We found a match
Your institution may have access to this item. Find your institution then sign in to continue.
- Title
The p. R168 Q mutation is associated with the B<sub>w</sub> phenotype and a predicted decrease in the stability of the resulting ABO glycosyltransferase.
- Authors
Lee, Seung Yeob; Ihm, Chunhwa; Shin, Dong‐Jun; Lee, Ho‐Jin; Yazer, Mark Harris; Kim, Seung Yeon; Shin, Myung Geun; Shin, Jong Hee; Suh, Soon Pal; Ryang, Dong Wook; Cho, Duck
- Abstract
Background Mutation of ABO glycosyltransferase ( GT) can cause protein stability changes that can result in a weak ABO phenotype. To explain the Bw phenotype of a novel ABO* Bw allele, a protein stability of the mutant GT, which enhances the information of the three-dimensional (3 D) structural analysis, was calculated. Study Design and Methods ABO serology and genotyping were performed on a neonate and her five family members. A 3 D structural analysis of the wild-type GTB and enzymes with a variety of mutations at Residue 168, along with predicted protein stability changes (ΔΔ G) and flow cytometric analysis of ABO antigen expression on He La cells transfected with plasmids containing R168 Q, R168 L, and R168 P mutants was also performed. Results A novel ABO* Bw allele (c.503 G> A, p. R168 Q) was discovered. The structural analysis of 3 D homology modeling predicted reduced protein stability of the mutant GTB, and the ΔΔ G values, which inversely correlated with the mean relative fluorescence intensity of ABO antigen expression, quantitatively explained the reduced ABO antigen expression. Conclusions The predicted protein stability change of a mutant GT enzyme might be a useful and convenient approach to objectively and quantitatively explain the reduced ABO antigen expression.
- Subjects
GENETIC mutation; GLYCOSYLTRANSFERASES; ABO blood group system; PROTEIN stability; MUTANT proteins; ALLELES
- Publication
Transfusion, 2014, Vol 54, Issue 5, p1298
- ISSN
0041-1132
- Publication type
Article
- DOI
10.1111/trf.12461