Cut and trim: Generating MHC class I peptide ligands

Current Opinion in Immunology

Volumn 13, Issue 1, 2001, Pages 13-18

  Yewdell, J W ^a   Bennink, J R ^a  

^a NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CARRIER PROTEIN; LIGAND; MAJOR HISTOCOMPATIBILITY ANTIGEN; PROTEASOME;

ANTIGEN PRESENTATION; CELLULAR DISTRIBUTION; PROTEIN BINDING; PROTEIN DEGRADATION; PROTEIN SYNTHESIS; REVIEW; RIBOSOME;

EID: 0035142615     PISSN: 09527915     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0952-7915(00)00175-8     Document Type: Review

References (33)

1. Rapid degradation of a large fraction of newly synthesized proteins by the proteasome
2. The major substrates for TAP in vivo are derived from newly synthesized proteins
3. Intracellular rate-limiting steps in MHC class I antigen processing
4. The proteasome activator 11 S REG (PA28) and class I antigen presentation
5. 26 S proteasome-mediated production of an authentic major histocompatibility class I-restricted epitope from an intact protein substrate
6. The human 26 S and 20 S proteasomes generate overlapping but different sets of peptide fragments from a model protein substrate
7. The sizes of peptides generated from protein by mammalian 26 and 20 S proteasomes. Implications for understanding the degradative mechanism and antigen presentation
8. Potential immunocompetence of proteolytic fragments produced by proteasomes before evolution of the vertebrate immune system
9. The selective proteasome inhibitors lactacystin and epoxomicin can be used to either up- or down-regulate antigen presentation at nontoxic doses
10. Evidence for the existence of a non-catalytic modifier site of peptide hydrolysis by the 20 S proteasome
11. A theoretical approach towards the identification of cleavage-determining amino acid motifs of the 20 S proteasome
12. An algorithm for the prediction of proteasomal cleavages
13. Sequence signals for generation of antigenic peptides by the proteasome: Implications for proteasomal cleavage mechanism
14. Abrogation of CTL epitope processing by single amino acid substitution flanking the C-terminal proteasome cleavage site
15. Sequences that flank subdominant and cryptic epitopes influence the proteolytic generation of MHC class I-presented peptides
16. Specific proteolytic cleavages limit the diversity of the pool of peptides available to MHC class I molecules in living cells
17. Processing of some antigens by the standard proteasome but not by the immunoproteasome results in poor presentation by dendritic cells
18. Dendritic cells up-regulate immunoproteasomes and the proteasome regulator PA28 during maturation
19. MHC class I antigen processing of an adenovirus CTL epitope is linked to the levels of immunoproteasomes in infected cells
20. Overexpression of the proteasome subunits LMP2, LMP7, and MECL-1, but not PA28 alpha/beta, enhances the presentation of an immunodominant lymphocytic choriomeningitis virus T cell epitope
21. Generation of an immunodominant CTL epitope is affected by proteasome subunit composition and stability of the antigenic protein
22. -/- mice
23. Intracellular localization of proteasomal degradation of a viral antigen
24. Cytotoxic T lymphocyte epitopes of HIV-1 Nef:Generation of multiple definitive major histocompatibility complex class I ligands by proteasomes
25. Distinct proteolytic processes generate the C and N termini of MHC class I-binding peptides
26. Proteolytic processing of peptides in the lumen of the endoplasmic reticulum for antigen presentation by major histocompatibility class I
27. Sequential cleavage by metallopeptidases and proteasomes is involved in processing HIV-1 ENV epitope for endogenous MHC class I antigen presentation
28. Human transporters associated with antigen processing (TAPs) select epitope precursor peptides for processing in the endoplasmic reticulum and presentation to T cells
29. Discrete proteolytic intermediates in the MHC class I antigen processing pathway and MHC I-dependent peptide trimming in the ER
30. Thimet oligopeptidase and the stability of MHC class I epitopes in macrophage cytosol
31. Thimet oligopeptidase (EC 3.4.24.15), a novel protein on the route of MHC class I antigen presentation
32. A giant protease with potential to substitute for some functions of the proteasome
33. Efficiency of MHC class I antigen processing: A quantitative analysis