30. Transfection Results (B transferase Codon 268)

 

The original B transferase construct possessed A and expressed B antigens. In the in vitro enzymatic assays, weak activity of A transferase was also detected as previously reported (Greenwell et al., 1986). When it was replaced with smaller G, the construct expressed both A and B antigens. When it was replaced with slightly larger S or C, the constructs still exhibited strong B antigen expression. When it was replaced with larger N or T, the constructs exhibited decreased B antigen expression. When the N and D constructs were compared with the glutamine (Q) and glutamic acid (E) constructs, the expression of B antigen was stronger with the N and D constructs than the Q and E constructs. Similarly, when the N construct was compared with the D construct or when the Q construct was compared with the E construct, the expression of the B antigen was stronger with the N construct than with the D construct and also stronger with the Q construct than with the E construct. Taken together, it was concluded that the size and charge of the amino acid residue at codon 268 was crucial in determining the activity and specificity of the glycosyltransferases. Because the results differed between the constructs with the A transferase backbone and those with the B transferase backbone, it was also shown that not only codon 268, but also amino acid substitutions at other 3 locations, are important, with codon 266 most likely being of primary importance.

31. Nucleotide-Sugar Specificity (B Transferase Codons 266-268)

01. ABO Blood Group System

Yamamoto, F., and McNeill, P.D. (1996). Amino acid residue at codon 268 determines both activity and nucleotide-sugar donor substrate specificity of human histo-blood group A and B transferases: In vitro mutagenesis study. J Biol Chem 271, 10515-10520. (http://www.jbc.org/cgi/content/full/271/18/10515)


Keywords

Histo-blood group ABO system, blood group ABO system, ABO system, AB0 system, ABO blood groups, AB0 blood groups, ABO blood types, AB0 blood types, ABO genetic locus, ABO genes, ABO, AB0, A glycosyltransferases, B glycosyltransferases, glycosyltransferases, A transferase, B transferase, cell surface antigens, carbohydrate antigens, oligosaccharide antigens, oligosaccharides, complex carbohydrate antigens, complex carbohydrates, A antigen, B antigen, H antigen, red blood cell antigens, A/B antigens, ABH antigens, glycolipid, glycosphingolipids, glycoproteins, oligo sugars, red blood cells, RBC, blood transfusion, transfusion medicine, cell/tissue/organ transplantation, transplantation medicine, immunohematology, immunohaematology, immuno-hematology, immunology, ABO genotyping, forensic sciences, legal medicine, human genetics, population genetics, evolution, enzymology, glycobiology, glycosciences, human genes, primate genes, mouse gene, pig genes, alpha 1,3-Gal(NAc) transferases, a1,3-galactosyl transferase, a1,3-GalNAc transferase, structural basis, molecular genetic basis of ABO, ABO polymorphism, single nucleotide polymorphism, SNP, A, B, AB, O, A2, A3, Ax, B3, alleles, weak subgroups, homo sapiens, pig AO genes, cis-AB, B(A), mouse cis-AB gene, ABO genotype, ABO phenotype, DNA methylation, transcription, alternative splicing, Golgi apparatus, transferase chimeras, GBGT1, GGTA1, A3GALT2, monoclonal antibody, sera, plant lectins, Fumi-ichiro Yamamoto, Fumiichiro Yamamoto, F. Yamamoto, Landsteiner, enzyme, kinetics, sugar specificity, acceptor substrate specificity, acceptors, donors, sugars, nucleotide-sugars, genetic engineering, differential susceptibility to infectious diseases, differential cancer susceptibility, alterations in glycosylation in cancer, pancreatic cancer, diets, Peter D'Adamo, Blood type diets, neurobiology, Masahiko Nomi, personality, Burnham Institute, Burnham Institute for Medical Research, Biomembrane Institute, IMPPC, IMPPC Institute of Predictive and Personalized Medicine of Cancer, Institut de Medicina Predictiva i Personalitzada del Càncer,  AABB, ISBT, dbRBC - Blood Group Antigen Gene Mutation Database

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