A basis for alloreactivity: MHC helical residues broaden peptide recognition by the TCR

Claude Daniel, Stephen Horvath, Paul M. Allen

Research output: Contribution to journalArticlepeer-review

86 Scopus citations

Abstract

The high frequency of alloreactive T cells is a major hindrance for transplantation; however, the molecular basis for alloreactivity remains elusive. We examined the I-E(p) alloreactivity of a well-characterized Hb(64- 76)/I-E(k)-specific murine T cell. Using a combinatorial peptide library approach, we identified a highly stimulatory alloepitope mimic and observed that the recognition of the central TCR contact residues (P3 and P5) was much more flexible than that seen with Hb(64-76)/I-E(k), but still specific. Therefore, alloreactive T cells can recognize a self-peptide/MHC surface; however, the allogeneic MHC molecule changes the recognition requirements for the central region of the peptide, allowing a more diverse repertoire of ligands to be recognized.

Original languageEnglish
Pages (from-to)543-552
Number of pages10
JournalImmunity
Volume8
Issue number5
DOIs
StatePublished - May 1998

Fingerprint

Dive into the research topics of 'A basis for alloreactivity: MHC helical residues broaden peptide recognition by the TCR'. Together they form a unique fingerprint.

Cite this