Evidence map›Paper›PMID 30146122›Full record

ReviewMolecular immunology2019

Selection of immunodominant epitopes during antigen processing is hierarchical.

Scheherazade Sadegh-Nasseri, AeRyon Kim

Open access · greenAbstract readReview
In one paragraph

Review in Molecular immunology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.1field-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

22 citing papers in PubMed, 27 citations in OpenAlex.

  1. Article
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  6. Immunoprotective effect and mechanism of rEg.P29 against CD4Acta biochimica et biophysica Sinica · 2024
    Article
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  12. Revisiting the Principles of Designing a Vaccine.Methods in molecular biology (Clifton, N.J.) · 2022
    Article
  13. 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

2 authors at 1 institution in 1 country.

Scheherazade Sadegh-NasseriDepartment of Pathology, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA. Electronic address: ssadegh@jhmi.edu.
AeRyon KimDepartment of Pathology, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.
Johns Hopkins University · US

Funding

Role of DM in Generation of Immunodominant Epitope(s)R01AI063764 · NIAID · JOHNS HOPKINS UNIVERSITY · PI SADEGH-NASSERI, SCHEHERAZADE · 2006 to 2015
$3.6M
Understanding the Impacts of HLA-DO in vivoR01AI120634 · NIAID · JOHNS HOPKINS UNIVERSITY · PI SADEGH-NASSERI, SCHEHERAZADE · 2016 to 2019
$1.6M
Molecular Mechanisms of HLA-DO in Antigen ProcessingR21AI101987 · NIAID · JOHNS HOPKINS UNIVERSITY · PI SADEGH-NASSERI, SCHEHERAZADE · 2012 to 2013
$433k
NIAID NIH HHS R01 AI063764NIAID NIH HHS R01 AI120634NIAID NIH HHS R21 AI101987
6 · The paper itself

Abstract

MHC II proteins present processed antigens to CD4 + T cells through a complex set of events and players that include chaperons and accessory molecules. Antigen processing machinery is optimized for the selection of the best fitting peptides, called 'immunodominant epitopes', in the MHC II groove to which, specific CD4 + T cells respond and differentiate into memory T cells. However, due to the complexity of antigen processing, understanding the parameters that lead to immunodominance has proved difficult. Moreover, immunodominance of epitopes vary, depending on multiple factors that include; simultaneous processing of multiple proteins, involvement of multiple alleles of MHC II that can bind to the same antigen, or competition among several suitable epitopes on a single protein antigen. The current dogma assumes that once an antigenic determinant is selected under a specific condition, it would emerge immunodominant wherever it is placed. Here we will discuss some established parameters that contribute to immunodominance as well as some new findings, which demonstrate that slight changes to antigen structure can cause a complete shift in epitope selection during antigen processing and distort the natural immunodominant epitope.

Indexed as

AnimalsAntigen PresentationAntigen-Presenting CellsAntigensCD4-Positive T-LymphocytesEpitopesHistocompatibility Antigens Class IIHumansImmunodominant EpitopesImmunologic MemoryPeptidesAntigensEpitopesHistocompatibility Antigens Class IIImmunodominant EpitopesPeptidesCathepsinsCell free antigen processingEpitope hierarchyHLA-DRImmunodominanceStructural constraints

Identifiers

PMID30146122
PMCPMC6387654
OpenAlexW2888194811

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.