Peptide-binding characteristics of the novel allele DRB1*0112 are probably identical to DRB1*0101.
So far 11 different amino acid variants of the HLA-DRB1*01 family have been reported. We here describe the identification of a new HLA-DRB1*01 allele in a healthy female Caucasian. The allele was detected by sequencing-based typing during high-resolution typing of a potential unrelated donor from the North German Bone Marrow Registry (NKR). Compared with DRB1*010101, to which it is closest, the new variant is characterized by a new replacement mutation (G-->T) at nucleotide position 202 of exon 2, resulting in the amino acid substitution Arg-->Leu at position 72. Because this amino acid position is not involved in peptide binding or T-cell interaction, it is likely to represent a permissive mismatch to the more common HLA-DRB1*0101 allele.
Horn
P A
PA
Department of Transfusion Medicine, Hannover Medical School, Carl-Neuberg-Strasse 1, 30625 Hannover, Germany.
DeLuca
D S
DS
Mueller
K
K
Blasczyk
R
R
D000328:Adult; D000483:Alleles; D000595:Amino Acid Sequence; D019943:Amino Acid Substitution; D001665:Binding Sites; D005091:Exons / Q000235:genetics; D005260:Female; D005802:Genes, MHC Class II; D005858:Germany; D006684:HLA-DR Antigens / Q000737:chemistry / Q000235:genetics* / Q000302:isolation & purification / Q000378:metabolism; D059811:HLA-DRB1 Chains; D006648:Histocompatibility; D006801:Humans; D008969:Molecular Sequence Data; D017354:Point Mutation; D011485:Protein Binding; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid
D006684:HLA-DR Antigens; D059811:HLA-DRB1 Chains; C503741:HLA-DRB1*01:12 antigen