HLA class I peptide polymorphisms contribute to class II DQβ0603:DQα0103 antibody specificity

N. Remi Shih, Thoa Nong, Cathi Murphey, Mayra Lopez-Cepero, Peter W. Nickerson, Jean-luc Taupin, Magali Devriese, Jakob Nilsson, Marie-Benedicte Matignon, Robert A. Bray and Jar-How Lee ()
Additional contact information
N. Remi Shih: Terasaki Innovation Center
Thoa Nong: Terasaki Innovation Center
Cathi Murphey: Southwest Immunodiagnostics, Inc.
Mayra Lopez-Cepero: Terasaki Innovation Center
Peter W. Nickerson: University of Manitoba
Jean-luc Taupin: Hôpital Saint-Louis APHP
Magali Devriese: Hôpital Saint-Louis APHP
Jakob Nilsson: University Hospital Zurich
Marie-Benedicte Matignon: Hôpital Henri Mondor APHP
Robert A. Bray: Emory University
Jar-How Lee: Terasaki Innovation Center

Nature Communications, 2024, vol. 15, issue 1, 1-13

Abstract: Abstract Antibodies reactive to human leukocyte antigens (HLA) represent a barrier for patients awaiting transplantation. Based on reactivity patterns in single-antigen bead (SAB) assays, various epitope matching algorithms have been proposed to improve transplant outcomes. However, some antibody reactivities cannot be explained by amino acid motifs, leading to uncertainty about their clinical relevance. Antibodies against the HLA class II molecule, DQβ0603:DQα0103, present in some candidates, represent one such example. Here, we show that peptides derived from amino acids 119-148 of the HLA class I heavy chain are bound to DQβ0603:DQα0103 proteins and contribute to antibody reactivity through an HLA-DM-dependent process. Moreover, antibody reactivity is impacted by the specific amino acid sequence presented. In summary, we demonstrate that polymorphic HLA class I peptides, bound to HLA class II proteins, can directly or indirectly be part of the antibody binding epitope. Our findings have potential important implications for the field of transplant immunology and for our understanding of adaptive immunity.

Date: 2024
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DOI: 10.1038/s41467-024-44912-0

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