Duffy blood group and malaria

References

• Mollison PL, Engelfried CP, Contreras M. Blood transfusion in clinical medicine. Oxford, England: Blackwell; 1997.
   Google Scholar
• Collins A, Keast BJ, Dracopoli N, Shields DC, Morton NE. Integration of gene maps: Chromosome 1. Proc Natl Acad Sci USA 1992;89: 4598–4602.
   PubMed Web of Science ®Google Scholar
• Cutbush M, Mollison PL, Parkin DM. A new human blood group. Nature 1950;165:188–189.
   Web of Science ®Google Scholar
• Sanger R, Race RR, Jack J. The Duffy blood groups of New York negroes: The phenotype Fy(a-b-). Br J Haematol 1955;1:370–374.
   PubMed Web of Science ®Google Scholar
• Tournamille C, Colin Y, Cartron JP, Le Van Kim C. Disruption of a GATA motif in the Duffy gene promoter abolishes erythroid gene expression in Duffy-negative individuals. Nat Genet 1995;10:224–228.
   PubMed Web of Science ®Google Scholar
• Chown B, Lewis M, Kaita H. The Duffy blood group system in caucasians: Evidence for a new allele. Am J Hum Genet 1965;17:384–389.
   PubMed Web of Science ®Google Scholar
• Zimmerman PA, Woolley I, Masinde GL, Miller SM, McNamara DT, Hazlett F, et al. Emergence of FY*A null in a Plasmodium vivax-endemic region of Papua New Guinea. Proc Natl Acad Sci USA 1999;96:13973–13977.
   PubMed Web of Science ®Google Scholar
• Langhi DM, Albuquerque SR, Covas DT, Perez CA, Bordin JO. The presence of FYAnull allele of Duffy blood group system in blood donors and individuals from a malarial endemic region of Brazil [abstract]. Blood 2004;104:741a.
   Web of Science ®Google Scholar
• Miller LH, Mason Si, Dvorak JÁ, McGinniss MH, Rothman IK. Erythrocyte receptors for (Plasmodium knowlesz) malaria: Duffy blood group determinants. Science 1975;189: 561–563.
   Google Scholar
• Nichols ME, Rubinstein P, Barnwell J, Rodriguez de Cordoba S, Rosenfield RE. A new human Duffy blood group specificity defined by a murine monoclonal antibody. Immunogenetics and association with susceptibility to Plasmodium vivax. J Exp Med 1987;166:776–785.
   PubMed Web of Science ®Google Scholar
• Miller LH, Mason SJ, Clyde DF, McGinniss MH. The resistance factor to Plasmodium vivax in black individuals. The Duffy blood group genotype, FyFy. N. Engl J Med 1976;295:302–304.
   PubMed Web of Science ®Google Scholar
• Horuk R, Chitnis CE, Darbonne WC, Colby TJ, Rybicki A, Hadley TJ, Miller LH. A receptor for the malarial parasite Plasmodium vivax: The erythrocyte chemokine receptor. Science 1993;261: 1182–1184.
   PubMed Web of Science ®Google Scholar
• Ikin EW, Mourant AE, Pettenkofer HJ, Pettenkoffer JH, Blumenthal G. Discovery of the expected haemagglutinin anti-Fyb. Nature 1951;168:1077–1078.
   PubMed Web of Science ®Google Scholar
• Race RR, Sanger R. Blood Groups in Man. 6th ed. Oxford: Blackwell Scientific Publications; 1975.
   Google Scholar
• Algora M, Barbolla L, Contreras M. Naturally occurring anti-D, anti-K, anti-Fy(a), and anti-Le(ab). [Letter] Vox Sang 1991;61:141.
   PubMed Web of Science ®Google Scholar
• Rosenfield RE, Vogel P, Race RR. A new case of ant-Fya in human serum. Rev Hematol 1950;5:315–317.
