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Analysis of MHC-specific peptide motifs: Applications in immunotherapy

  • D. J. Loftus
    ,
  • R. T. Kubo
    ,
  • K. Sakaguchi
    ,
  • E. Celis
    ,
  • A. Sette
    ,
  • E. Appella(corresponding author)
*Corresponding author for this work
  • National Institutes of Health
Scholary Output:
Contribution to journal
Article
Peer-review

Abstract

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.

Publication Information

Output type

Scholary Output:
Contribution to journal
Article
Peer-review

Original language

English (US)

Pages from-to (Number of pages)

Pages 201-210 (10 pages)

Journal (Volume, Issue Number)

Advances in experimental medicine and biology (Volume 383)

Publication milestones

  • Published - 1995

Publication status

Published - 1995

ISSN

0065-2598

Publication IDs

  • Scopus: 0028826161
  • PubMed: 8644503

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