Identification of a novel T421C mutation of α-1,3-N-acetylgalactosaminyltransferase allele responsible for an A variant.
- Author:
Manni WANG
1
;
Liping CHEN
;
Dazhou WU
;
Qinqin ZUO
;
Shihui YE
;
Hua XU
Author Information
- Publication Type:Case Reports
- MeSH: ABO Blood-Group System; genetics; Adult; Alleles; Female; Humans; Mutation; N-Acetylgalactosaminyltransferases; genetics
- From: Chinese Journal of Medical Genetics 2015;32(1):105-108
- CountryChina
- Language:Chinese
-
Abstract:
OBJECTIVETo investigate the molecular basis of an individual featuring weak A phenotype of ABO blood group system.
METHODSSerologic investigations, serum transferases activity assay and absorption-elution test were carried out to identify the ABO blood group. The 7 exons and flanking introns of ABO glycosyltransferase gene were amplified with polymerase chain reaction (PCR). The products were sequenced bidirectinally following enzyme digestion. Haplotypes of exons 6 and 7 of the ABO gene were analyzed.
RESULTSA weak A antigen was identified on red blood cells of the proband. Eight heterozygous sites in exons 6 and 7 (261delG 297A/G, 421C/T, 467C/T, 646T/A, 681G/A, 771C/T, 829G/A) of the ABO gene were identified. Based on haplotype analysis, one allele was determined as O02, while a novel mutation 421T>C was identified in another allele, which resulted in the amino acid change Ser141Pro of the A glycosyltransferase.
CONCLUSIONAbove results suggested that amino acid substitutions resulted from a novel mutation 421T>C of the ABO gene may decrease the enzymatic activity and result in the weak A phenotype.