   PubMedGoogle Scholar
• Pineda AA, Taswell HF, Brzica SM. Transfusion reaction. An immunologic hazard of blood transfusion. Transfusion 1978;18:1–7.
   PubMed Web of Science ®Google Scholar
• Weinstein L, Taylor ES. Hemolytic disease of the neonate secondary to anti-Fy(a). Am J Obstet Gynecol 1975; 121:643–645.
   PubMed Web of Science ®Google Scholar
• Marsh WL. Present status of the Duffy blood group system. CRC Crit Rev Clin Lab Sci 1975;5:387–412.
   PubMedGoogle Scholar
• Contreras M, Gordon H, Tidmarsh E. A proven case of maternal alloimmunization due to Duffy antigens in donor blood used for intrauterine transfusion. Br J Haematol 1983;53:355–356.
   PubMed Web of Science ®Google Scholar
• Issit PD. Applied Blood Group Serology. 3rd ed. Miami: Montgomery Scientific Publications; 1985.
   Google Scholar
• Albrey JA, Vincent EER, Hutchinson J, Marsh WL, Allen FH, Gavin J, Sanger R. A new antibody, anti-Fy3, in the Duffy blood group system. Vox Sang 1971;20: 29–35.
   PubMed Web of Science ®Google Scholar
• Behzad O, Lee CL, Gavin J, Marsh WL. A new anti-erythrocyte antibody in the Duffy system: Anti-Fy4. Vox Sang 1973;24: 337–342.
   PubMed Web of Science ®Google Scholar
• Habibi B, Perrier P, Salmon C. HD50 assay evaluation of the antigen Fy3 depression in Fyx individuals. J Immunogenet 1980;7: 191–193.
   PubMedGoogle Scholar
• Yazdanbakhsh K. Molecular mechanisms underlying defective expression of blood group antigens. [Review] Transfus Med Rev 2001;15:53–66.
   PubMed Web of Science ®Google Scholar
• Moore S, Woodrow CF, McClelland DB. Isolation of membrane components associated with human red cell antigens Rh(D), (c), (E) and Fy. Nature 1982;295:529–531.
   PubMed Web of Science ®Google Scholar
• Hadley TJ, David PH, McGinniss MH, Miller LH. Identification of an erythrocyte component carrying the Duffy blood group Fya antigen. Science 1984;223:597–599.
   PubMed Web of Science ®Google Scholar
• Chaudhuri A, Nielsen S, Elkjaer ML, Zbrzezna V, Fang G, Pogo AO. Detection of Duffy antigen in the plasma membranes and caveolae of vascular endothelial and epithelial cells of nonerythroid organs. Blood 1997;89:701–712.
   PubMed Web of Science ®Google Scholar
• Wasniowska K, Blanchard D, Janvier D, Wang ZX, Peiper SC, Hadley TJ, Lisowska E. Identification of the Fy6 epitope recognized by two monoclonal antibodies in the N-terminal extracellular portion of the Duffy antigen receptor for chemokines. Mol Immunol 1996;33: 917–923.
   PubMed Web of Science ®Google Scholar
• Neote K, Mak JY, Kolakowski LF, Schall TJ. Functional and biochemical analysis of the cloned Duffy antigen: Identity with the red blood cell chemokine receptor. Blood 1994;84:44–52.
   PubMed Web of Science ®Google Scholar
• Hadley TJ, Peiper SC. From malaria to chemokine receptor: The emerging physiologic role of the Duffy blood group antigen. [Review] Blood 1997;89:3077–3091.
   PubMed Web of Science ®Google Scholar
• Pogo AO, Chaudhuri A. The Duffy protein: A malarial and chemokine receptor. Semin Hematol 2000;37:122–129.
   PubMed Web of Science ®Google Scholar
• Mathew S, Chaudhuri A, Murty VV, Pogo AO. Confirmation of Duffy blood group antigen locus (FY) at 1q22-q23 by fluorescence in situ hybridization. Cytogenet Cell Genet 1994;67:68.
