NDLI: Sequence-specific alterations of epitope production by HIV protease inhibitors.

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Sequence-specific alterations of epitope production by HIV protease inhibitors.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Xu, Yang Gourdain, Pauline Shimada, Mariko Mondesire-Crump, Ijah Kourjian, Georgio Le Gall, Sylvie
Description	Author Affiliation: Kourjian G ( Ragon Institute of MGH, MIT and Harvard, Massachusetts General Hospital, Harvard Medical School, Cambridge, MA 02139.)
Abstract	Ag processing by intracellular proteases and peptidases and epitope presentation are critical for recognition of pathogen-infected cells by CD8+ T lymphocytes. First-generation HIV protease inhibitors (PIs) alter proteasome activity, but the effect of first- or second-generation PIs on other cellular peptidases, the underlying mechanism, and impact on Ag processing and epitope presentation to CTL are still unknown. In this article, we demonstrate that several HIV PIs altered not only proteasome but also aminopeptidase activities in PBMCs. Using an in vitro degradation assay involving PBMC cytosolic extracts, we showed that PIs altered the degradation patterns of oligopeptides and peptide production in a sequence-specific manner, enhancing the cleavage of certain residues and reducing others. PIs affected the sensitivity of peptides to intracellular degradation, and altered the kinetics and amount of HIV epitopes produced intracellularly. Accordingly, the endogenous degradation of incoming virions in the presence of PIs led to variations in CTL-mediated killing of HIV-infected cells. By altering host protease activities and the degradation patterns of proteins in a sequence-specific manner, HIV PIs may diversify peptides available for MHC class I presentation to CTL, alter the patterns of CTL responses, and provide a complementary approach to current therapies for the CTL-mediated clearance of abnormal cells in infection, cancer, or other immune disease.
ISSN	00221767
e-ISSN	15506606
DOI	10.4049/jimmunol.1302805
Journal	The Journal of Immunology
Issue Number	8
Volume Number	192
Language	English
Publisher	The American Association of Immunologists
Publisher Date	2014-04-15
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Aminopeptidases Metabolism Antigen Presentation Drug Effects Immunology Epitopes, T-lymphocyte Hiv Protease Inhibitors Pharmacology Amino Acid Sequence Cd8-positive T-lymphocytes Enzymology Enzyme Activation Chemistry Hiv-1 Intracellular Space Proteasome Endopeptidase Complex Protein Stability Proteolysis T-lymphocytes, Cytotoxic Research Support, N.i.h., Extramural Discipline Immunology
Content Type	Text
Resource Type	Article
Subject	Immunology and Allergy Immunology

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CD8+ TCR Bias and Immunodominance in HIV-1 Infection.

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Proteasome inhibitors induce the presentation of an Epstein-Barr virus nuclear antigen 1-derived cytotoxic T lymphocyte epitope in Burkitt’s lymphoma cells

HLA-F and MHC-I open conformers cooperate in a MHC-I antigen cross-presentation pathway.

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Fine-tuning of T-cell receptor avidity to increase HIV epitope variant recognition by cytotoxic T lymphocytes.

Clustering Patterns of Cytotoxic T-Lymphocyte Epitopes in Human Immunodeficiency Virus Type 1 (HIV-1) Proteins Reveal Imprints of Immune Evasion on HIV-1 Global Variation (2002)

Sequence-specific alterations of epitope production by HIV protease inhibitors.

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CD8+ TCR Bias and Immunodominance in HIV-1 Infection.

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Sequence-specific alterations of epitope production by HIV protease inhibitors.