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Blood, Vol. 92 No. 12 (December 15), 1998:
pp. 4836-4843
By
From the Department of Pathology, Brigham and Women's Hospital,
Harvard Medical School, Boston, MA; the Institute of Hematology and
Blood Transfusion, Prague, Czech Republic; the Department of Biomedical
Research, St. Elizabeth's Medical Center, Tufts University School of
Medicine, Boston, MA; and the Immunohematology Laboratory, New York
Blood Center, New York, NY.
Recent studies have demonstrated that band 3 carries antigens of the
Diego blood group system and have elucidated the molecular basis of
several previously unassigned low incidence and high incidence
antigens. Because the available serological data suggested that band 3 may carry additional low incidence blood group antigens, we screened
band 3 genomic DNA encoding the membrane domain of band 3 for
single-strand conformational polymorphisms. We found that the putative
first ectoplasmic loop of band 3 carries blood group antigen ELO, 432 Arg
BAND 3 (anion exchanger 1 [AE1]) is the
most abundant integral protein of the red blood cell (RBC) membrane,
being present in more than 1 million copies per RBC. It consists of two
structurally and functionally largely independent domains. The
N-terminal cytoplasmic domain of band 3 links the membrane to the
underlying spectrin-based membrane skeleton and interacts with several
glycolytic enzymes, hemoglobin, and hemichromes. The main function of
the C-terminal membrane domain is to mediate exchange of chloride and
bicarbonate anions across the plasma membrane. Current structural
models predict that the membrane domain consists of 12 to 14 transmembrane helices connected by ectoplasmic and endoplasmic
loops.1-4 The longest, fourth loop of band 3 is
N-glycosylated1,4 and the carbohydrate chain carries more
than half of the RBC ABO blood group epitopes.5
Mutations of band 3 protein have been implicated in the pathogenesis of
Southeast Asian ovalocytosis,6,7 hereditary
spherocytosis,8-11 congenital acanthocytosis,12
and, recently, distal renal tubular acidosis.13,14 An amino
acid substitution in the cytoplasmic domain of band 3 underlies the
abnormal electrophoretic mobility of a polymorphic band 3 variant known
as band 3 Memphis.15,16 Yet another variant of band 3, known as band 3 Memphis II, displays, in addition to the abnormal
electrophoretic mobility, an increased binding of the anion flux
inhibitor dihydrodiisothiocyanatodisulfonate, disodium salt
(H2DIDS).17 Spring et al18 reported
that the Memphis II variant of band 3 carries the Dia blood
group antigen.
Dia is a low incidence blood group antigen in Caucasians
that is antithetical to Dib.19 Prevalence of
Dia is much higher in American Indians, reaching up to 54%
in some groups of South American Indians.20 The underlying
polymorphism is a single amino acid substitution in position 854, with
proline of the wild-type band 3 corresponding to the Dib
antigen and leucine to the Dia antigen.21,22
Dia and Dib became the first fully
characterized antigens of the Diego blood group system assigned to the
band 3 protein.21 Subsequently, Bruce et al23
and our group24 have mapped the low incidence blood group
antigen Wra to the C-terminal end of the fourth ectoplasmic
loop. Glutamic acid 658 from the wild-type band 3 sequence underlies
the high incidence antigen, Wrb, whereas the low incidence
antigen, Wra, has lysine in the same position.
Recently, we and others have shown25,26 that three
additional low incidence antigens, Rba,27
WARR,28 and Wda,29 are associated
with different single point mutations on band 3 and therefore belong to
the Diego system. The amino acid changes associated with these three
antigens are, respectively, 548Pro Discovery of the molecular basis of these antigens yielded the first
insight into the Diego blood group system as well as valuable
information on the position and size of the external loops of band 3. In addition, in the case of Wrb, it helped to characterize
the site of the band 3-glycophorin A interaction, because the
Wrb antigen requires the presence of both these proteins
for its expression.24,36,37 These results also suggested
band 3 might carry additional low incidence antigens. We therefore
reviewed the list of remaining low incidence antigens that had
serological characteristics consistent with the possibility of their
being carried by band 3 and that we had in liquid nitrogen storage. We
found that antigens Bpa (Bishop),38 Wu
(Wulfsberg),39 Moa (Moen),40
Vga (Van Vugt),41 Hga
(Hughes),42 BOW,43 and ELO44
fulfilled these criteria and proceeded with characterization of their
molecular basis.