   PubMedGoogle Scholar
• Chaudhuri A, Polyakova J, Zbrzezna V, Williams K, Gulati S, Pogo AO. Cloning of glycoprotein D cDNA which encodes the major subunit of the Duffy blood group system and the receptor for the Plasmodium vivax malaria parasite. Proc Natl Acad Sci USA 1993;90:10793–10797.
   PubMed Web of Science ®Google Scholar
• Iwamoto S, Li J, Omi T, Ikemoto S, Kajii E. Identification of a novel exon and spliced form of Duffy mRNA that is the predominant transcript in both erythroid and postcapillary venule endothelium. Blood 1996;87:378–385.
   PubMed Web of Science ®Google Scholar
• Issit PD, Anstee DJ. Applied blood group serology. 4th ed. Durham: Montgomery Scientific Publications; 1998. p 1208.
   Google Scholar
• Shimizu Y, Ao H, Soemantri A, Tiwawech D, Settheetham-Ishida W, Kayame OW. Sero and molecular typing of Duffy blood group in Southeast Asians and Oceanians. Hum Biol 2000;72:511–518.
   PubMed Web of Science ®Google Scholar
• Lewis Jr, GE, Miller LH, Ibrahim L, Wong PW, McGinniss M, Ooi WL. Duffy phenotypes in Malaysian populations: Corrections of previous unusual findings. Trans R Soc Trop Med Hyg 1988;82:509–510.
   PubMed Web of Science ®Google Scholar
• Parasol N, Reid M, Rios M, Castilho L, Harari I, Kosower NS. A novel mutation in the coding sequence of the FY*B allele of the Duffy chemokine receptor gene is associated with an altered erythrocyte phenotype. Blood 1998;92:2237–2243.
   PubMed Web of Science ®Google Scholar
• Castilho L, Rios M, Pellegrino Jr., J, Saad STO, Bianco C, Reid ME. A novel point mutation in the erythrocyte Duffy protein. [Abstract] Transfusion 1999;39\(suppl. 10).
   Google Scholar
• Garraty G. Blood group antigens as tumor markers, parasitic/bacterial/viral receptors, and their association with immunologically important proteins. Immunol Invest 1995;24:213–222.
   PubMed Web of Science ®Google Scholar
• Moulds JM, Moulds JJ. Blood group associations with parasites, bacteria, and viruses. Transfus Med Rev 2000; 14:302–311.
   PubMed Web of Science ®Google Scholar
• Karlsson KA. Animal glycosphingolipids as membrane attachment sites for bacteria. Annu Rev Biochem 1989; 58:309–350.
   PubMed Web of Science ®Google Scholar
• Darbonne WC, Rice GC, Mohler MA, Apple T, Hebert CA, Valente AJ, Baken JB. Red blood cells are a sink for interleukin-8, a leukocyte chemotaxin. J Clin Invest 1991;88: 1362–1369.
   PubMed Web of Science ®Google Scholar
• Rossi D, Zlotinik A. The biology of chemokines and their receptors. Annu Rev Immunol 2000;18:217–242.
   PubMed Web of Science ®Google Scholar
• Wells TN, Proudfoot AE, Power CA. Chemokine receptor and their role in leukocyte activation. Immunol Lett 1999; 65:35–40.
   PubMed Web of Science ®Google Scholar
• Tamasauskas D, Powell V, Saksela K, Yazdanbaksh K. A homologous naturally occurring mutation in Duffy and CCR5 leading to reduced receptor expression. Blood 2001;97: 3651–3654.
   PubMed Web of Science ®Google Scholar
• Middleton J, Neil S, Wintle J, Clark-Lewis I, Moore H, Lam C, Auer M, Hub E, Rot A. Transcytosis and surface presentation of IL8 by venular endothelial cells. Cell 1997; 91:385–395.
   PubMed Web of Science ®Google Scholar
• Bates P. Chemokine receptors and HIV-1: An attractive pair? Cell 1996;86:1–3.
