Three novel HLA-B alleles identified in haematopoietic stem cell donors by NGS: HLA-B*07:513, HLA-B*07:514 and HLA-B*50:01:25.
Three novel HLA-B alleles identified in haematopoietic stem cell donors by NGS: HLA-B*07:513, HLA-B*07:514 and HLA-B*50:01:25.
HLA-DQB1*03:533 differs from HLA-DQB1*03:02:01:01 by a non-synonymous nucleotide substitution in exon 3.
HLA-C*07:640:02 differs from HLA-C*07:640:01 by a single non-synonymous nucleotide change in exon 3.
HLA-A*02:558 differs from HLA-A*02:06:01:01 by one nucleotide substitution in codon 96 in exon 3.
HLA-A*02:559 differs from HLA-A*02:01:01:01 by one nucleotide substitution in codon 188 in exon 4.
Imlifidase cleaves intact IgG molecules, generating F(ab′)2 fragments that still bind to the target antigen but are devoid of the Fc-dependent effector functions, notably complement activation. Imlifidase (Idefirix) has been conditionally approved for desensitisation to enable kidney transplantation in highly sensitised adult patients. We hypothesised that the F(ab′)2 fragments can prevent the attachment of the full IgG at the time of anti-HLA antibodies rebound when imlifidase action fades away, lowering the deleterious effect of the antibody burden on the transplant. This competition was explored in vitro using the Luminex Mixed or Single Antigen bead assays, and with an antibody detecting the specific imlifidase-cleaved IgG. Functional assays for complement activation were also performed, which were the C1q bead assay and complement-dependent cytotoxicity crossmatches. We selected sera from patients with a high amount of class I or class II anti-HLA antibodies. Competition by imlifidase-digested serum was observed in Luminex antibody-binding assays and cellular complement activation assays. F(ab′)2 fragments generated from anti-HLA antibodies after imlifidase cleavage had a biological impact on intact IgG binding, leading to reduced complement activation. Additional studies are needed to demonstrate whether these in vitro features have beneficial clinical consequences in vivo, that is, protecting the graft from potentially deleterious effects of DSA rebound.
L. A. Marin Rubio and J. Ontañon, “HLA-DPA1*01:228 is the First DPB1 Allele Described With an Alanine at Position 42 of Alpha-1 Domain,” HLA 106, no. 5 (2025): e70450, https://doi.org/10.1111/tan.70450.
In the article, the ‘DPB1’ in the title was incorrect and should be changed to ‘DPA1’.
The incorrect title is:
HLA-DPA1*01:228 is the First DPB1 Allele Described With an Alanine at Position 42 of Alpha-1 Domain
The correct title should be:
HLA-DPA1*01:228 is the First DPA1 Allele Described With an Alanine at Position 42 of Alpha-1 Domain
The online version of the article has been corrected.
We apologise for this error.
HLA-B*35:359 differs from HLA-B*35:01:01:01 by one nucleotide substitution at position 650 (C → T) in exon 4.
The novel HLA-B*35:01:86 and HLA-DRB1*15:243 alleles were detected during the HLA typing process.
Three HLA-B and three HLA-C novel alleles detected by next-generation sequencing.
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