molecules, 64-3-7+ Ld molecules are not peptide ligand inducible, are more susceptible to proteolysis, lack beta 2 microglobulin association, and display a slower rate of oligosaccharide maturation. In spite of their deficiencies, the non- ligand-associated 64-3-7 Ld molecules were detected on the surface of all cell types tested; however, they appear not to be recognized by alloreactive cytotoxic T lymphocytes. The Rockefeller University Press 1991-02-01 /pmc/articles/PMC2118782/ /pubmed/1703208 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
The specific binding of peptide ligand to Ld class I major histocompatibility complex molecules determines their antigenic structure
title The specific binding of peptide ligand to Ld class I major histocompatibility complex molecules determines their antigenic structure
title_full The specific binding of peptide ligand to Ld class I major histocompatibility complex molecules determines their antigenic structure
title_fullStr The specific binding of peptide ligand to Ld class I major histocompatibility complex molecules determines their antigenic structure
title_full_unstemmed The specific binding of peptide ligand to Ld class I major histocompatibility complex molecules determines their antigenic structure
title_short The specific binding of peptide ligand to Ld class I major histocompatibility complex molecules determines their antigenic structure
title_sort specific binding of peptide ligand to ld class i major histocompatibility complex molecules determines their antigenic structure
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2118782/
https://www.ncbi.nlm.nih.gov/pubmed/1703208