   PubMed Web of Science ®Google Scholar
• Lachgar A, Jaureguiberry G, Le Buenac H, Bizzini B, Zagury JF, Rappaport J, Zagury D. Binding of HIV-1 to RBCs involves the Duffy antigen receptors of Chemokines. Biomed Pharmac-other 1998;52: 436–439.
   PubMed Web of Science ®Google Scholar
• Mendis K, Sine BJ, Marchsini P. Carter R. The neglected burden of Plasmodium vivax malaria. [Review] Am J Trop Med Hyg 2001;64\(Suppl 1–2):97–106.
   PubMed Web of Science ®Google Scholar
• Miller LH, Aikawa M, Johnson JG, Shiroish T Interaction between cytochalasin B-treated malarial parasites and eryth-rocytes. Attachment and junction formation. J Exp Med 1979;149:172–184.
   PubMed Web of Science ®Google Scholar
• Barnwell JW, Nichols ME, Rubinstein P. In vitro evaluation of the role of the Duffy blood group in erythrocyte invasion by Plasmodium vivax. J Exp Med 1989;169:1795–1802.
   PubMed Web of Science ®Google Scholar
• Galinski MR, Medina C, Ingravalio P, Ingravallo P, Barnwell JW. A reticulocyte-binding protein complex of Plasmodium vivax merozoites. Cell 1992;69:1213–1226.
   PubMed Web of Science ®Google Scholar
• Hadley TJ, Miller LH, Haynes JD. Recognition of red cells by malaria parasites: The role of erythrocyte-binding proteins. Transfus Med Rev 1991;5:108–122.
   PubMedGoogle Scholar
• Wertheimer SP, Barnwell JW. Plasmodium vivax interaction with the human Duffy blood group glycoprotein: Identification of a parasite receptor-like protein. Exp Parasitol 1989;69: 340–350.
   PubMed Web of Science ®Google Scholar
• Xainli J, Adams JH, King CL. The erythrocyte binding motif of Plasmodium vivax Duffy binding protein is highly polymorphic and functionally conserved in isolates from Papua New Guinea. Mol Biochem Parasitol 2000;111: 253–260.
   PubMed Web of Science ®Google Scholar
• Chitnis CE, Miller LH. Identification of the erythrocyte binding domains of Plasmodium vivax and Plasmodium knowlesi proteins involved in erythrocyte invasion. J Exp Med 1994;180:497–506.
   PubMed Web of Science ®Google Scholar
• Su XZ, Heatwole VM, Wertheimer SP, Guinet F, Herrfeldt JA, Peterson DS, Ravetch JA, Wellems TE. The large diversity gene family var encodes proteins involved in cytoadherence and antigenic variation of Plasmodium falciparum infected erythrocytes. Cell 1995;82:89–100.
   PubMed Web of Science ®Google Scholar
• Hadley TJ, Klotz FW, Pasvol G, Haynes JD, McGinniss MH, Okubo Y, Miller LH. Falciparum malarial parasites invade erythrocytes that lack glycophorin A and B (M'M'). Strain differences indicate receptor heterogeneity and two pathways for invasion. J Clin Invest 1987;80:1190–1193.
   Google Scholar
• Dolan SA, Miller LH, Wellems TE. Evidence for a switching mechanism in the invasion of erythrocytes by Plasmodium falciparum. J Clin Invest 1990;86:618–624.
   PubMed Web of Science ®Google Scholar
• Sim BK. EBA-175: an erythrocyte-binding ligand of Plasmo-dium falciparum. Parasitol Today 1995;11:213–217.
   PubMedGoogle Scholar
• Chitnis CE, Chaudhuri A, Horuk R, Pogo AO, Miller LH. The domain on the Duffy blood group antigen for binding Plasmodium vivax and Plasmodium knowlesi malarial parasites to erythrocytes. J Exp Med 1996;184:1531–1536.
