Biophysical mechanism of the scavenger site near T cell-presented epitopes.
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.
Department of Pharmacology, University of Massachusetts Medical Center, Worcester 01655.
S
S
Lu
V E
VE
Reyes
C M
CM
Bositis
T G
TG
Goldschmidt
V
V
Lam
R R
RR
Torgerson
T
T
Ciardelli
L
L
Hardy
R A
RA
Lew
R E
RE
Humphreys
D000595:Amino Acid Sequence; D000818:Animals; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D000939:Epitopes / Q000737:chemistry*; D006801:Humans; D008285:Major Histocompatibility Complex / Q000276:immunology; D008969:Molecular Sequence Data; D011487:Protein Conformation; D013601:T-Lymphocytes / Q000276:immunology*
D000939:Epitopes