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. 1993 Aug 1;90(15):6949–6951. doi: 10.1073/pnas.90.15.6949

Alloantibodies can discriminate class I major histocompatibility complex molecules associated with various endogenous peptides.

L A Sherman 1, S Chattopadhyay 1, J A Biggs 1, R F Dick 2nd 1, J A Bluestone 1
PMCID: PMC47052  PMID: 8346201

Abstract

Molecules encoded by a single major histocompatibility complex class I gene can associate with any one of a large number of peptide ligands. T-cell receptors have the capacity to discriminate among these peptide-class I complexes and in many cases bind only a single peptide-class I complex with sufficient affinity to trigger effector function. In contrast, it is generally assumed that class I-specific alloantibodies are indifferent to peptide heterogeneity, being directed toward allele-specific determinants on the molecule. In this report, three monoclonal antibodies were used to precipitate Kb molecules from cell lysates. Surprisingly, in each case a different set of peptides was found to be associated with Kb as detected by peptide-dependent Kb-specific alloreactive cytolytic T lymphocytes or by biochemical resolution. These results demonstrate that the affinity of binding by alloantibodies can be affected by the endogenous peptide ligand.

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Selected References

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