Neoantigen quality predicts immunoediting in survivors of pancreatic cancer

a, Neoantigen high quality mannequin. b, The mannequin and experimental method to estimate cross-reactivity distance C. c, d, Measured (high) and fitted (backside) p^MT–TCR activation curves (c, amino acid (AA) place 4), and activation warmth maps (d, all amino acid positions) for stronger and weaker p^WT–TCR pairs. e, Composite p^MT–TCR EC₅₀ values of all stronger and weaker p^WT–TCR pairs. f, p^MT–TCR activation warmth map and noticed versus modelled C(p^WT, p^MT) for the HLA-B*27:05-restricted p^WT–TCR pair. n signifies the variety of single-amino-acid-substituted p^WT, p^MT and p^MT, p^MT pairs. g, Cross-reactivity distance mannequin C and dendrogram of agglomerative clustering of substitution matrix M. h, Noticed amino acid substitution frequency versus matrix M-defined substitution distance in major and recurrent STS and LTS PDACs. M distance is the matrix M-defined amino acid distance from g. Circles point out substituted residues. n signifies the variety of substitutions. i, Cumulative likelihood distributions of log(C) and D. n signifies the variety of neoantigens. The crimson rectangles within the warmth maps point out amino acids in p^WT. The inexperienced line is a linear regression match. Warmth maps are ordered in accordance with the amino acid order within the dendogram in g. P values had been decided utilizing two-tailed Pearson correlation (f and h) and two-sided Kolmogorov–Smirnov assessments (i).

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