TY - JOUR
T1 - Selection of class I MHC-restricted peptides with the strip-of-helix hydrophobicity algorithm
AU - Reyes, Victor E.
AU - Chin, L. Thomas
AU - Humphreys, Robert E.
N1 - Funding Information:
*This work was supported by grant CA37645 from the National Institutes of Health. L. T. Chin was a Betty Lee Stone Fellow of the American Cancer Society, Massachusetts Division, Inc. and was supported by training grant R25 CA36762 from the National Cancer Institute. tAuthor to whom correspondence should be addressed at: Department of Pharmacology, University of Massachusetts Medical School, 55 Lake Avenue North, Worcester, MA 01655, U.S.A.
PY - 1988/9
Y1 - 1988/9
N2 - A strip-of-helix hydrophobicity algorithm to predict class II MHC-restricted peptides, on the basis of their structural similarity to an amphipathic, α -helix in Ii, also predicted peptides which were presented to cytotoxic T-cells by class I MHC molecules. This algorithm ranked peptides according to mean Kyte-Doolittle hydrophobicity values of amino acids at positions n, n + 4, n + 7, n + 11, n + 14 and n + 18 in a sequence which when coiled as a putative α-helix, had the indicated residues in an axial strip along one side of the helix. Sequences selected for highly scoring, hydrophobic strips were required to have at least 1 of the 4 adjacent strips scoring more negatively than -1 in the strip-of-helix hydrophobicity index and the entire sequence could contain no prolines. This algorithm predicted the class I MHC-restricted, T-cell-presented peptides in sequences of 4 proteins from which some class I MHC-restricted, T-cell-presented sequences had been experimentally determined. Since both class I and class II MHC-restricted peptides could be identified with this algorithm, one can propose that: (I) foreign peptide-binding sites (desetopes) of the class I and class II MHC molecules are structurally similar; and (2) any one T-cell-presented peptide can be presented by some specific allele of both a class I and a class II MHC antigen.
AB - A strip-of-helix hydrophobicity algorithm to predict class II MHC-restricted peptides, on the basis of their structural similarity to an amphipathic, α -helix in Ii, also predicted peptides which were presented to cytotoxic T-cells by class I MHC molecules. This algorithm ranked peptides according to mean Kyte-Doolittle hydrophobicity values of amino acids at positions n, n + 4, n + 7, n + 11, n + 14 and n + 18 in a sequence which when coiled as a putative α-helix, had the indicated residues in an axial strip along one side of the helix. Sequences selected for highly scoring, hydrophobic strips were required to have at least 1 of the 4 adjacent strips scoring more negatively than -1 in the strip-of-helix hydrophobicity index and the entire sequence could contain no prolines. This algorithm predicted the class I MHC-restricted, T-cell-presented peptides in sequences of 4 proteins from which some class I MHC-restricted, T-cell-presented sequences had been experimentally determined. Since both class I and class II MHC-restricted peptides could be identified with this algorithm, one can propose that: (I) foreign peptide-binding sites (desetopes) of the class I and class II MHC molecules are structurally similar; and (2) any one T-cell-presented peptide can be presented by some specific allele of both a class I and a class II MHC antigen.
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U2 - 10.1016/0161-5890(88)90123-X
DO - 10.1016/0161-5890(88)90123-X
M3 - Article
C2 - 3264884
AN - SCOPUS:0023712880
SN - 0161-5890
VL - 25
SP - 867
EP - 871
JO - Molecular Immunology
JF - Molecular Immunology
IS - 9
ER -