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PreprintCited by 1vaccines and immunoinformatics approachesImmune Cell Function and InteractionHIV Research and Treatment

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

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Ross, Philipp, Hilton, Hugo G., Lodwick, Jane, Slezak, Tomasz, Guethlein, Lisbeth A., McMurtrey, Curtis P., Han, Alex S., Nielsen, Morten, Yong, Daniel, Dulberger, Charles L., Nolan, Kristof T., Roy, Sobhan, Castro, Caitlin D., Hildebrand, William H., Zhao, Minglei, Kossiakoff, Anthony, Parham, Peter, Adams, Erin J.·2024·Journal of Biological Chemistry
DOI 10.1101/2024.11.25.625330PMC PMC12450638

Preprint — published as 10.1016/j.jbc.2025.110542 · Paper page

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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.

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Metadata

Authors
Ross, P., Hilton, H. G., Lodwick, J., Slezak, T., Guethlein, L. A., McMurtrey, C. P., Han, A. S., Nielsen, M., Yong, D., Dulberger, C. L., Nolan, K. T., Roy, S., Castro, C. D., Hildebrand, W. H., Zhao, M., Kossiakoff, A., Parham, P., & Adams, E. J.
Affiliations
  • University of Chicago (US)
  • Stanford Medicine (US)
  • University of Oklahoma Health Sciences Center (US)
  • Technical University of Denmark (DK)
Corresponding author
  • Parham, Peter
  • Adams, Erin J.
ORCID
Venue
Journal of Biological Chemistry
Publisher
openRxiv
Published
2024-11-28
Volume
301
Issue
9
Pages
110542-110542
ISSN
0021-9258 (ISSN-L)
DOI
10.1101/2024.11.25.625330
PMC
PMC12450638
OpenAlex
W4412737771
Cited by
1
References
1
Citations by year
2026: 1
FWCI
0.30
Type
journal article
Language
en
Open access
Licence
Locations
  • Journal of Biological Chemistry (publishedVersion, cc-by)
  • bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc-nd)
  • Europe PMC (PubMed Central) (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed Central (submittedVersion, cc-by-nc-nd)
Funders
  • U.S. Department of Energy
  • University of Chicago (SCR_019198, SCR_017760)
  • National Institutes of Health (AI17892, 1s10od028655-01)
  • Office of Science
  • Research Computing Center, University of Chicago
  • National Institute of General Medical Sciences (R01GM117372, R35GM143052)
  • National Institute of Allergy and Infectious Diseases (R01AI022039, R01AI155984, R01AI017892, F31AI178923)
  • Argonne National Laboratory (DE- AC02-06-CH11357)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › vaccines and immunoinformatics approaches
  • Life Sciences › Immunology and Microbiology › Immunology › Immune Cell Function and Interaction
  • Life Sciences › Immunology and Microbiology › Virology › HIV Research and Treatment
Keywords
archaic introgression, HLA class I, peptide binding motifs, peptide length distribution, KIR2DL2, HLA-C, cell surface expression, pathogen resistance

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