BACKGROUND: Anti-KANNO, a broadly reactive RBC alloantibody, is found among some Japanese pregnant women, but the genetic basis of the corresponding antigen remains unclear. ABBREVIATIONS: BAM = binary alignment map; cf = cysteine-free; DMEM = Dulbecco modified minimum essential medium; GPI = glycosylphosphatidylinositol; GWAS = genome-wide association study; LD = linkage disequilibrium; MAIEA = monoclonal antibodyspecific immobilization of erythrocyte antigens; mT = mTurquoise; PCR = polymerase chain reaction; QC = quality control; SNP = single-nucleotide polymorphism; SNV = single-nucleotide variation; WES = whole-exome sequencing.From the
Glycophorin hybrids such as GP.Mur are common in Southeast Asians. In Taiwan, clinically significant alloantibodies to the GP.Mur phenotype are the most important issue in blood banks. A large-scale screening of glycophorin hybrids in the Taiwanese population is urgently needed to ensure transfusion safety. Four clones of human hybridomas that secrete anti-Mia, anti-MUT, and anti-Mur were established by fusing human B-lymphocytes and myeloma cells (JMS-3). The specificity of each monoclonal antibody (MoAb) was characterized. Three MoAbs were applied on an Automated Pretransfusion Blood Testing Analyzer (PK7300/PK7400) for donor screening. Genotyping was performed to determine the detailed subgrouping of glycophorin hybrids. Four MoAbs are IgM antibodies. Anti-Mia (377T) binds to 46DXHKRDTYA54, 48HKRDTYAAHT57 peptides, and anti-Mia (367T) binds to 43QTNDXHKRD51 peptides (X indicates T, M, or K). Anti-Mur is reactive with 49KRDTYPAHTA58 peptides. Anti-MUT is reactive with 47KHKRDTYA54. A total of 78,327 donors were screened using three MoAbs, and 3690 (4.71%) were GP.Mur, 20 (0.025%) were GP.Hut, and 18 (0.022%) were GP.Vw. When the Mia antigen was introduced as routine screening, the frequency of Mi(a+) among blood donors in Taiwan was 4.66% (67,348/1,444,541). Mia antigen was implemented as a routine blood testing, and the results were labeled on all red blood cell (RBC) units.
BACKGROUND MNS is one of the highly polymorphic blood groups comprising many antigens generated by genomic recombination among the GYPA, GYPB, and GYPE genes as well as by single‐nucleotide changes. We report a patient with red blood cell (RBC) antibody against an unknown low‐frequency antigen, tentatively named SUMI, and investigated its carrier molecule and causal gene. STUDY DESIGN AND METHODS Standard serologic tests, including enzyme tests, were performed. Monoclonal anti‐SUMI–producing cells (HIRO‐305) were established by transformation and hybridization methods using lymphocytes from a donor having anti‐SUMI. SUMI+ RBCs were examined by immunocomplex capture fluorescence analysis (ICFA) using HIRO‐305 and murine monoclonal antibodies against RBC membrane proteins carrying blood group antigens. Genomic DNA was extracted from whole blood, and the GYPA gene was analyzed by polymerase chain reactions and Sanger sequencing. RESULTS Serologic screening revealed that 23 of the 541,522 individuals (0.0042%) were SUMI+, whereas 1351 of the 10,392 individuals (13.0%) had alloanti‐SUMI. SUMI antigen was sensitive to ficin, trypsin, pronase, and neuraminidase, but resistant to α‐chymotrypsin and sulfydryl‐reducing agents. ICFA revealed that the SUMI antigen was carried on glycophorin A (GPA). According to Sanger sequencing and cloning, the SUMI+ individuals had a GYPA*M allele with c.91A>C (p.Thr31Pro), which may abolish the O‐glycan attachment site. CONCLUSIONS The new low‐frequency antigen SUMI is carried on GPA encoded by the GYPA*M allele with c.91A>C (p.Thr31Pro). Neuraminidase sensitivity suggests that glycophorin around Pro31 are involved in the SUMI determinant.
Background and Objectives: Antigens of the MNS blood group system are expressed on the red blood cell (RBC) membrane on glycophorin A (GPA) and glycophorin B (GPB) or on hybrid molecules of GPA and GPB. This study investigated the distribution of glycophorin variants and alloantibodies against Hil and MINY among Japanese individuals.Methods: Mi(a+) or Hil+ RBCs were screened using an automated blood grouping machine (PK7300) with monoclonal anti-Mi a or polyclonal anti-Hil. Glycophorin variants were defined by serology with monoclonal antibodies against Mi a , Vw, MUT and Mur, and polyclonal antibodies against Hil, MINY and Hop + Nob (KIPP). The glycophorin variants were further confirmed by immunoblotting and Sanger sequencing. Alloanti-Hil and alloanti-MINY in the plasma were screened using GP.Hil RBCs in an antiglobulin test. The specificity of anti-Hil or anti-MINY was assessed using GP.Hil (Hil+MINY+) and GP.JL (HilMINY+) RBCs.
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