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Neuromyelitis optica spectrum disorder (NMOSD) is a relapsing autoimmune disease characterized by the presence of pathogenic autoantibodies, anti-aquaporin 4 (AQP4) antibodies. Recently,  HLA-DQA1*05:03  was shown to be significantly associated with NMOSD in a Japanese patient cohort. However, the specific mechanism by which  HLA-DQA1*05:03  is associated with the development of NMOSD has yet to be elucidated. In the current study, we revealed that  HLA-DQA1*05:03  exhibited significantly higher cell surface expression levels compared to other various  DQA1  alleles, and that its expression strongly depended on the amino acid sequence of the α1 domain, with a preference for leucine at position 75. Moreover, in silico analysis indicated that the HLA-DQ encoded by  HLA-DQA1*05:03  preferentially presents immunodominant AQP4 peptides, and that the peptide major histocompatibility complexes (pMHCs) are more energetically stable in the presence of  HLA-DQA1*05:03  than other  HLA-DQA1  alleles. In silico 3D structural models were also applied to investigate the validity of the energetic stability of pMHCs. Taken together, our findings indicate that  HLA-DQA1*05:03  possesses a distinct property to play a pathogenic role in the development of NMOSD.

High cell surface expression and peptide binding affinity of HLA-DQA1*05:03, a susceptible allele of neuromyelitis optica spectrum disorders (NMOSD)