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 Previous Article | Table of Contents | Next Article 
Blood, Vol. 92 No. 7 (October 1), 1998:
pp. 2237-2243
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
By
Niva Parasol,
Marion Reid,
Maria Rios,
Lilian Castilho,
Ilana Harari, and
Nechama S. Kosower
From the Department of Human Genetics, Sackler School of Medicine,
Tel-Aviv University, Tel Aviv, Israel; the Department of Molecular
Genotyping, New York Blood Center, New York, NY; and the Blood Services
Center, Magen David Adom, Tel-Hashomer, Israel.
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ABSTRACT |
The Duffy blood group system is of clinical and biological
significance. Antibodies to Duffy antigens are responsible for some
cases of transfusion incompatibility and newborn hemolytic disease. The
Duffy protein is a receptor for the Plasmodium vivax erythrocyte-binding protein and is also a receptor for various chemokines (thus renamed Duffy Antigen Receptor for Chemokines [DARC]). The two Duffy polymorphic antigens, Fya and
Fyb (coded by the FY*A and FY*B alleles), are present on
erythrocyte membranes. The Fy(a b) phenotype is the predominant
one in populations of black people and also occurs in other
populations, including some non-Ashkenazi Jewish groups. The
Fy(ab) phenotype has been associated with a mutation in the FY*B
promoter at the GATA box that abolishes the expression of erythrocyte
Duffy protein. We describe here a novel mutation, present in the FY*B
coding sequence (271C  T), that is associated with some
Fy(b) phenotypes among non-Ashkenazi Jews and among Brazilian
blacks. The mutation is present in Fy(b) individuals, who have
wild-type FY*B GATA and carry the previously described 304G A substitution. The 271C T and 304G A can be
identified by restriction enzyme-generated restriction fragment length
polymorphisms. The 271C T substitution represents a
considerable change in chemical nature (Arg91 Cys), one
which may affect the antigenic determinants of DARC, and thus be of
clinical significance. The mutation may have implications for some
physiological roles of DARC and be of interest in malaria research and
in studies of population genetics.
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INTRODUCTION |
THE DUFFY BLOOD GROUP system is
significant in humans, and novel mutations with functional
consequences, such as the one we report here, are of considerable
interest. The two Duffy polymorphic antigens, Fya and
Fyb, are carried on proteins produced by the Duffy gene
alleles FY*A and FY*B. The antisera, anti-Fya and
anti-Fyb, define four major erythrocyte Duffy phenotypes:
Fy(a+b), Fy(ab+), Fy(a+b+), and
Fy(ab).1-3 The Fy(ab) phenotype
is rare among white and Asian populations, whereas it is the
predominant phenotype among populations of black people, especially
those originating in West Africa.3 The gene, the first one
to be assigned to a specific autosome,4 has been mapped to
1q22-23.5 The gene has been cloned and
sequenced6 and shown to have two exons.7 The
FY*A and FY*B alleles differ by a single-base substitution at
nucleotide 131 of the cDNA (A in FY*B and G in FY*A), resulting in a
polymorphism at amino acid residue 44, with aspartic acid (Asp) in
Fyb and glycine (Gly) in Fya.6-10
(The numbering of nucleotides and amino acid residues used here is
according to the cDNA and predicted protein sequence based on a single
exon published by Chaudhuri et al.6 The amino acid 44 cited
here would be amino acid 42, as predicted by Iwamoto et
al,7 based on a spliced transcript of two exons.) The
presence of guanine at this site generates a Ban I restriction
site in FY*A, thus allowing the identification of FY*A and FY*B by
Ban I restriction fragment length polymorphism
(RFLP).9,10 A substitution of T to C at the GATA box of the
FY*B promoter (46T C) (based on numbering
by Tournamille et al11) has been found in
Fy(ab) black individuals.11 This mutation
disrupts the binding site for the GATA-1 erythroid transcription
factor, results in a silent FY*B allele in erythroid cells, and is
considered to be responsible for most cases of Fy(ab)
erythrocytes in the black populations.11 The GATA mutation
generates a Sty I restriction site, allowing the identification
of this mutation by RFLP.11
