Protein stability changes of the novel p.Arg180Cys mutant A glycosyltransferase resulted in a weak A phenotype

• Published in: Vox sanguinis Vol. 111; no. 4; pp. 441 - 444
• Main Authors: Lee, H.-S., Choi, K.-M., Won, E. J., Thi Phan, M.-T., Lee, S. Y., Shin, D.-J., Chun, S., Park, G., Kim, S.-K., Lee, K.-B., Lee, H.-J., Cho, D.
• Format: Journal Article
• Language: English
• Published: England Blackwell Publishing Ltd 01.11.2016; S. Karger AG
• Subjects: ABO Blood-Group System - genetics; Adult; blood groups; Blood transfusions; Enzyme Stability; Enzymes; Female; Flow cytometry; Genetic Association Studies; genetics; Genotype & phenotype; genotyping; HeLa Cells; Humans; immunogenetics; Mutation, Missense; N-Acetylgalactosaminyltransferases - genetics; Phenotype; Proteins; RBC antigens and antibodies; Sequence Analysis, DNA; blood groups; immunogenetics; genetics; RBC antigens and antibodies; genotyping
• ISSN: 0042-9007; 1423-0410
• DOI: 10.1111/vox.12440

A novel A subgroup allele (c.538C>T p.Arg180Cys) showing weak A phenotype was found in a 30‐year‐old Korean woman with ABO discrepancy. Using 3D structural analysis, protein stability prediction and flow cytometric analysis of ABO antigen expression on HeLa cells transfected with plasmids containing the p.Arg180Cys mutant, we found that the Arg180 residue in the loop region of the A glycosyltransferases (GTA) structure plays significant role in stabilizing its closed conformation, which is required for substrate binding and catalysis study.