Biophysical mechanism of the scavenger site near T cell-presented epitopes

S. Lu, V. E. Reyes, C. M. Bositis, T. G. Goldschmidt, V. Lam, R. R. Torgerson, T. Ciardelli, L. Hardy, R. A. Lew, R. E. Humphreys

Research output: Contribution to journalShort surveypeer-review

8 Scopus citations


We seek to identify consensus sequences in digested fragments of antigenic proteins regulating selection and major histocompatibility complex (MHC)-restricted presentation to T cells of epitopes within those fragments. One such pattern, of recurrent, hydrophobic sidechains forming a longitudinal hydrophobic strip when a sequence is coiled as an α-helix, is found in or near most T cell-presented epitopes. Such recurrent hydrophobicity may lead to protease-protected coiling of the fragment against endosomal membranes and transfer to MHC molecules. This concept leads to better identification of T cell-presented sequences and possibly to engineering of T cell-presented vaccines to affect their potency and MHC restriction.

Original languageEnglish (US)
Pages (from-to)3-7
Number of pages5
Issue number1
StatePublished - 1992
Externally publishedYes


  • Antigen processing
  • MHC molecules
  • T cell-presented epitope
  • peptide vaccines
  • α-helix

ASJC Scopus subject areas

  • Molecular Medicine
  • General Immunology and Microbiology
  • General Veterinary
  • Public Health, Environmental and Occupational Health
  • Infectious Diseases


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