The Duffy gene product is a transmembrane glycoprotein of 35 to 43 kD. The Duffy antigens are important in transfusion
incompatibility and hemolytic disease of the newborn. In addition, the
Duffy protein is a receptor for the erythrocyte-binding protein of
Plasmodium vivax; the resistance in West African populations to
infection by P vivax malarial parasites has been attributed to
the high incidence of Fy(ab) in these
populations.12 The Duffy protein has also been identified
as a receptor for various chemokines and renamed as Duffy Antigen
Receptor for Chemokines (DARC). DARC is expressed in various tissues,
where it has been identified in endothelial cells lining postcapillary
venules. It has also been identified in cerebellar Purkinje cells. DARC
may have important physiological functions in homeostatic processes in
some brain regions and in processes involving inflammatory
chemokines.10,12-14
Several examples of erythrocytes have been described that exhibit weak
reactivity with some anti-Fyb sera, and no reactivity with
others, thereby giving apparent discrepancies between the
Fyb phenotype and genotype.3,12,15 In the
course of work on possible association of schizophrenia with Duffy
antigens,16,17 we found a sample for which the erythrocyte
phenotype of Fy(ab) (as determined by standard
agglutination assays) did not correspond to the Duffy genotype. This
sample was found to be FY*B/FY*B as determined by Ban I RFLP,
and only heterozygous for the mutation at the GATA box, as identified
by Sty I RFLP.11 DNA sequencing showed two
mutations in the coding sequence, a novel mutation at nucleotide (nt)
271 from C to T (271C T), and the previously reported
mutation at nt 304 from G to A (304 G A).8,13
Subsequently, polymerase chain reaction (PCR)-RFLP assays were
established to screen for these mutations. As described here, the
simultaneous presence of these two mutations resulted in the silencing
of the Fyb antigen in erythrocytes. This phenomenon is of
clinical significance and may have implications for physiological roles
of DARC in tissues other than erythrocytes, and it may be of interest
in studies of population genetics.
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MATERIALS AND METHODS |
Phenotyping of erythrocyte Duffy antigens.
Blood samples were from donors whose identity was unknown (unlinked).
The Fy(b) samples were selected based on routine phenotyping of
washed erythrocytes with anti-Fya and anti-Fyb
used according to the manufacturer's instructions. Erythrocytes from
the non-Ashkenazi Jews in Israel were tested with antiserum from Gamma
Biologicals Inc (Houston, TX). Erythrocytes from Brazilian blacks were
tested with antisera from three companies (Gamma Biologicals Inc;
Biotest-São Paulo, Brazil; and DiaMed, Cressier sur Morat, Switzerland). It should be noted that the serological
testing used here does not distinguish between Fy(ab) and
Fy(abweak) erythrocyte phenotypes.
Fy(abweak) erythrocytes often type as
Fy(ab) if only the usual anti-Fyb are used by
routine methods. Further testing with a variety of anti-Fyb
reagents as well as a quantitative adsorption and elution analysis have
to be performed on erythrocytes identified as Fy(b-) by standard agglutination assays, to characterize such samples. DNA was prepared at
the time of Fyb testing and by the time that analysis of
DNA showed the mutations described here, erythrocytes were not
available for further testing.
DNA preparation.
White blood cells (WBCs) from whole blood were obtained after
erythrocyte lysis with a solution containing 155 mmol/L
NH4Cl, 10 mmol/L KHCO3, and 1.0 mmol/L
Na2-EDTA. The washed pellets were suspended in buffer
containing 10 mmol/L Tris-HCl, pH 7.5, 75 mmol/L NaCl, 24 mmol/L EDTA,
0.5% sodium dodecyl sulfate, and 150 µg proteinase K/mL, and kept
for 4 hours at 55°C. Proteins were precipitated by salting out,
using saturated NaCl solution, vigorous mixing, and
centrifugation.18 The supernatants were mixed with cold
ethanol. The precipitated DNA was solubilized in 10 mmol/L Tris-HCl, pH
7.5, 1.0 mmol/L EDTA. Alternatively, WBC DNA was extracted using DNAzol
Kit (GIBCO-BRL, Gaithersburg, MD), according to the manufacturer's
recommendations. The DNA solutions were analyzed for quality by agarose
gel electrophoresis and for quantity by optical density measurements at
260 nm.
DNA amplification.
