Evidence map›Paper›PMID 40749828›Full record

ArticleThe Journal of biological chemistry2025

Molecular characterization of the archaic HLA-B∗73:01 allele reveals presentation of a unique peptidome and skewed engagement by KIR2DL2.

Philipp Ross, Hugo G Hilton, Jane Lodwick, Tomasz Slezak, Lisbeth A Guethlein, Curtis P McMurtrey, Alex S Han, Morten Nielsen, Daniel Yong, Charles L Dulberger and 8 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in The Journal of biological chemistry, 2025. 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

5 · Who and what money

Authors and funding

18 authors.

Philipp RossDepartment of Biochemistry and Molecular Biology, The University of Chicago, Chicago, Illinois, USA; Committee on Genetics, Genomics and Systems Biology, The University of Chicago, Chicago, Illinois, USA.
Hugo G HiltonDepartment of Structural Biology, School of Medicine, Stanford University, Stanford, USA; Department of Microbiology & Immunology, School of Medicine, Stanford University, Stanford, USA.
Jane LodwickDepartment of Biochemistry and Molecular Biology, The University of Chicago, Chicago, Illinois, USA.
Tomasz SlezakDepartment of Biochemistry and Molecular Biology, The University of Chicago, Chicago, Illinois, USA.
Lisbeth A GuethleinDepartment of Structural Biology, School of Medicine, Stanford University, Stanford, USA; Department of Microbiology & Immunology, School of Medicine, Stanford University, Stanford, USA.
Curtis P McMurtreyDepartment of Microbiology & Immunology, University of Oklahoma Health Sciences Center, Oklahoma City, Oklahoma, USA.
Alex S HanDepartment of Structural Biology, School of Medicine, Stanford University, Stanford, USA; Department of Microbiology & Immunology, School of Medicine, Stanford University, Stanford, USA.
Morten NielsenDepartment of Health Technology, Technical University of Denmark, Kgs. Lyngby, Denmark.
Daniel YongDepartment of Biochemistry and Molecular Biology, The University of Chicago, Chicago, Illinois, USA.
Charles L DulbergerDepartment of Biochemistry and Molecular Biology, The University of Chicago, Chicago, Illinois, USA.
Kristof T NolanDepartment of Biochemistry and Molecular Biology, The University of Chicago, Chicago, Illinois, USA.
Sobhan RoyDepartment of Biochemistry and Molecular Biology, The University of Chicago, Chicago, Illinois, USA.
Caitlin D CastroDepartment of Biochemistry and Molecular Biology, The University of Chicago, Chicago, Illinois, USA.
William H HildebrandDepartment of Microbiology & Immunology, University of Oklahoma Health Sciences Center, Oklahoma City, Oklahoma, USA.
Minglei ZhaoDepartment of Biochemistry and Molecular Biology, The University of Chicago, Chicago, Illinois, USA.
Anthony KossiakoffDepartment of Biochemistry and Molecular Biology, The University of Chicago, Chicago, Illinois, USA.
Peter ParhamDepartment of Structural Biology, School of Medicine, Stanford University, Stanford, USA; Department of Microbiology & Immunology, School of Medicine, Stanford University, Stanford, USA. Electronic address: peropa@stanford.edu.
Erin J AdamsDepartment of Biochemistry and Molecular Biology, The University of Chicago, Chicago, Illinois, USA; Committee on Genetics, Genomics and Systems Biology, The University of Chicago, Chicago, Illinois, USA. Electronic address: ejadams@uchicago.edu.

Funding

STRUCTURAL BIOLOGY OF HLA-A,B ANTIGENSR01AI017892 · NIAID · STANFORD UNIVERSITY · PI PARHAM, PETER R · 1985 to 2019
$6.1M
INTERACTIONS BETWEEN HLA CLASS I &CYTOLYTIC LYMPHOCYTESR01AI022039 · NIAID · STANFORD UNIVERSITY · PI PARHAM, PETER R · 1985 to 2017
$5.2M
Chaperone-Assisted Structure Determination of Membrane ProteinsR01GM117372 · NIGMS · UNIVERSITY OF CHICAGO · PI ANTHONY A KOSSIAKOFF · 2016 to 2026
$4.0M
Molecular and functional investigation of the role of CD1 in gamma delta T cell surveillanceR01AI155984 · NIAID · UNIVERSITY OF CHICAGO · PI ADAMS, ERIN JUNE · 2020 to 2024
$2.7M
Structural and Functional Studies of Molecular Machines Involved in Chemical Modifications of MacromoleculesR35GM143052 · NIGMS · UNIVERSITY OF CHICAGO · PI ZHAO, MINGLEI · 2021 to 2025
$2.1M
Beagle-3: A Shared GPU Cluster for Biomolecular SciencesS10OD028655 · OD · UNIVERSITY OF CHICAGO · PI ROUX, BENOIT · 2020 to 2020
$2.0M
Chemoproteomic discovery of secreted microbial enzymes for engineered probioticsF31AI178923 · NIAID · UNIVERSITY OF CALIFORNIA-IRVINE · PI FALCO, NATALIE · 2024 to 2025
$92k
NIAID NIH HHS F31 AI178923NIAID NIH HHS R01 AI017892NIAID NIH HHS R01 AI022039NIAID NIH HHS R01 AI155984NIGMS NIH HHS R01 GM117372NIGMS NIH HHS R35 GM143052NIH HHS S10 OD028655
6 · The paper itself

Abstract

HLA class I alleles of archaic origin may have been retained in modern humans because they provide immunity against diseases to which archaic humans had evolved resistance. According to this model, archaic introgressed alleles were somehow distinct from those that evolved in African populations. Here, we show that HLA-B∗73:01, a rare allotype with putative archaic origins, has a relatively rare peptide binding motif with an unusually long-tailed peptide length distribution. We also find that HLA-B∗73:01 combines a restricted and unique peptidome with high-cell surface expression, characteristics that make it well-suited to combat one or a number of closely related pathogens. Furthermore, a crystal structure of HLA-B∗73:01 in complex with KIR2DL2 highlights differences from previously solved structures with HLA-C molecules. These molecular characteristics distinguish HLA-B∗73:01 from other HLA class I alleles previously investigated and may have provided early modern human migrants that inherited this allele with a selective advantage as they colonized Europe and Asia.

Indexed as

HLA-B AntigensProteomeReceptors, KIR2DL2AllelesAmino Acid SequenceBinding SitesCell LineCrystallography, X-RayHumansHydrogen BondingModels, MolecularPeptidesProtein Structure, QuaternaryProtein Structure, TertiaryHLA-B AntigensKIR2DL2 protein, humanPeptidesProteomeReceptors, KIR2DL2antigens/peptides/epitopescomparative immunology/evolutionMHCnatural killer cells

Identifiers

PMID40749828
PMCPMC12450638

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.