ArticleThe Journal of experimental medicine2000
Efficient generation of a hepatitis B virus cytotoxic T lymphocyte epitope requires the structural features of immunoproteasomes.
Article in The Journal of experimental medicine, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.
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Who cites it
53 citing papers in PubMed, 150 citations in OpenAlex.
- ANKRD11 deficiency reprograms CD8Nature immunology · 2026Article
- Identification of novel HLA class I-restricted hepatitis B virus peptides and their modulation by peptide editor TAPBPR.Frontiers in immunology · 2026Article
- IFN-γ production by brain-resident cells activates cerebral mRNA expression of a wide spectrum of molecules critical for both innate and T cell-mediated protective immunity to control reactivation of chronic infection withFrontiers in cellular and infection microbiology · 2023Article
- The role of cellular proteostasis in antitumor immunity.The Journal of biological chemistry · 2022Review
- The Importance of Being Presented: Target Validation by Immunopeptidomics for Epitope-Specific Immunotherapies.Frontiers in immunology · 2022Review
- Mechanistic diversity in MHC class I antigen recognition.The Biochemical journal · 2021Review
- Review
- Review
- Co-Inhibition of the Immunoproteasome Subunits LMP2 and LMP7 Ameliorates Immune Thrombocytopenia.Frontiers in immunology · 2020Article
- Spatiotemporal Differences in Presentation of CD8 T Cell Epitopes during Hepatitis B Virus Infection.Journal of virology · 2019Article
- Immunoproteasome induction is suppressed in hepatitis C virus-infected cells in a protein kinase R-dependent manner.Experimental & molecular medicine · 2016Article
- Proteasome subtypes and regulators in the processing of antigenic peptides presented by class I molecules of the major histocompatibility complex.Biomolecules · 2014Review
- Differential global structural changes in the core particle of yeast and mouse proteasome induced by ligand binding.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- The proteasome complex and the maintenance of pluripotency: sustain the fate by mopping up?Stem cell research & therapy · 2014Review
- Immunoproteasome Activation During Early Antiviral Response in Mouse Pancreatic β-cells: New Insights into Auto-antigen Generation in Type I Diabetes?Journal of clinical & cellular immunology · 2013Article
- Article
- Emerging roles of immunoproteasomes beyond MHC class I antigen processing.Cellular and molecular life sciences : CMLS · 2012Review
- Proteomic identification of immunoproteasome accumulation in formalin-fixed rodent spinal cords with experimental autoimmune encephalomyelitis.Journal of proteome research · 2012Article
- Immunoproteasomes: structure, function, and antigen presentation.Progress in molecular biology and translational science · 2012Review
- The role of the proteasome in the generation of MHC class I ligands and immune responses.Cellular and molecular life sciences : CMLS · 2011Review
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
Abstract
Interferon (IFN)-gamma-induced cells express the proteasome subunits low molecular weight protein (LMP)2, LMP7, and MECL-1 (multicatalytic endopeptidase complex-like 1), leading to the formation of immunoproteasomes. Although these subunits are thought to optimize MHC class I antigen processing, the extent of their role and the mechanistic aspects involved remain unclear. Herein, we study the proteolytic generation of an human histocompatibility leukocyte antigen (HLA)-Aw68-restricted hepatitis B virus core antigen (HBcAg) cytotoxic T lymphocyte (CTL) epitope that is recognized by peripheral blood lymphocytes from patients with acute self-limited but not chronic hepatitis B virus (HBV). Immunological data suggest that IFN-gamma-induced rather than uninduced HeLa cells process and present the HBV CTL epitope upon infection with HBcAg-expressing vaccinia viruses. Analyses of 20S proteasome digests of synthetic polypeptides covering the antigenic HBcAg peptide demonstrate that only immunoproteasomes efficiently perform the cleavages needed for the liberation of this HBV CTL epitope. Although the concerted presence of the three immunosubunits appears essential, we find that both catalytically active LMP7 and inactive LMP7 T1A support CTL epitope generation. We conclude that LMP7 influences the structural features of 20S proteasomes, thereby enhancing the activity of the LMP2 and MECL-1 catalytic sites, which provide cleavage specificity. Thus, LMP7 incorporation is of greater functional importance for the generation of an HBV CTL epitope than cleavage specificity.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.