Stability of peptide-HLA-I complexes and tapasin folding facilitation - tools to define immunogenic peptides

被引:6
作者
Geironson, Linda [1 ]
Roder, Gustav [2 ]
Paulsson, Kajsa [1 ,2 ]
机构
[1] Lund Univ, Immunol Sect, SE-22184 Lund, Sweden
[2] Univ Copenhagen, Panum Inst 18 3, Dept Expt Immunol, Inst Int Hlth Immunol & Microbiol, DK-2200 Copenhagen, Denmark
基金
英国医学研究理事会;
关键词
Tapasin; MHC-I; Peptide; Stability; Vaccine; ANTIGEN PRESENTATION; MOLECULES; BINDING; TAP; DISSOCIATION; MECHANISM; PREDICTIONS; REPERTOIRE; DEPENDENCE; RETENTION;
D O I
10.1016/j.febslet.2012.03.045
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Only a small fraction of the peptides generated inside the cell end up being presented by HLA-I on the cell surface. High stability of peptide-HLA-I complexes and a low HLA-I tapasin-facilitation have been proposed to predict immunogenicity. We here set out to investigate if these parameters correlated and defined immunogenic peptides. Both peptide-HLA-B*08:01 and peptide-HLA-A*02:01 complexes showed small differences in tapasin-facilitation and larger differences in stability. This suggests that the stability of immunogenic peptide-HLA-I complexes vary above an HLA-I allomorph dependent lower limit (e. g. > 2 h for HLA-A*02:01), immunogenicity predicted by tapasin-facilitation may be defined by an equally allomorph unique upper value (e. g. tapasin-facilitation <1.5 for HLA-A*02:01), and variation above the stability-threshold does not directly reflect a variation in tapasin-facilitation. (C) 2012 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.
引用
收藏
页码:1336 / 1343
页数:8
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