Compound heterozygosity of two novel RHAG alleles leads to a considerable disruption of the Rh complex

Transfusion. 2016 Apr;56(4):950-5. doi: 10.1111/trf.13476.

Abstract

Background: The Rhesus (Rh) complex consists of a core comprising the Rh proteins (RhD/RhCE) and the Rh-associated glycoprotein (RhAG) with accessory chains (GPB, LW, CD47). Molecular defects of the RHAG gene may cause a regulator Rhnull phenotype without Rh antigen expression or a Rhmod phenotype with decreased Rh antigen expression.

Study design and methods: Blood samples of a donor with strongly diminished Rh antigens and five family members were analyzed by serological phenotyping, flow cytometry, molecular testing, and gene expression analysis of Rh complex candidate genes.

Results: RHAG sequencing identified a missense mutation, c.241G>C (p.Gly81Arg) and a splice site mutation, c.640 + 3del14, among the cohort. Compound heterozygosity of these novel alleles identified in the propositus and two siblings gave rise to a strongly diminished expression of RhAG, Rh, and CD47 antigens on the RBC surface.

Conclusion: The Rhmod phenotype was caused by a novel RHAG splice site mutation in association with a non-functional allele. The primary depression of RhAG is most likely due to posttranslational events that affect the interaction and processing of the RhAG glycoprotein and gave rise to a secondary depression of RhD, RhCE, and CD47, the major members of the Rh complex.

Publication types

  • Case Reports

MeSH terms

  • Alleles
  • Amino Acid Sequence
  • Base Sequence
  • Blood Proteins / genetics*
  • Blood Proteins / metabolism
  • Erythrocyte Membrane / metabolism
  • Heterozygote
  • Humans
  • Membrane Glycoproteins / genetics*
  • Membrane Glycoproteins / metabolism
  • Molecular Sequence Data
  • Rh-Hr Blood-Group System / genetics*
  • Rh-Hr Blood-Group System / metabolism
  • Siblings

Substances

  • Blood Proteins
  • Membrane Glycoproteins
  • RHAG protein, human
  • Rh-Hr Blood-Group System