scholarly journals Genomic organization of the glycoprotein D gene: Duffy blood group Fya/Fyb alloantigen system is associated with a polymorphism at the 44- amino acid residue

Blood ◽  
1995 ◽  
Vol 85 (3) ◽  
pp. 622-626 ◽  
Author(s):  
S Iwamoto ◽  
T Omi ◽  
E Kajii ◽  
S Ikemoto
Keyword(s):  
Amino Acid ◽  
Blood Group ◽  
Direct Repeat ◽  
Base Change ◽  
Repeat Sequence ◽  
Blood Group System ◽  
Glycoprotein D ◽  
Flanking Sequence ◽  
Duffy Blood Group ◽  
Flanking Region

The Duffy blood group antigen has been characterized by its roles on red blood cells: as a receptor for the malarial parasites and as a promiscuous receptor for chemokine superfamily. Recently, the Duffy blood group associated glycoprotein D (gpFy) cDNA has been cloned (Chaudhuri et al: Proc Natl Acad Sci USA 90:10793, 1993). In this report we describe the organization of genomic DNA coding for the gpFy and elucidate the molecular nature of Fya/b polymorphisms. By a Southern blotting analysis probed with gpFy cDNA, gpFy gene was shown to be composed of three DNA fragments; 1.1-kb Sac I, 1.9-kb EcoRI, and their intervening 47-bp fragments. We cloned the 1.1-kb Sac I and 1.9- kb EcoRI fragments by inverted polymerase chain reaction (IPCR) procedure. The promoter region of the gpFy gene was cloned by IPCR of 1.1-kb Sac I fragment and the 3′ flanking sequence was cloned by IPCR of 1.9 kb EcoRI fragment. The both IPCR products contained on both side the known gpFy cDNA sequence without introns, as expected. Although no TATA or CCAAT boxes are present in the promoter sequence, several transcription factor binding site motifs are contained, including AP-1, HNF-5, TCF-1, ApoE B2, W-element, H-APF-1, and Sp-1. The 3′ flanking region has two additional polyadenylation signals, other than that used in the cDNA, and also has an indirect and a direct repeat sequence clustered with the 5′ flanking region. These facts indicate a possibility that the gpFy gene has been evolved by multiple retrotransposition events. By comparing the coding area of the gpFy gene in 28 Duffy-positive individuals, we elucidated that one base change that results in an amino acid substitution [GA-T(Asp44)-- >GGT(Gly)] is in accordance with the Fya/Fyb polymorphism. This fact proves that the gpFy cDNA and its gene described in this report encode the Duffy blood group system.

scholarly journals Protein-sequence studies on Rh-related polypeptides suggest the presence of at least two groups of proteins which associate in the human red-cell membrane

1988 ◽  
Vol 256 (3) ◽  
pp. 1043-1046 ◽  
Author(s):  
N D Avent ◽  
K Ridgwell ◽  
W J Mawby ◽  
M J Tanner ◽  
D J Anstee ◽  
...  
Keyword(s):  
Amino Acid ◽  
Blood Group ◽  
Protein Sequence ◽  
Amino Acid Sequences ◽  
Red Cells ◽  
British Library ◽  
Blood Group System ◽  
Terminal Amino Acid ◽  
Red Cell Membrane ◽  
Terminal Amino

The Rh D blood-group antigen forms part of a complex, involving several other polypeptides, that is deficient in the red cells of individuals who lack all the antigens of the Rh blood-group system (Rhnull red cells). These include components recognized by anti-(Rh D) antibodies and the murine monoclonal antibodies R6A and BRIC 125. We have carried out protein-sequence studies on the components immunoprecipitated by these antibodies. Anti-(Rh D) antibodies immunoprecipitate an Mr-30,000-32,000 polypeptide (the D30 polypeptide) and an Mr-45,000-100,000 glycoprotein (D50 polypeptide). Antibody R6A immunoprecipitates two glycoproteins of Mr 31,000-34,000 (R6A32 polypeptide) and Mr 35,000-52,000 (R6A45 polypeptide). The D30 and R6A32 polypeptides were found to have the same N-terminal amino acid sequences, showing that they are closely related proteins. The D50 polypeptide and the R6A45 polypeptide also had indistinguishable N-terminal amino acid sequences that differed from that of the D30 and R6A32 polypeptides. The putative N-terminal membrane-spanning segments of the two groups of proteins showed homology in their amino acid sequence, which may account for the association of each of the pairs of proteins during co-precipitation by the antibodies. Supplementary data related to the protein sequence have been deposited as Supplementary Publication SUP 50417 (6 pages) at the British Library Document Supply Centre, Boston Spa, Wetherby, West Yorkshire LS23 7BQ, U.K., from whom copies can be obtained on the terms indicated in Biochem. J. (1988) 249, 5.

