DCS‐1, DCS‐2, and DFV share amino acid substitutions at the extracellular RhD protein vestibule

  title={DCS‐1, DCS‐2, and DFV share amino acid substitutions at the extracellular RhD protein vestibule},
  author={Willy Albert Flegel and Inge von Zabern and Andrea Doescher and Franz Friedrich Wagner and Jindři{\vs}ka Vytiskov{\'a} and Martin P{\'i}{\vs}acka},
BACKGROUND: RhD and RhCE are structurally related to ammonium transporter proteins, yet their physiologic function remains unclear. Recent three‐dimensional homology modeling with Escherichia coli AmtB as a template defined a putative transmembraneous channel. Three RhD variants with amino acid substitutions located at the extracellular channel aperture are described. 

Full‐length nucleotide sequence of ERMAP alleles encoding Scianna (SC) antigens

Scianna (SC) blood group system comprises two antithetical antigens, Sc1 and Sc2, and five additional antigens. The antigens reside on a glycoprotein encoded by the erythroblast membrane–associated

D variants at the RhD vestibule in the weak D type 4 and Eurasian D clusters

One branch of the RHD phylogenetic tree is represented by the weak D type 4 cluster of alleles with F223V as the primordial amino acid substitution with a large number of further substitutions causing D variants located at the extracellular RhD protein vestibule.

Insights into anti‐D formation in carriers of RhD variants through studies of 3D intraprotein interactions

Many RhD variants associated with anti‐D formation (partial D) in carriers exposed to the conventional D antigen carry mutations affecting extracellular loop residues. Surprisingly, some carry

The DAU cluster: a comparative analysis of 18 RHD alleles, some forming partial D antigens

The DaU cluster of RHD alleles is characterized by the single‐nucleotide change producing the p.Thr379Met amino acid substitution and has been postulated to be the primordial allele, from which all other alleles of the DAU cluster have eventually evolved.

Molecular genetics and clinical applications for RH.

  • W. Flegel
  • Biology, Medicine
    Transfusion and apheresis science : official journal of the World Apheresis Association : official journal of the European Society for Haemapheresis
  • 2011

Alloimmunization risk associated with amino acid 223 substitution in the RhD protein: analysis in the light of molecular modeling

A three‐dimensional (3D) structural model is built to investigate the consequences of substitutions of Amino Acid 223 involved in a large number of D variants.

Genetic variation of the whole ICAM4 gene in Caucasians and African Americans

Landsteiner‐Wiener (LW) is the human blood group system Number 16, which comprises two antithetical antigens, LWa and LWb and the high‐prevalence antigen LWab. LW is encoded by the intracellular

D category IV: a group of clinically relevant and phylogenetically diverse partial D

The D typing strategies in several European countries protect carriers of D category VI (DVI) from anti‐D immunization but not carriers of other partial D. Besides DVI, one of the clinically most

Molecular analysis of inactive and active RHD alleles in native Congolese cohorts

This study identified inactive and active RHD alleles at the molecular level in Congolese cohorts and confirmed the importance of knowing the carrier and removal status of these alleles in the context of RHD infection.

RhCE protein variants in Southwestern Germany detected by serologic routine testing

The molecular background of variant RhCE antigens identified by standard serologic routine testing in German blood donors and patients was determined.



In‐frame triplet deletions in RHD alter the D antigen phenotype

BACKGROUND: The deletion of three adjacent nucleotides in an exon may cause the lack of a single amino acid, while the protein sequence remains otherwise unchanged. Only one such in‐frame deletion is

A DV‐like phenotype is obliteratedby A226P in the partial D DBS

A proline at position 226 in RHCE encodes the antigen E, which is typical of the prevalent RHD allele and observed in all RHCE alleles encoding the antigen e.

Hydrophobic cluster analysis and modeling of the human Rh protein three-dimensional structures.

  • I. CallebautF. Dulin J. Cartron
  • Biology, Chemistry
    Transfusion clinique et biologique : journal de la Societe francaise de transfusion sanguine
  • 2006

The human Rhesus-associated RhAG protein and a kidney homologue promote ammonium transport in yeast

It is shown here that RhAG and also RhGK, a new human homologue expressed in kidney cells only, function as ammonium transport proteins when expressed in yeast, and specifically complement the growth defect of a yeast mutant deficient in ammonium uptake.

Modelling the human rhesus proteins: implications for structure and function

The mammalian rhesus (Rh) proteins that carry the Rh blood group antigens of red blood cells are related to the ammonium channel (Amt) proteins found in both pro‐ and eukaryotes. However, despite

The RHCE allele ceRT: D epitope 6 expression does not require D‐specific amino acids

BACKGROUND:  False‐positive D typing in patients may lead to anti‐D immunization caused by D+ transfusions or by omission of anti‐D prophylaxis. Known causes of such errors are RhCE variants carrying

Mechanism of Genetic Complementation of Ammonium Transport in Yeast by Human Erythrocyte Rh-associated Glycoprotein*

Previous observations of RhAG-mediated transport in yeast are clarified and expanded and the hypothesis that ammonium transport is coupled to the H+ gradient and that RhAG functions as a NH4+/H+ exchanger is supported.

Transcript analysis of D category phenotypes predicts hybrid Rh D-CE-D proteins associated with alteration of D epitopes.

The RH blood group locus from RhD-positive donors is composed of two closely related genes, RHCE and RHD, encoding the Cc/Ee and D antigens, respectively. The major Rh antigen, D, is serologically

Transport characteristics of mammalian Rh and Rh glycoproteins expressed in heterologous systems.

  • C. WesthoffD. Wylie
  • Biology
    Transfusion clinique et biologique : journal de la Societe francaise de transfusion sanguine
  • 2006

Human Rhesus-associated glycoprotein mediates facilitated transport of NH(3) into red blood cells.

The results show that RhAG facilitates CH(3)NH(2)/NH( 3) movement across the RBC membrane and represents a potential example of a gas channel in mammalian cells.