Comparison of three related methods to select T cell-presented sequences of protein antigens

Victor Reyes, Elisabeth J. Fowlie, Shan Lu, Lisa Phillips, L. Thomas Chin, Robert E. Humphreys, Robert A. Lew

Research output: Contribution to journalArticle

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Abstract

A comparison of three methods to predict T cell-presented sequences within antigenic proteins led to the view that recurrent hydrophobic residues might nucleate excised peptides as α-helices against hydrophobic surfaces. Such helices could be protease-protected structures on their way to desetope binding. The compared methods were: the amphipathicity algorithm of DeLisi and Berzofsky [Proc. natn. Acad. Sci. U.S.A. 82, 7048-7052. (1985)] as modified by Margalit et al. [J. Immun. 138, 2213-2229. (1987)] the strip of-helix hydrophobicity algorithm (SOHHA) of Stille et al. [Molec. Immun. 24, 1021-1027. (1987)] and the motifs algorithm of Rothbard and Taylor [EMBO J. 7, 93-100. (1988)]. Correct prediction was denned at two levels of stringency: (1) the predicted sequence overlapped the experimentally reported sequence when the ratio of the intersection of both to the union of both ≥0.5 or (2) the sequences touched when there was a non-empty intersection of both sequences. We determined the sensitivity (correct predictions/number of reported T cell-presented sequences) and efficiency (correct predictions/number of predictions) at each level of stringency. In terms of overlap, the SOHHA was more sensitive (0.43) than the amphipathicity (0.29) (not significant) and motifs (0.0, 0.0) (p < 0.05) predictions and more efficient (0.35) than the amphipathicity (0.14) and motifs (0.0, 0.0) predictions. At the less stringent criterion touching, the amphipathicity method (0.71) was as sensitive as motif Rothbard-4 (0.79) and more sensitive than SOHHA (0.57) and motif Rothbard-5 (0.43). At that criterion, the SOHHA was more efficient (0.47) than the amphipathicity (0.36) and motifs (0.25, 0.40) methods. We hypothesize that the comparability of these approaches reflected the common, predominant influence of recurrent hydrophobicity in their predictions.

Original languageEnglish (US)
Pages (from-to)1021-1027
Number of pages7
JournalMolecular Immunology
Volume27
Issue number10
DOIs
StatePublished - 1990
Externally publishedYes

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Hydrophobic and Hydrophilic Interactions
T-Lymphocytes
Antigens
Proteins
Peptide Hydrolases
Peptides

ASJC Scopus subject areas

  • Molecular Biology
  • Immunology

Cite this

Reyes, V., Fowlie, E. J., Lu, S., Phillips, L., Chin, L. T., Humphreys, R. E., & Lew, R. A. (1990). Comparison of three related methods to select T cell-presented sequences of protein antigens. Molecular Immunology, 27(10), 1021-1027. https://doi.org/10.1016/0161-5890(90)90125-J

Comparison of three related methods to select T cell-presented sequences of protein antigens. / Reyes, Victor; Fowlie, Elisabeth J.; Lu, Shan; Phillips, Lisa; Chin, L. Thomas; Humphreys, Robert E.; Lew, Robert A.

In: Molecular Immunology, Vol. 27, No. 10, 1990, p. 1021-1027.

Research output: Contribution to journalArticle

Reyes, V, Fowlie, EJ, Lu, S, Phillips, L, Chin, LT, Humphreys, RE & Lew, RA 1990, 'Comparison of three related methods to select T cell-presented sequences of protein antigens', Molecular Immunology, vol. 27, no. 10, pp. 1021-1027. https://doi.org/10.1016/0161-5890(90)90125-J
Reyes, Victor ; Fowlie, Elisabeth J. ; Lu, Shan ; Phillips, Lisa ; Chin, L. Thomas ; Humphreys, Robert E. ; Lew, Robert A. / Comparison of three related methods to select T cell-presented sequences of protein antigens. In: Molecular Immunology. 1990 ; Vol. 27, No. 10. pp. 1021-1027.
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abstract = "A comparison of three methods to predict T cell-presented sequences within antigenic proteins led to the view that recurrent hydrophobic residues might nucleate excised peptides as α-helices against hydrophobic surfaces. Such helices could be protease-protected structures on their way to desetope binding. The compared methods were: the amphipathicity algorithm of DeLisi and Berzofsky [Proc. natn. Acad. Sci. U.S.A. 82, 7048-7052. (1985)] as modified by Margalit et al. [J. Immun. 138, 2213-2229. (1987)] the strip of-helix hydrophobicity algorithm (SOHHA) of Stille et al. [Molec. Immun. 24, 1021-1027. (1987)] and the motifs algorithm of Rothbard and Taylor [EMBO J. 7, 93-100. (1988)]. Correct prediction was denned at two levels of stringency: (1) the predicted sequence overlapped the experimentally reported sequence when the ratio of the intersection of both to the union of both ≥0.5 or (2) the sequences touched when there was a non-empty intersection of both sequences. We determined the sensitivity (correct predictions/number of reported T cell-presented sequences) and efficiency (correct predictions/number of predictions) at each level of stringency. In terms of overlap, the SOHHA was more sensitive (0.43) than the amphipathicity (0.29) (not significant) and motifs (0.0, 0.0) (p < 0.05) predictions and more efficient (0.35) than the amphipathicity (0.14) and motifs (0.0, 0.0) predictions. At the less stringent criterion touching, the amphipathicity method (0.71) was as sensitive as motif Rothbard-4 (0.79) and more sensitive than SOHHA (0.57) and motif Rothbard-5 (0.43). At that criterion, the SOHHA was more efficient (0.47) than the amphipathicity (0.36) and motifs (0.25, 0.40) methods. We hypothesize that the comparability of these approaches reflected the common, predominant influence of recurrent hydrophobicity in their predictions.",
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