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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.

journal_name

Mol Immunol

journal_title

Molecular immunology

authors

Lázaro S,Gamarra D,Del Val M

doi

10.1016/j.molimm.2015.04.014

subject

Has Abstract

pub_date

2015-12-01 00:00:00

pages

72-6

issue

2 Pt A

eissn

0161-5890

issn

1872-9142

pii

S0161-5890(15)00373-9

journal_volume

68

pub_type

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