Multiple class I motifs revealed by sequencing naturally processed peptides eluted from rat T cell MHC molecules

Gregory Burrows, K. Ariail, B. Celnik, J. E. Gambee, H. Offner, A. A. Vandenbark

Research output: Contribution to journalArticlepeer-review

5 Scopus citations


Class I major histocompatibility complex (MHC) molecules interact with a diverse array of self and foreign peptides. Displayed on the cell surface, the class I/peptide complex provides an extracellular indication of the intracellular milieu. We have characterized the Lewis rat Vβ8.2+ T cell hybridoma C14/BW12-12A1 by FACS analysis and have used immunoaffinity chromatography to purify class I molecules from these cells. Peptides eluted from the class I molecules have been fractinnated by HPLC and sequenced. Self-peptide mixtures indicate two distinct peptide motifs, suggesting the possibility of multiple class I loci. The majority of the naturally processed peptide ligands were nonamers. Naturally processed peptide ligands fitting the first motif contained a hydrophobic leucine anchor residue at position three and a carboxyl-terminal serine anchor residue. A second motif was characterized by a tyrosine or phenylalanine residue at position three and a phenylalanine or isoleucine carboxyl-terminal residue. Four peptides derived from the Vβ8.2 T cell receptor have sequences that fit these motifs, providing a mechanistic explanation for their immunoregulatory role. Identification of these class I peptide binding motifs will be useful for predicting potential CTL epitopes in studies on autoimmunity, immunoregulation and transplantation in the Lewis rat.

Original languageEnglish (US)
Pages (from-to)107-116
Number of pages10
JournalJournal of Neuroscience Research
Issue number1
StatePublished - Jul 1 1997


  • EAE
  • Immunoregulation
  • Lewis rat
  • Peptide-binding motif

ASJC Scopus subject areas

  • Cellular and Molecular Neuroscience


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