Duffy blood group system

2004 ◽  
pp. 278-289 ◽  
Author(s):  
Marion E. Reid ◽  
Christine Lomas-Francis
Keyword(s):  
Blood Group ◽  
Blood Group System ◽  
Group System ◽  
Duffy Blood Group

Duffy blood group system genotyping in an urban Tunisian population

2008 ◽  
Vol 35 (4) ◽  
pp. 406-415 ◽  
Author(s):  
M. H. Sellami ◽  
H. Kaabi ◽  
B. Midouni ◽  
A. Dridi ◽  
N. Mojaat ◽  
...  
Keyword(s):  
Blood Group ◽  
Tunisian Population ◽  
Blood Group System ◽  
Group System ◽  
Duffy Blood Group

scholarly journals Duffy blood group system and the malaria adaptation process in humans

2011 ◽  
Vol 33 (1) ◽  
pp. 55-64
Author(s):  
Gledson Barbosa de Carvalho ◽  
Glauber Barbosa de Carvalho
Keyword(s):  
Blood Group ◽  
Blood Group System ◽  
Adaptation Process ◽  
Group System ◽  
Duffy Blood Group

The Duffy blood group system in the Tunisian population

2015 ◽  
Vol 22 (2) ◽  
pp. 76-79 ◽  
Author(s):  
M. Ouchari ◽  
H. Romdhane ◽  
T. Chakroun ◽  
S. Abdelkefi ◽  
I. Jarrey ◽  
...  
Keyword(s):  
Blood Group ◽  
Tunisian Population ◽  
Blood Group System ◽  
Group System ◽  
Duffy Blood Group

The Duffy Blood Group System in Caucasians.

Vox Sanguinis ◽  
1972 ◽  
Vol 23 (6) ◽  
pp. 523-527 ◽  
Author(s):  
Marion Lewis ◽  
H. Kaita ◽  
B. Chown
Keyword(s):  
Blood Group ◽  
Blood Group System ◽  
Group System ◽  
Duffy Blood Group

The Presence of FYAnull Alele of Duffy Blood Group System in Blood Donors and Individuals from a Malarial Endemic Region of Brazil.

Blood ◽  
2004 ◽  
Vol 104 (11) ◽  
pp. 2714-2714 ◽  
Author(s):  
Dante M. Langhi ◽  
Sergio R. Albuquerque ◽  
Dimas T. Covas ◽  
Clovis A. Perez ◽  
Jose O. Bordin
Keyword(s):  
Sequence Analysis ◽  
Blood Group ◽  
Blood Donors ◽  
Single Point Mutation ◽  
Binding Motif ◽  
Blood Group System ◽  
Endemic Region ◽  
Group System ◽  
Duffy Blood Group ◽  
Gata Box

Abstract BACKGROUND: Malaria is a virulent disease caused by the Plasmodium parasite. Innate resistance to malaria infections in humans is conferred by various blood group polymorphisms. The Duffy blood group system consists of Fya and Fyb antigens which are encoded by codominant alleles FYA and FYB. Four phenotypes are defined: Fy(a+b+), Fy(a+b−), Fy(a−b+) and Fy(a−b−). Erythrocytes of Duffy-negative individuals are resistant to invasion by P. vivax. In Blacks the Fy(a−b−) phenotype is associated with a single point mutation (-33T-C) in the GATA-1 binding motif for the erythroid promoter of FYB. STUDY DESIGN AND METHODS: We investigated the phenotypes and the genotypes of Duffy blood group system of 250 individuals living in a malarial endemic region (MER) in the state of Amazon (Brazil), and of 199 blood donors (BD) from a non-endemic region. The phenotyping was done by agglutination gel tests (DiaMed-Latino América) using anti-Fya and anti-Fyb reagents. The molecular analysis for FYA, FYB, FYBES (GATA box mutation nt -33T-C), and FYBWeak (mutations 265 C-T, and 298 G-A) alleles, were performed by PCR-RFLP. The PCR products were digested by Ban I for FYA and FYB identifications; by Sty I for GATA box mutation; Acy I and Mwo I for 265 C-T and 298 G-A mutations, respectively. Some samples that showed discrepancy between the phenotype and genotype results were examined by sequence analysis using the ABI PrismâBig Dyeä Terminator Cycle Sequencing Ready Reaction Kit” (Perkin Elmer), and the interpretation by the software ABI PRISMä 377 DNA Sequencer”, 3.3 version (Perkin Elmer). RESULTS: We found that 34/250 (13.6%) of 250 persons living in the MER and 37/199 (18.6%) of BD had phenotype and genotype discrepant results [Fy(a+b−) FYA/FYB]. In addition, we found that 16/34 (47%) of people living in the MER, and 4/37 (10.8%) of BD did not present the -33T-C mutation, the 265 C-T, or the 298 G-A mutations. The sequence analysis of 2 samples from persons from MER indicated the presence of -33T-C mutation in the FYA allele in one individual (1 FYA/FYB and W/M; FYA/FYB and M/M). Additionally, we detected that 18/34 (53%) of people living in the MER, and 33/37 (89.2%) of BD presented the -33T-C mutation. The sequence analysis of 5 samples indicated the presence of -33T-C mutation in the FYA allele in 4 cases [2 persons from MER and 2 from BD (FYA/FYB e M/M)]. CONCLUSION: Recently the mutation responsible for erythrocyte Duffy antigen-negativity [Fy(a−b−)] was demonstrated in FYA allele in a malarial endemic region of Papua New Guinea. The present data demonstrated the presence of the FYAnull allele not only in persons living in a malarial endemic region but also in Brazilian blood donors from non-endemic areas. In contrast with that which happens with the FYB allele, our results indicated that the presence of the -33T-C mutation in the FYA allele does not abolish the expression of the Fya antigen in the erythrocyte.

Sign in / Sign up

Export Citation Format

Share Document