   PubMed Web of Science ®Google Scholar
• Mayer DC, Kaneko O, Hudson-Taylor DE, Reid ME, Miller LH. Characterization of a Plasmodium falciparum erythrocyte-binding protein paralogous to EBA-175. Proc Natl Acad Sci USA 2001;98: 5222–5227.
   PubMed Web of Science ®Google Scholar
• Chen Q, Schlichtherle M, Wahlgren M. Molecular aspects of severe malaria. Clin Microbiol Rev 2000;13:439–450.
   PubMed Web of Science ®Google Scholar
• Medana IM, Chaudhuri G, Chang-Ling T, Hunt NH. Central nervous system in cerebral malaria: "Innocent bystander" or active participant in the induction of immunopathology. Immunol Cell Biol 2001;79: 101–120.
   Google Scholar
• Baruch DI. Adhesive receptors on malaria-parazited red cells. Baillieres Best Pract Res Clin Hematol 1999;12:747–761.
   PubMed Web of Science ®Google Scholar
• Rowe JA, Moulds JM, Newbold CI, Miller LH. P falciparum rosetting mediated by a parasite-variant erythrocyte mem-brane protein and complement-receptor 1. Nature 1997; 338:292–295.
   Google Scholar
• Barragan A, Fernandez V, Chen Q, von Euler A, Wahlgren M, Spillmann D. The Duffy-binding like domain of Plasmodium falciparum erythrocyte membrane protein 1 (PfEMP1) is a heparan sulfate ligand that requires 12 mers for binding. Blood 2000;95: 3594–3599.
   Google Scholar
• Telen MJ. Blood group antigens on complement receptor/re-gulatory proteins. Transfus Med Rev 1995;9:20–28.
   PubMed Web of Science ®Google Scholar
• Moulds JM, Zimmerman PA, Doumbo OK, Kassambara L, Sagara I, Diallo DA, Atkinson JP, Krych-Goldberg M, Hauhart RE, Hourcade DE, McNamara DT, Birmingham DJ, Rowe JA, Moulds JJ, Miller LH. Molecular identification of Knops blood group polymorphisms found in long homologous region D of complement receptor 1. Blood 2001;97: 2879–2885.
   PubMed Web of Science ®Google Scholar
• Woolley Ij, Hotmire KA, Sramkoski RM, Zimmerman PA, Kazura JW. Differential expression of the Duffy antigen receptor for chemokines according to RBC age and FY genotype. Transfusion 2000;40:949–953.
   PubMed Web of Science ®Google Scholar
• Yazdanbakhsh K, Rios M, Storry JR, Kosower N, Parasol N, Chaudhuri A, Reid ME. Molecular mechanisms that lead to reduced expression of Duffy antigens. Transfusion 2000; 40:310–320.
   PubMed Web of Science ®Google Scholar
• Michon P, Woolley I, Wood EM, Kastens W, Zimmerman PA, Adams JH. Duffy-null promoter heterozygosity reduces DARC expression and abrogates adhesion of the P vivax ligand required for blood-stage infection. FEBS Lett 2001;495:111–114.
   PubMed Web of Science ®Google Scholar
• Cavasini CE, Pereira FJT, Ribeiro WL, Wunderlich G, Ferreira MU. Duffy blood group genotypes among malaria patients in Rondonia, Western Brazilian Amazon. Rev Soc Bras Med Trop 2001;34:591–595.
   PubMedGoogle Scholar
• Masson SJ, Miller LH, Shiroish T, Dvorak JA, McGinniss MH. The Duffy blood group determinants: Their role in the susceptibility of human and animal erythrocytes to Plasmodium knowlesi malaria. Br J Haematol 1977;36: 327–335.
   PubMed Web of Science ®Google Scholar
• Shimizu Y, Kimura M, Settheetham-Ishida W, Duangchang P, Ishida T. Serotyping of Duffy blood group in several Thai ethnic groups. Southeast Asian J Trop Med Public Health 1997;28:32–35.
   PubMedGoogle Scholar