PCR was performed using 100 to 200 ng of DNA, 3 pmol of each primer, 2 nmol of each dNTP, 1.0 U Taq polymerase and buffer (Perkin Elmer,
Norwalk, CT), in a total volume of 40 µL. The primers used for PCR
amplification, FY3, 5 -CCCTCTTGTGTCCCTCCCTTT, located at
276 256, and FY4,
5-CAGAGCTGCGAGTGCTACCTA, located at 385 365, were
designed to encompass the coding region containing nt 131 (site for
FY*A/FY*B polymorphism9,10), nt 271 (site of novel mutation
described here), and nt 304 (site of mutation previously
described8,13). Reactions were performed in an automated
thermal cycler (PTC 100 MJ Research, Watertown, MA), with
denaturation at 94°C for 4 minutes, followed by 30 cycles of
amplification (94°C, 1 minute; 60°C, 1 minute; 72°C, 1 minute) and a final extension at 72°C for 10 minutes. A second PCR
amplification of a DNA segment containing the GATA mutation site
(nt 46) was performed using the published conditions
and primers P38 and P3911 (here named FY1 and FY2).
RFLP analysis of PCR products.
The restriction enzymes, buffers, and details for their use were
supplied by New England BioLabs (Beverly, MA). For the
identification of FY*A and FY*B, 15 µL of the PCR product (DNA
amplified by the FY3 and FY4 primers) was digested with Ban I. The restriction fragments were resolved by electrophoresis on 1%
agarose gel. For the identification of the GATA mutation, 25 µL of
the PCR product (DNA amplified by the FY1 and FY2 primers) was digested with Sty I,11 followed by electrophoresis on 12%
acrylamide gel. For the identification of the 271C T
mutation, 10 µL of the PCR product (DNA amplified by the FY3 and FY4
primers) was digested with Aci I, and for the identification of
the 304G A mutation, 10 µL of the same PCR product was
digested with Mwo I. The restriction fragments were resolved on
1% agarose gel.
Nucleotide sequence analysis.
The PCR-amplified fragments were sequenced on both strands by
thermocycling sequencing with automatic 377 DNA sequencer (Perkin Elmer). For the initial sample that showed the discrepancy between the
phenotype and genotype determined by Ban I and Sty I
[phenotype Fy(ab), and genotype FY*B/FY*B-46T C, ie, being only heterozygous for the GATA mutation], sequencing was
carried out between nt 276 to nt 1944, on overlapping DNA
fragments, amplified by several primers. After the identification of
the 271C T and 304G A mutations, other samples
were sequenced using FY3 for the PCR products generated by FY3 and FY4.
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RESULTS |
Alleles FY*A and FY*B in Fy(b) phenotypes among non-Ashkenazi
Jews.
Although the phenotype Fy(ab) is known to be present in
about 20% of Jews from Yemen and has also been observed among other non-Ashkenazi Jews,19,20 there is no published information on the genotypes among these ethnic groups. Using the Ban I
RFLP for the identification of the FY*A and FY*B
alleles,5-7 we analyzed the DNA samples of unrelated
individuals having Fy(ab) and Fy(a+b) phenotypes
(Fig 1). Among the Fy(a+b)
phenotypes, we found FY*A/FY*A (lanes 4, 6, and 7) and FY*A/FY*B (lanes
3 and 9); the Fy(ab) phenotypes were found to be
FY*B/FY*B (lanes 5, 8, and 10). The Ban I restriction patterns
of the PCR products indicate that the FY*B allele is the silent one in
the Fy(ab) samples from non-Ashkenazi Jews, as is the
case for the Fy(ab) phenotypes in the black populations.10,11
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| Fig 1.
Ban I RFLP for the identification of FY*A and
FY*B alleles in non-Ashkenazi Jews. DNA was amplified using FY3 and FY4
primers for the amplification of a DARC fragment containing the 131G
A substitution, responsible for FY*A and FY*B, respectively.
Restriction fragments were separated on 1% agarose gel. (A) Schematic
diagram of fragments generated by the Ban I digestion of FY*A
and FY*B DNA. (B) RFLP patterns of DNA from samples with the indicated
phenotypes, identified by antisera (the 52- and 44-bp fragments are not
detected in this gel). Lanes: 1, 100-bp ladder; 2, uncut; 3, 4, 6, 7, and 9, Fy (a+b); 5, 8, and 10, Fy(ab).
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The GATA mutation in Fy(b), FY*B non-Ashkenazi Jews.
