S12.12N-glycanase,O-glycanase and endoglycosidase-f treatment of purified tryptic peptide of the duffy blood group antigen: evidence for N-glycosylation

1993 ◽  
Vol 10 (4) ◽  
pp. 298-299
Author(s):  
K. Wasniowska ◽  
P. Eichenberger ◽  
F. Kugele ◽  
T. Hadley
Keyword(s):  
Blood Group ◽  
Tryptic Peptide ◽  
Blood Group Antigen ◽  
Duffy Blood Group

scholarly journals Role ofPlasmodium vivaxDuffy-binding protein 1 in invasion of Duffy-null Africans

2016 ◽  
Vol 113 (22) ◽  
pp. 6271-6276 ◽  
Author(s):  
Karthigayan Gunalan ◽  
Eugenia Lo ◽  
Jessica B. Hostetler ◽  
Delenasaw Yewhalaw ◽  
Jianbing Mu ◽  
...  
Keyword(s):  
Blood Group ◽  
Malaria Parasite ◽  
Binding Protein ◽  
Squirrel Monkeys ◽  
Blood Group Antigen ◽  
Affinity Binding ◽  
Duffy Binding Protein ◽  
Duffy Blood Group ◽  
Duffy Antigen ◽  
The World

The ability of the malaria parasitePlasmodium vivaxto invade erythrocytes is dependent on the expression of the Duffy blood group antigen on erythrocytes. Consequently, Africans who are null for the Duffy antigen are not susceptible toP. vivaxinfections. Recently,P. vivaxinfections in Duffy-null Africans have been documented, raising the possibility thatP. vivax, a virulent pathogen in other parts of the world, may expand malarial disease in Africa.P. vivaxbinds the Duffy blood group antigen through its Duffy-binding protein 1 (DBP1). To determine if mutations in DBP1 resulted in the ability ofP. vivaxto bind Duffy-null erythrocytes, we analyzedP. vivaxparasites obtained from two Duffy-null individuals living in Ethiopia where Duffy-null and -positive Africans live side-by-side. We determined that, although the DBP1s from these parasites contained unique sequences, they failed to bind Duffy-null erythrocytes, indicating that mutations in DBP1 did not account for the ability ofP. vivaxto infect Duffy-null Africans. However, an unusual DNA expansion of DBP1 (three and eight copies) in the two Duffy-nullP. vivaxinfections suggests that an expansion of DBP1 may have been selected to allow low-affinity binding to another receptor on Duffy-null erythrocytes. Indeed, we show that Salvador (Sal) IP. vivaxinfects Squirrel monkeys independently of DBP1 binding to Squirrel monkey erythrocytes. We conclude thatP. vivaxSal I and perhapsP. vivaxin Duffy-null patients may have adapted to use new ligand–receptor pairs for invasion.

The Duffy Blood Group Antigen: An Update

1994 ◽  
Vol 8 (4) ◽  
pp. 281-288 ◽  
Author(s):  
Kazimiera Wasniowska ◽  
Terence J. Hadley
Keyword(s):  
Blood Group ◽  
Blood Group Antigen ◽  
Duffy Blood Group

scholarly journals Distribution of ABO, Rh, MNSs, Kell and Duffy blood-group antigens in population of Vojvodina

2003 ◽  
Vol 56 (3-4) ◽  
pp. 173-177
Author(s):  
Svetlana Vojvodic
Keyword(s):  
Blood Group ◽  
American Indians ◽  
Significance Test ◽  
Blood Groups ◽  
Blood Group Antigen ◽  
Blood Group Antigens ◽  
Test Results ◽  
Australian Aborigines ◽  
Duffy Blood Group ◽  
Genotype Frequencies

Introduction Analysis of erythrocyte blood group antigen polymorphisms and genetic variability in population of Vojvodina was performed by investigating gene and genotype frequencies which determine antigens of ABO, Rh, MNSs, Kell and Duffy blood-group systems. Material and methods We investigated 350 unrelated persons from Vojvodina in regard to appurtenance of ABO, Rh, MNSs, Kell and Duffy blood-group systems. We calculated gene, genotype, phenotype frequencies and proportion significance test. Results and discussion Results of investigation revealed that gene and genotype frequencies of investigated blood-group systems are similar to corresponding data for majority of European populations, while statistically significant differences were established in inhabitants of geographically distant regions. Values of proportion significance test revealed statistically significant differences of genotype frequencies for ABO and MNSs blood-group antigens in populations of: Australian Aborigines, Chinese population, Arabians, Blacks, Eskimos, American Indians (Navaho and Pueblo) and population of Papua New Guinea. Statistically significant differences of genotype frequencies were established in inhabitants of narrow geographical areas of Europe such as: Finland, Germany, Sweden, Albania, England and Netherlands. Conclusion Our results point to the fact that erythrocyte blood-groups have different frequencies in some parts of the world, and that there are great differences in frequencies of some blood-groups among inhabitants of various continents and races. Genetical peculiarity of the population of Vojvodina points to the fact that differences in blood-group frequencies are also present among inhabitants of narrow geographical areas.

scholarly journals The domain on the Duffy blood group antigen for binding Plasmodium vivax and P. knowlesi malarial parasites to erythrocytes.

1996 ◽  
Vol 184 (4) ◽  
pp. 1531-1536 ◽  
Author(s):  
C E Chitnis ◽  
A Chaudhuri ◽  
R Horuk ◽  
A O Pogo ◽  
L H Miller
Keyword(s):  
Amino Acid ◽  
Plasmodium Vivax ◽  
Blood Group ◽  
Blood Group Antigen ◽  
Human Erythrocytes ◽  
Cos Cells ◽  
Duffy Blood Group ◽  
Duffy Antigen ◽  
Extracellular Region ◽  
Region Ii

Plasmodium vivax and the related simian malarial parasite P. knowlesi use the Duffy blood group antigen as a receptor to invade human erythrocytes and region II of the parasite ligands for binding to this erythrocyte receptor. Here, we identify the peptide within the Duffy blood group antigen of human and rhesus erythrocytes to which the P. vivax and P. knowlesi ligands bind. Peptides from the NH2-terminal extracellular region of the Duffy antigen were tested for their ability to block the binding of erythrocytes to transfected Cos cells expressing on their surface region II of the Duffy-binding ligands. The binding site on the human Duffy antigen used by both the P. vivax and P. knowlesi ligands maps to a 35-amino acid region. A 34-amino acid peptide from the equivalent region of the rhesus Duffy antigen blocked the binding of P. vivax to human erythrocytes, although the P. vivax ligand expressed on Cos cells does not bind rhesus erythrocytes. The binding of the rhesus peptide, but not the rhesus erythrocyte, to the P. vivax ligand was explained by interference of carbohydrate with the binding process. Rhesus erythrocytes, treated with N-glycanase, bound specifically to P. vivax region II. Thus, the interaction of P. vivax ligand with human and rhesus erythrocytes appears to be mediated by a peptide-peptide interaction. Glycosylation of the rhesus Duffy antigen appears to block binding of the P. vivax ligand to rhesus erythrocytes.

Purification of a 28 kD Non-Aggregating Tryptic Peptide of the Duffy Blood Group Protein

1993 ◽  
Vol 192 (2) ◽  
pp. 366-372 ◽  
Author(s):  
K. Wasniowska ◽  
P. Eichenberger ◽  
F. Kugele ◽  
T.J. Hadley
Keyword(s):  
Blood Group ◽  
Tryptic Peptide ◽  
Duffy Blood Group ◽  
Group Protein
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