Proteolytic enzymes involved in MHC class I antigen processing: A guerrilla army that partners with the proteasome
- PMID: 26006050
- DOI: 10.1016/j.molimm.2015.04.014
Proteolytic enzymes involved in MHC class I antigen processing: A guerrilla army that partners with the proteasome
Abstract
Major histocompatibility complex class I proteins (MHC-I) load short peptides derived from proteolytic cleavage of endogenous proteins in any cell of the body, in a process termed antigen processing and presentation. When the source proteins are altered self or encoded by a pathogen, recognition of peptide/MHC-I complexes at the plasma membrane leads to CD8(+) T-lymphocyte responses that clear infections and probably underlie tumor immune surveillance. On the other hand, presentation of self peptides may cause some types of autoimmunity. The peptides that are presented determine the specificity and efficiency of pathogen clearance or, conversely, of immunopathology. In this review we highlight the growing number of peptidases which, as a by-product of their regular activity, can generate peptide epitopes for immune surveillance. These ∼20 peptidases collectively behave as a guerrilla army partnering with the regular proteasome army in generating a variety of peptides for presentation by MHC-I and thus optimally signaling infection.
Keywords: Antigen processing; CD8(+) cytotoxic T lymphocyte; Epitope; Major Histocompatibility Complex class I; Peptidase; Protease.
Copyright © 2015 The Authors. Published by Elsevier Ltd.. All rights reserved.
Similar articles
-
Invariant chain as a vehicle to load antigenic peptides on human MHC class I for cytotoxic T-cell activation.Eur J Immunol. 2014 Mar;44(3):774-84. doi: 10.1002/eji.201343671. Epub 2013 Dec 27. Eur J Immunol. 2014. PMID: 24293164
-
An essential role for tripeptidyl peptidase in the generation of an MHC class I epitope.Nat Immunol. 2003 Apr;4(4):375-9. doi: 10.1038/ni905. Epub 2003 Feb 24. Nat Immunol. 2003. PMID: 12598896
-
Proteolysis and class I major histocompatibility complex antigen presentation.Immunol Rev. 1999 Dec;172:49-66. doi: 10.1111/j.1600-065x.1999.tb01355.x. Immunol Rev. 1999. PMID: 10631936 Review.
-
Role of tripeptidyl peptidase II in the processing of Listeria monocytogenes-derived MHC class I-presented antigenic peptides.Microbes Infect. 2009 Jul-Aug;11(8-9):795-802. doi: 10.1016/j.micinf.2009.04.019. Epub 2009 May 6. Microbes Infect. 2009. PMID: 19426827
-
Peptidases trimming MHC class I ligands.Curr Opin Immunol. 2013 Feb;25(1):90-6. doi: 10.1016/j.coi.2012.10.001. Epub 2012 Oct 19. Curr Opin Immunol. 2013. PMID: 23089230 Review.
Cited by
-
Vaccine-Induced CD8+ T Cell Responses in Children: A Review of Age-Specific Molecular Determinants Contributing to Antigen Cross-Presentation.Front Immunol. 2020 Dec 23;11:607977. doi: 10.3389/fimmu.2020.607977. eCollection 2020. Front Immunol. 2020. PMID: 33424857 Free PMC article. Review.
-
In silico and in vitro arboviral MHC class I-restricted-epitope signatures reveal immunodominance and poor overlapping patterns.Front Immunol. 2022 Nov 17;13:1035515. doi: 10.3389/fimmu.2022.1035515. eCollection 2022. Front Immunol. 2022. PMID: 36466864 Free PMC article.
-
Research and prospect of peptides for use in obesity treatment (Review).Exp Ther Med. 2020 Dec;20(6):234. doi: 10.3892/etm.2020.9364. Epub 2020 Oct 16. Exp Ther Med. 2020. PMID: 33149788 Free PMC article. Review.
-
The role of cellular proteostasis in antitumor immunity.J Biol Chem. 2022 May;298(5):101930. doi: 10.1016/j.jbc.2022.101930. Epub 2022 Apr 11. J Biol Chem. 2022. PMID: 35421375 Free PMC article. Review.
-
Transcriptome of Sphaerospora molnari (Cnidaria, Myxosporea) blood stages provides proteolytic arsenal as potential therapeutic targets against sphaerosporosis in common carp.BMC Genomics. 2020 Jun 16;21(1):404. doi: 10.1186/s12864-020-6705-y. BMC Genomics. 2020. PMID: 32546190 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Research Materials