Evidence map›Paper›PMID 38939106›Full record

ArticleiScience2024

CRISPR-Cas9 screening reveals a distinct class of MHC-I binders with precise HLA-peptide recognition.

Tom A W Schoufour, Anneloes van der Plas-van Duijn, Ian Derksen, Marije Melgers, Jacqueline M F van Veenendaal, Claire Lensen, Mirjam H M Heemskerk, Jacques Neefjes, Ruud H M Wijdeven, Ferenc A Scheeren

Abstract read
In one paragraph

Article in iScience, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact
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

1 citing paper in PubMed.

  1. Review
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

10 authors.

Tom A W SchoufourDepartment of Cell and Chemical Biology, Oncode Institute, Leiden University Medical Center, 2333 ZA Leiden, Zuid-Holland, the Netherlands.
Anneloes van der Plas-van DuijnDepartment of Medical Oncology, Leiden University Medical Center, 2333 ZA Leiden, Zuid-Holland, the Netherlands.
Ian DerksenDepartment of Dermatology, Leiden University Medical Center, 2333 ZA Leiden, Zuid-Holland, the Netherlands.
Marije MelgersDepartment of Cell and Chemical Biology, Oncode Institute, Leiden University Medical Center, 2333 ZA Leiden, Zuid-Holland, the Netherlands.
Jacqueline M F van VeenendaalDepartment of Dermatology, Leiden University Medical Center, 2333 ZA Leiden, Zuid-Holland, the Netherlands.
Claire LensenDepartment of Medical Oncology, Leiden University Medical Center, 2333 ZA Leiden, Zuid-Holland, the Netherlands.
Mirjam H M HeemskerkDepartment of Hematology, Leiden University Medical Center, 2333 ZA Leiden, Zuid-Holland, the Netherlands.
Jacques NeefjesDepartment of Cell and Chemical Biology, Oncode Institute, Leiden University Medical Center, 2333 ZA Leiden, Zuid-Holland, the Netherlands.
Ruud H M WijdevenDepartment of Cell and Chemical Biology, Oncode Institute, Leiden University Medical Center, 2333 ZA Leiden, Zuid-Holland, the Netherlands.
Ferenc A ScheerenDepartment of Dermatology, Leiden University Medical Center, 2333 ZA Leiden, Zuid-Holland, the Netherlands.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Human leukocyte antigen (HLA) class-I molecules present fragments of the cellular proteome to the T cell receptor (TCR) of cytotoxic T cells to control infectious diseases and cancer. The large number of combinations of HLA class-I allotypes and peptides allows for highly specific and dedicated low-affinity interactions to a diverse array of TCRs and natural killer (NK) cell receptors. Whether the divergent HLA class-I peptide complex is exclusive for interactions with these proteins is unknown. Using genome-wide CRISPR-Cas9 activation and knockout screens, we identified peptide-specific HLA-C∗07 combinations that can interact with the surface molecules CD55 and heparan sulfate. These interactions closely resemble the HLA class-I interaction with the TCR regarding both the affinity range and the specificity of the peptide and HLA allele. These findings indicate that various proteins can specifically bind HLA class-I peptide complexes due to their polymorphic nature, which suggests there are more interactions like the ones we describe here.

Indexed as

BiochemistryBioinformaticsBiological sciencesImmunologyNatural sciences

Identifiers

PMID38939106
PMCPMC11209011

What OpenQuestion holds

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Registered trials

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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.