Immunodominance of H60 is caused by an abnormally high precursor T cell pool directed against its unique minor histocompatibility antigen peptide.

Document Type

Article

Publication Date

2002

Keywords

Antigen-Presentation, Flow-Cytometry, Human, Immunodominant-Epitopes, Ligands, Mice, Minor-Histocompatibility-Antigens, Minor-Histocompatibility-Loci, Organ-Transplantation, Receptors-Immunologic, SUPPORT-U-S-GOVT-P-H-S, Transplantation-Immunology

First Page

593

Last Page

603

JAX Source

Immunity 2002 Nov; 17(5):593-603.

Grant

AI28802/AI/NIAID, HL54977/HL/NHLBI, HL65479/HL/NHLBI

Abstract

The H60 minor histocompatibility (H) antigen peptide is derived from a glycoprotein that serves as a ligand for the stimulatory NKG2D receptor. We show that this peptide is remarkably immunodominant in that it competes effectively with MHC alloantigens, is efficiently crosspresented by host antigen-presenting cells (APCs), and readily elicits naive CD8 T cell responses in vitro. H60 immunodominance is neither a consequence of NKG2D engagement nor competition among minor H antigens on APCs. Instead, H60 immunodominance is a consequence of an abnormally high naive precursor frequency of H60 peptide reactive CD8 T cells. Understanding why the H60 peptide is so immunogenic has important implications in tissue transplantation and vaccine design.

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