THE CLEAVAGE PREFERENCE OF THE PROTEASOME GOVERNS THE YIELD OF ANTIGENIC PEPTIDES

被引:107
作者
EGGERS, M
BOESFABIAN, B
RUPPERT, T
KLOETZEL, PM
KOSZINOWSKI, UH
机构
[1] UNIV HEIDELBERG,VIROL ABT,D-69120 HEIDELBERG,GERMANY
[2] HUMBOLDT UNIV BERLIN,INST BIOCHEM,D-10155 BERLIN,GERMANY
关键词
D O I
10.1084/jem.182.6.1865
中图分类号
R392 [医学免疫学]; Q939.91 [免疫学];
学科分类号
100102 ;
摘要
Proteasomes degrade endogenous proteins in the cytosol. The potential contribution of the proteasome to the effect of flanking sequences on the presentation of an antigenic epitope presented by the major histocompatibility complex class I allele L(d) was studied. Peptides generated in cells from minigenes coding for peptides of 17- and 19-amino acid length were compared with the in vitro 20S proteasome degradation products of the respective synthetic peptides. The quality of generated peptides was independent of ubiquitination. In vivo and in vitro processing products were indistinguishable with respect to peptide size and abundance. Altering the neighboring sequence substantially improved the yield of the final antigenic nonapeptide by 20S proteasome cleavage. These results suggest that, in addition to the presence of major histocompatibility complex class I allelic motifs, the cleavage preference of the proteasome can define the antigenic potential of a protein.
引用
收藏
页码:1865 / 1870
页数:6
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