Evidence map›Paper›PMID 32265295›Full record

ArticleMolecular & cellular proteomics : MCP2020

Modulation of Natural HLA-B*27:05 Ligandome by Ankylosing Spondylitis-associated Endoplasmic Reticulum Aminopeptidase 2 (ERAP2).

Elena Lorente, Miguel G Fontela, Eilon Barnea, Antonio J Martín-Galiano, Carmen Mir, Begoña Galocha, Arie Admon, Pilar Lauzurica, Daniel López

Open access · hybridAbstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
2.5field-weighted citation impact, top 10% 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

14 citing papers in PubMed, 23 citations in OpenAlex.

  1. Review
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  3. Endoplasmic reticulum aminopeptidase 2 regulates CD4Arthritis research & therapy · 2024
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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

9 authors at 3 institutions in 2 countries.

Elena LorenteUnidad de Presentación y Regulación Inmunes, 28220 Majadahonda (Madrid), Spain.
Miguel G FontelaUnidad de Presentación y Regulación Inmunes, 28220 Majadahonda (Madrid), Spain.
Eilon BarneaDepartment of Biology, Technion-Israel Institute of Technology, 32000 Haifa, Israel.
Antonio J Martín-GalianoUnidad de Bioinformática, Instituto de Salud Carlos III, 28220 Majadahonda (Madrid), Spain.
Carmen MirUnidad de Presentación y Regulación Inmunes, 28220 Majadahonda (Madrid), Spain.
Begoña GalochaUnidad de Presentación y Regulación Inmunes, 28220 Majadahonda (Madrid), Spain.
Arie AdmonDepartment of Biology, Technion-Israel Institute of Technology, 32000 Haifa, Israel.
Pilar LauzuricaUnidad de Presentación y Regulación Inmunes, 28220 Majadahonda (Madrid), Spain.
Daniel LópezUnidad de Presentación y Regulación Inmunes, 28220 Majadahonda (Madrid), Spain. Electronic address: dlopez@isciii.es.
Technion – Israel Institute of Technology · ILCentro Nacional de Microbiologia · ESInstituto de Salud Carlos III · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The HLA-B*27:05 allele and the endoplasmic reticulum-resident aminopeptidases are strongly associated with AS, a chronic inflammatory spondyloarthropathy. This study examined the effect of ERAP2 in the generation of the natural HLA-B*27:05 ligandome in live cells. Complexes of HLA-B*27:05-bound peptide pools were isolated from human ERAP2-edited cell clones, and the peptides were identified using high-throughput mass spectrometry analyses. The relative abundance of a thousand ligands was established by quantitative tandem mass spectrometry and bioinformatics analysis. The residue frequencies at different peptide position, identified in the presence or absence of ERAP2, determined structural features of ligands and their interactions with specific pockets of the antigen-binding site of the HLA-B*27:05 molecule. Sequence alignment of ligands identified with species of bacteria associated with HLA-B*27-dependent reactive arthritis was performed. In the absence of ERAP2, peptides with N-terminal basic residues and minority canonical P2 residues are enriched in the natural ligandome. Further, alterations of residue frequencies and hydrophobicity profile at P3, P7, and PΩ positions were detected. In addition, several ERAP2-dependent cellular peptides were highly similar to protein sequences of arthritogenic bacteria, including one human HLA-B*27:05 ligand fully conserved in a protein from

Indexed as

AllelesAmino Acid SequenceAminopeptidasesCampylobacter jejuniCell LineComputational BiologyEndoplasmic ReticulumGene Knockout TechniquesHigh-Throughput Screening AssaysHLA-B27 AntigenHumansHydrophobic and Hydrophilic InteractionsLigandsPeptidesProteomeSequence AlignmentAminopeptidasesERAP2 protein, humanHLA-B27 AntigenLigandsPeptidesProteomeAnkylosing SpondylitisAntigen ProcessingHLAHPLCImmunologyLabel-Free QuantificationMass SpectrometryPeptides

Identifiers

PMID32265295
PMCPMC7261815
OpenAlexW3014362057

What OpenQuestion holds

Textmetadata
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.