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

G. G. Burrows, K. Ariail, B. Celnik, J. E. Gambee, Halina Offner, Arthur Vandenbark

Research output: Contribution to journalArticle

5 Citations (Scopus)

Abstract

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
Volume49
Issue number1
DOIs
StatePublished - Jul 1 1997

Fingerprint

Major Histocompatibility Complex
T-Lymphocytes
Peptides
Phenylalanine
Ligands
Isoleucine
Hybridomas
T-Cell Antigen Receptor
Autoimmunity
Leucine
Serine
Tyrosine
Chromatography
Epitopes
Transplantation
High Pressure Liquid Chromatography

Keywords

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

ASJC Scopus subject areas

  • Neuroscience(all)

Cite this

Multiple class I motifs revealed by sequencing naturally processed peptides eluted from rat T cell MHC molecules. / Burrows, G. G.; Ariail, K.; Celnik, B.; Gambee, J. E.; Offner, Halina; Vandenbark, Arthur.

In: Journal of Neuroscience Research, Vol. 49, No. 1, 01.07.1997, p. 107-116.

Research output: Contribution to journalArticle

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