To determine whether the GATA mutation, identified in the
Fy(ab) black population,11 was associated
with the Fy(b) phenotype among the non-Ashkenazi Jews,
Sty I RFLP11 were performed on PCR-amplified
genomic DNA from samples of Fy(ab) FY*B/FY*B, Fy(a+b) FY*A/FY*A, and Fy(a+b) FY*A/FY*B (genotypes as
identified by Ban I). As can be seen in
Fig 2, the Sty I RFLP identifies samples that are homozygous and heterozygous for the mutation, with
several samples that exhibit discrepancy between their phenotypes and
genotypes, as determined by Ban I and Sty I RFLPs
(genotypes of samples shown in lanes 1, 2, 4, and 7 corresponded to
their phenotypes; genotypes of samples shown in lanes 3, 5, and 6 did not correspond to their phenotypes). As shown in
Table 1, among 16 Fy(b) individuals,
the genotype corresponded to the phenotype in 12: 6 individuals were
Fy(ab), FY*B/FY*B by Ban I and homozygous for the
GATA mutation; 4 individuals were Fy(a+b), FY*A/FY*B by
Ban I and heterozygous for the GATA mutation; and 2 were
Fy(a+b), FY*A/FY*A by Ban I and homozygous for the
wild-type promoter. In contrast, 4 individuals showed a discrepancy
between the phenotype and genotype: 2 individuals, who were
Fy(ab), FY*B/FY*B by Ban I, were only
heterozygous for the GATA mutation, and two individuals, who were
Fy(a+b), FY*A/FY*B by Ban I, were homozygous for
wild-type promoter, ie, lacked the GATA mutation. These results
indicate that in some of the Fy(b) FY*B individuals among the
non-Ashkenazi Jews, some mutation(s) other than the GATA mutation is
responsible for the erythrocyte "silent" FY*B.
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| Fig 2.
Sty I RFLP for the identification of the GATA
mutation (46 T C). DNA was amplified using FY1 and FY2
primers11 for the amplification of a DARC fragment
encompassing nt 46. The restriction fragments were separated on 12%
acrylamide gel. (A) Schematic diagram of fragments generated by
Sty I digestion of the DARC fragment encompassing nt 46
FY*B, GATA mutation. (B) RFLP patterns of DNA from samples with the
indicated phenotyes, identified by antisera, and genotypes, as
determined by Ban I (the 12-bp fragment is not detected in
this gel). Lanes: 1, 2, and 4, Fy (a+b)FY*A/FY*A; 3 and 7, Fy(a-b-)FY*B/FY*B; 5 and 6, Fy (a+b)FY*A/FY*B.
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Identification of mutations at nucleotides 271 and 304.
DNA from the first discordant sample, identified as
Fy(ab) FY*B/FY*B and heterozygous for the GATA mutation,
was sequenced and found to have two mutations in the coding sequence,
as compared with the sequence of the wild FY*B allele.8-10
The first one was a novel mutation of C T at nucleotide 271 (271C T) and the second one was a previously described
mutation of G A at nucleotide 304 (304G A).8,13 Based on these mutations, PCR-RFLP were developed
for the identification of the mutations, Aci I RFLP for 271C
T (Fig 3) and Mwo I RFLP
for 304G A (Fig 4). As can be
seen in Table 1, all four individuals, whose GATA genotypes did not
correspond to their phenotypes were found to be heterozygous for both
mutations. The mutations detected by RFLP using Aci I and
Mwo I were further confirmed by sequencing the PCR-amplified DNA of these samples. The simultaneous presence of the 271C T and 304G A in the discordant cases implies that these
mutations are responsible for some cases of Fy(b), wild-type
GATA erythrocytes among Fy(b) non-Ashkenazi Jews.
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| Fig 3.
Aci I RFLP for the identification of the 271C T mutation. DNA was amplified using the FY3 and FY4 primers.
Restriction fragments were separated on 1% agarose gel. (A) Schematic
diagram of fragments generated by Aci I digestion of the
DARC fragment encompassing nt 271. (B) RFLP patterns of DNA from
samples with the indicated phenotypes, identified by antisera, and
genotypes, determined by Ban I and Sty I (FY*B
= wild-type GATA; FY*B = GATA mutation). Lanes: 1 through 3, Fy(ab)FY*B/FY*B; 4, Fy(ab)FY*B/FY*B; 5 through 7, Fy(a+b)FY*A/FY*B; 8, Fy (a+b)FY*A/FY*B.
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| Fig 4.
Mwo I RFLP for the identification of the 304G A mutation. DNA was amplified using the FY3 and FY4 primers.
