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

来源：

FEBS LETTERS | 2012年 / 586卷 / 09期

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

页码：1336 / 1343

页数：8

共 36 条

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