Biophysical mechanism of the scavenger site near T cell-presented epitopes
Graduate School of Biomedical Sciences; Department of Pharmacology
Medical Subject Headings
Amino Acid Sequence; Animals; Chemistry, Physical; Epitopes; Humans; Major Histocompatibility Complex; Molecular Sequence Data; Protein Conformation; T-Lymphocytes
Life Sciences | Medicine and Health Sciences
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 alpha-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 possible to engineering of T cell-presented vaccines to affect their potency and MHC restriction.
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Citation: Vaccine. 1992;10(1):3-7.
Lu, Shan; Reyes, Victor E.; Bositis, Christopher M.; Goldschmidt, Thomas G.; Lam, Valery; Torgerson, Rochelle R.; Ciardelli, Thomas; Hardy, Larry W.; Lew, Robert A.; and Humphreys, Robert E., "Biophysical mechanism of the scavenger site near T cell-presented epitopes" (1992). GSBS Student Publications. 786.