Analysis of MHC-specific peptide motifs: Applications in immunotherapy

D. J. Loftus, R. T. Kubo, K. Sakaguchi, E. Celis, A. Sette, E. Appella

Research output: Contribution to journalArticlepeer-review

6 Scopus citations


The structural features which underlie peptide binding to MHC molecules permit the binding of a diverse array of peptides. Polymorphic residues of class I, and to a lesser extent, class II molecules, determine the peptide selectivities associated with various allomorphs. The motifs which are described here and elsewhere in the literature mainly reflect peptide features which contribute to high affinity binding. While high affinity MHC binding is not an absolute prerequisite for the immunologic relevance of a peptide, motifs provide general guidelines for eliciting and characterizing cellular responses to epitopes presented by a given MHC allomorph or group of related allomorphs. The utility of motifs is underscored by emerging developments in the clinical application of peptides to elicit specific and effective cellular responses.

Original languageEnglish (US)
Pages (from-to)201-210
Number of pages10
JournalAdvances in experimental medicine and biology
StatePublished - 1995
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)


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