Two new proteases in the MHC class I processing pathway

Citation
L. Stoltze et al., Two new proteases in the MHC class I processing pathway, NAT IMMUNOL, 1(5), 2000, pp. 413-418
Citations number
32
Categorie Soggetti
Immunology
Journal title
NATURE IMMUNOLOGY
ISSN journal
15292908 → ACNP
Volume
1
Issue
5
Year of publication
2000
Pages
413 - 418
Database
ISI
SICI code
1529-2908(200011)1:5<413:TNPITM>2.0.ZU;2-Q
Abstract
The proteasome generates exact major histocompatibility complex (MHC) class I ligands as well as NH2-terminal-extended precursor peptides, The proteas es responsible for the final NH2-terminal trimming of the precursor peptide s had, until now, not been determined, By using specific selective criteria we purified two cytosolic proteolytic activities, puromycin-sensitive amin opeptidase and bleomycin hydrolase,These proteases could remove NH2-termina l amino acids from the vesicular stomatitis virus nucleoprotein cytotoxic T cell epitope 52-59 (RGYVYQGL) resulting, in combination with proteasomes, in the generation of the correct epitope, Our data provide evidence for the existence of redundant systems acting downstream of the proteasome in the antigen-processing pathway for MHC class I molecules.