Evidence map›Paper›PMID 20934997›Full record

ArticleHaematologica2011

The impact of human leukocyte antigen (HLA) micropolymorphism on ligand specificity within the HLA-B*41 allotypic family.

Christina Bade-Döding, Alex Theodossis, Stephanie Gras, Lars Kjer-Nielsen, Britta Eiz-Vesper, Axel Seltsam, Trevor Huyton, Jamie Rossjohn, James McCluskey, Rainer Blasczyk

Open access · goldAbstract read
In one paragraph

Article in Haematologica, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

31 citing papers in PubMed, 48 citations in OpenAlex.

  1. Skewed MHC Class I Peptide Presentation in Psoriatic Arthritis.International journal of molecular sciences · 2026
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  6. Unravelling the Proteomics of HLA-B*57:01Journal of personalized medicine · 2022
    Article
  7. The molecular basis of how buried human leukocyte antigen polymorphism modulates natural killer cell function.Proceedings of the National Academy of Sciences of the United States of America · 2020
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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

10 authors at 4 institutions in 2 countries.

Christina Bade-DödingInstitute for Transfusion Medicine, Hannover Medical School, Hannover, Germany.
Alex Theodossis
Stephanie Gras
Lars Kjer-Nielsen
Britta Eiz-Vesper
Axel Seltsam
Trevor Huyton
Jamie Rossjohn
James McCluskey
Rainer Blasczyk
Medizinische Hochschule Hannover · DEMonash University · AUUniversity of Melbourne · AUGerman Red Cross · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundPolymorphic differences between human leukocyte antigen (HLA) molecules affect the specificity and conformation of their bound peptides and lead to differential selection of the T-cell repertoire. Mismatching during allogeneic transplantation can, therefore, lead to immunological reactions. DESIGN AND

methodsWe investigated the structure-function relationships of six members of the HLA-B*41 allelic group that differ by six polymorphic amino acids, including positions 80, 95, 97 and 114 within the antigen-binding cleft. Peptide-binding motifs for B*41:01, *41:02, *41:03, *41:04, *41:05 and *41:06 were determined by sequencing self-peptides from recombinant B*41 molecules by electrospray ionization tandem mass spectrometry. The crystal structures of HLA-B*41:03 bound to a natural 16-mer self-ligand (AEMYGSVTEHPSPSPL) and HLA-B*41:04 bound to a natural 11-mer self-ligand (HEEAVSVDRVL) were solved.

resultsPeptide analysis revealed that all B*41 alleles have an identical anchor motif at peptide position 2 (glutamic acid), but differ in their choice of C-terminal pΩ anchor (proline, valine, leucine). Additionally, B*41:04 displayed a greater preference for long peptides (>10 residues) when compared to the other B*41 allomorphs, while the longest peptide to be eluted from the allelic group (a 16mer) was obtained from B*41:03. The crystal structures of HLA-B*41:03 and HLA-B*41:04 revealed that both alleles interact in a highly conserved manner with the terminal regions of their respective ligands, while micropolymorphism-induced changes in the steric and electrostatic properties of the antigen-binding cleft account for differences in peptide repertoire and auxiliary anchoring.

conclusionsDifferences in peptide repertoire, and peptide length specificity reflect the significant functional evolution of these closely related allotypes and signal their importance in allogeneic transplantation, especially B*41:03 and B*41:04, which accommodate longer peptides, creating structurally distinct peptide-HLA complexes.

Indexed as

Epitopes, T-LymphocyteHLA-B AntigensHumansPeptide FragmentsPolymorphism, Single NucleotideProtein BindingProtein ConformationRecombinant ProteinsSpectrometry, Mass, Electrospray IonizationT-Lymphocytes, CytotoxicEpitopes, T-LymphocyteHLA-B41 antigenHLA-B AntigensPeptide FragmentsRecombinant Proteins

Identifiers

PMID20934997
PMCPMC3012774
OpenAlexW2167272317

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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.