Restriction fragments were separated on 1% agarose gel. (A) Schematic
diagram of fragments generated by Mwo I digestion of the DARC
fragment encompassing nt 304. (B) RFLP patterns of DNA from samples
with the indicated phenotypes, identified by antisera, and genotypes,
determined by Ban I and Sty I (FY*B = wild-type GATA;
FY*B = GATA mutation). Lanes: 1 and 2, Fy(a+b)FY*A/FY*B; 3 and 8, Fy(ab)FY*B/FY*B; 4 and 5, Fy(a+b)FY*A/FY*B; 6 and 7, Fy (ab) FY*B/FY*B.
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Identification of the 271C T and 304G A
mutations among Brazilian black Fy(b) individuals.
Thirty-four Fy(ab) and 15 Fy(a+b) samples from
Brazilian black people were analyzed for FY*A and FY*B alleles, using
the Ban I RFLP. As shown in Table
2, all Fy(ab) phenotypes were homozygous for the FY*B
allele. Among the Fy(a+b), 3 were homozygous for FY*A and 12 were heterozygous, FY*A/FY*B. These results correspond to those
observed in other studies on black populations,11,12 in
which homozygosity for the FY*B allele was found in
Fy(ab), and homozygosity for FY*A or heterozygosity for
FY*A/FY*B was shown in Fy(a+b), as determined by Ban I
RFLP. Analysis of the 49 samples with Sty I showed that 33 Fy(a-b-)FY*B/ FY*B were homozygous for the GATA mutation; thus, their
phenotype can be accounted for by the GATA mutation. One
Fy(ab)FY*B/FY*B individual was heterozygous for the GATA
mutation, thus showing a discrepancy between his phenotype and
genotype. Among the 15 Fy(a+b) individuals, the FY and GATA
genotypes corresponded to their phenotypes in 12: as expected, the
three Fy(a+b)FY*A/FY*A had the wild-type GATA and 9 Fy(a+b)FY*A/FY*B were heterozygous for the GATA mutation. In
contrast, in three individuals, who were Fy(a+b)FY*A/FY*B, wild-type GATA was found. Thus, in four individuals of the 49 analyzed,
their Duffy phenotypes and genotypes could not be explained by FY and
GATA genotyping. RFLP analysis by Aci I and Mwo I
showed that all four individuals were heterozygous for both the 271C T mutation and the 304G A mutation. These two
mutations were not found in the other 45 Fy(b) individuals, in
whom the genotype corresponded to the phenotype according to the FY and
GATA analysis (Table 2). These results show that, as in non-Ashkenazi
Jews, an FY*B mutation different from the common GATA mutation in black populations is also associated with some Fy(b) phenotypes among the Brazilian blacks. The findings indicate that the presence of both
mutations result in an Fy(b) phenotype.
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DISCUSSION |
We describe here a novel mutation in the FY*B allele of the Duffy
chemokine receptor gene. This mutation, together with a previously
described mutation, results in erythrocyte Fy(b) phenotype as
identified by standard agglutination assays (see Materials and
Methods). The phenotype Fy(ab), similarly identified by standard reagents, is present in about 70% of both American
blacks2,3 and Brazilian blacks,21 and is also
present in non-Ashkenazi Jews, notably in about 20% of Yemenite
Jews.19,20 The promoter GATA mutation in the FY*B
allele11 accounts for the Fy(b) phenotype among
African black populations.8-12 As is shown here, the same mutation is prevalent among the Brazilian blacks and is also found in
the FY*B allele among Fy(b) non-Ashkenazi Jews. However, in some
individuals there appeared to be a discrepancy between their Fy(b) phenotype and genotype, with a discordant FY*B allele
having the promoter wild-type GATA. In these individuals, two mutations in the coding sequence (271C T and 304G A) were
found in the discordant FY*B allele.
