Evidence map›Paper›PMID 24616479›Full record

ArticleJournal of immunology (Baltimore, Md. : 1950)2014

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

Georgio Kourjian, Yang Xu, Ijah Mondesire-Crump, Mariko Shimada, Pauline Gourdain, Sylvie Le Gall

Open access · bronzeAbstract read
In one paragraph

Article in Journal of immunology (Baltimore, Md. : 1950), 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.2field-weighted citation impact, top 24% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

17 citing papers in PubMed, 19 citations in OpenAlex.

  1. Trial
  2. Article
  3. Animal models for COVID-19: advances, gaps and perspectives.Signal transduction and targeted therapy · 2022
    Review
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 2 institutions in 1 country.

Georgio KourjianRagon Institute of MGH, MIT and Harvard, Massachusetts General Hospital, Harvard Medical School, Cambridge, MA 02139.
Yang Xu
Ijah Mondesire-Crump
Mariko Shimada
Pauline Gourdain
Sylvie Le Gall
Ragon Institute of MGH, MIT and Harvard · USHarvard University · US

Funding

Mechanisms and optimization of epitope presentation by HIV-infectable cell subsetR01AI084753 · NIAID · MASSACHUSETTS GENERAL HOSPITAL · PI LE GALL, SYLVIE · 2009 to 2013
$2.3M
Immune responses against HIV-induced cell-derived neoepitopes and HIV controlR01AI084106 · NIAID · MASSACHUSETTS GENERAL HOSPITAL · PI LE GALL, SYLVIE · 2009 to 2012
$2.1M
NIAID NIH HHS AI084106NIAID NIH HHS AI084753NIAID NIH HHS R01 AI084106NIAID NIH HHS R01 AI084753
6 · The paper itself

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.

Indexed as

Amino Acid SequenceAminopeptidasesAntigen PresentationCD8-Positive T-LymphocytesEnzyme ActivationEpitopes, T-LymphocyteHIV-1HIV Protease InhibitorsHumansIntracellular SpaceProteasome Endopeptidase ComplexProtein StabilityProteolysisT-Lymphocytes, CytotoxicAminopeptidasesEpitopes, T-LymphocyteHIV Protease InhibitorsProteasome Endopeptidase Complex

Identifiers

PMID24616479
PMCPMC3983674
OpenAlexW1751357090

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

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.