Both mutations were identified among the Fy(b)FY*B non-Ashkenazi
Jews and among the Brazilian blacks, suggesting an association with
FY*B gene silencing in erythroid cells. The 304G A mutation, which codes for Ala Thr at amino acid residue 102, has been previously described in a study using reverse transcriptase
(RT)-PCR of placental RNA as a source for cloning and
sequencing of the Duffy gene.13 In another study, the same
mutation was found in Fy(a+b+) and Fy(a+b) samples.8
Based on these studies, the 304G A mutation may be a
polymorphic one, as has been suggested.13 Further studies
are required to establish whether 304G A is a polymorphic
mutation, whether the 271C T mutation occurred in this
variant and whether the expression of both is necessary for the
Fy(b) phenotype. It is of interest to note that according to the
proposed three-dimensional structure of DARC (involving seven
transmembrane segments),12 the amino acid 102 (amino acid residue according to Chaudhuri et al6; residue 100 according to Iwamoto et al7) would be in the second
transmembrane segment, and a substitution of Ala Thr might not lead
to more than a modest change in receptor properties The 271C T
mutation, on the other hand, converts the residue 91 (amino acid
residue according to Chaudhuri et al6; residue 89 according
to Iwamoto et al7), assumed to be in the first cytoplasmic
loop, from Arg Cys. This substitution represents a considerable
change in the chemical nature of the local region and may affect the
behavior of DARC and its extracellular antigenic sites.
The finding that a combination of two mutations within the coding
sequence may result in an apparent erythrocyte Fy(b) phenotype raises several important questions. The promoter GATA substitution, which impairs the binding site of the erythroid transcription factor
and results in a silent erythroid FY*B allele and lack of erythrocyte
Duffy receptor, does not affect the expression of the gene in other
cells.10-12 It is not known at present whether the DARC
Arg91 Cys, Ala102 Thr mutant protein is present
in the erythrocyte membranes. The point mutations leading to amino acid
substitutions would be expected to allow the expression of the protein,
albeit in a possibly altered conformation and altered ligand-binding
properties. However, it cannot be excluded that such mutations result
in a deficiency or absence of the protein (eg, due to failure of being
incorporated into the cell membrane, or being susceptible to
degradation). It would be of interest to study whether this DARC mutant
is fully or partially expressed in or absent from erythrocytes and from
other cells. In addition, because the spliced transcript may normally
be the predominant one,7 it may be relevant to find out
whether there is any preferential effect on the expression of one of
the two transcripts6,7 in the mutant cells. In any case,
the overall phenotype of the mutant described here is expected to be
different from the GATA mutation, because both the erythrocytes and
other DARC expressing cells would be affected by mutations in the
coding sequence that alter the expression and/or ligand-binding
properties of the protein. Additional studies on the binding of a
variety of anti-Fyb, including quantitative titrations of
antibody binding, are necessary to determine whether the mutant
erythrocytes described here behave as a Fy(bweak) variant.
It may be important to define the properties of the mutant erythrocytes
and other DARC-expressing cells for binding malarial parasites and
chemokines. It should also be pointed out that chemokine binding to
DARC has characteristics different from those of antibody
binding,22 and that differences exist among various
chemokines in their interaction with DARC.23 Thus, DARC mutant erythrocytes that do not bind anti-Fyb may
nevertheless react with chemokines. Although the precise roles of DARC
in various tissues are not known at present, the properties of a mutant
such as the one described here may be of physiological significance.
In view of the importance of Duffy blood group system in clinical
medicine, eg, in cases of transfusion incompatibility and hemolytic
disease of the newborn,24,25 in forensic medicine, and in
malaria epidemiology, screening procedures are being developed for
detection of the known common variants and mutations.26,27 The restriction enzyme-generated RFLPs described here provide a means
for screening samples for the 271C T and the 304G A. Screening for these mutations in samples identified as Fy(b) and Fy(bweak) phenotypes would be important both for
clinical purposes and for population genetic studies.
| |
FOOTNOTES |
Submitted May 11, 1998;
accepted July 9, 1998.
Supported in part by the Israel Mental Health Association (Enosh), by
the Pioneer Fund, and by the Igo Ornstein Chair for the Study of
Geriatrics (to N.S.K.); by a National Institutes of Health Specialized
Center of Research (SCOR) grant in Transfusion Medicine and Biology No.
HL54459 (to M.R.); and by Fundação de Amparo à
Pesquisa do Estado de São Paulo, Brazil (to L.C.). This work is
in partial fulfillment of the requirements for the PhD degree from Tel
Aviv University (N.P.).
Address reprint requests to Nechama S. Kosower, MD, Department of Human
Genetics, Sackler School of Medicine, Tel-Aviv University, Tel Aviv
69978, Israel; e-mail: nkosower{at}ccsg.tau.ac.il.
The publication costs of this article were defrayed in part by page charge payment. This article must therefore be hereby marked "advertisement" is accordance with 18 U.S.C. section 1734 solely to indicate this fact.
| |
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Abstract
Introduction
Abstract