Subjects.
Samples were obtained through the Serum, Cell and Rare Fluid (SCARF)
exchange program or as gifts from numerous colleagues. Initial testing
was performed on DNA isolated from blood samples stored in liquid
nitrogen; additional testing was performed on freshly drawn blood
samples shipped on ice to Boston. The subjects were heterozygotes for
the studied blood group antigens.
DNA preparation.
DNA was isolated from blood samples (~150 µL) that had been stored
in liquid nitrogen or that had been obtained as fresh samples using the
QIAamp Blood Kit (QIAGEN Inc, Chatsworth, CA). The manufacturer's procedure for DNA isolation from whole blood was followed. The eluted
DNA was used directly for polymerase chain reaction (PCR) amplification.
Single-strand conformational polymorphism (SSCP) analysis and
sequencing of band 3 genomic DNA.
SSCP screening was performed according to Orita et al,45,46
with minor modifications. Exons encoding the membrane domain of band 3 were PCR-amplified using pairs of intronic primers flanking the exons
(Table 1; 35 cycles of 1 minute at 94°C
and 1 minute at 60°C). To each 10 µL PCR reaction, 2.5 µCi
32P-dATP (3,000 µCi/mmol; ICN, Costa Mesa, CA) was added.
The PCR products were diluted in formamide loading buffer (86%
formamide, 10% glycerol, 20 mmol/L EDTA, 0.25% bromophenol blue,
0.25% xylene cyanol), heat-denatured by boiling for 5 minutes, and
quickly cooled on ice. Samples were electrophoresed for 16 hours at
room temperature in a nondenaturing polyacrylamide mutation detection enhancement (MDE) gel (FMC BioProducts, Rockland, ME). Briefly, 25 mL
MDE gel solution was mixed with 69 mL deionized water, 6 mL 10×
TBE, 0.4 mL 10% ammonium persulfate, and 40 µL TEMED, and electrophoresis was performed at 8 W in the presence and at 4 W in the
absence of 10% glycerol. The gel was exposed to Kodak XAR-5 film
(Eastman Kodak, Rochester, NY) overnight at
Sequence comparisons and structural predictions.
All 12 currently known amino acid sequences of human,1,4
mouse,2 rat,47 chicken,48,49 and
trout50 erythroid band 3 proteins (AE1) and of the related
anion exchangers AE2 from human,51,52 mouse,53
rat,48 and rabbit54 and AE3 from
human,55 mouse,56 and rat48 were
retrieved from Genbank and aligned using the program CLUSTAL (PCGene;
Intelligenetics, Mountain View, CA). Predictions of the number and
position of band 3 transmembrane helices were made using programs
RAOARGOS, HELIXMEM, and SOAP (PCGene) based on the reported human AE1
cDNA sequence.1,4 Based on these predictions, sequence
comparisons, and available data on band 3 modifications by enzymes and
chemicals with known cleavage and binding sites, we created a model of
band 3 with 14 transmembrane helices.
Detection of band 3 mRNA alleles in reticulocyte RNA.
Total reticulocyte RNA was isolated by ammonium chloride
lysis57 and reverse transcribed using random primers. cDNA
was PCR-amplified using primers flanking the mutations, and the PCR product was digested with the appropriate restriction endonuclease. The
digested PCR product was visualized by electrophoresis in agarose gels
stained by ethidium bromide and the amount of DNA of individual bands
was quantitated by densitometric scanning using the Eagle Eye II system
(Stratagene, La Jolla, CA) and the ONE-Dscan 1.0 program (Scanalytics,
Billerica, MA).
Sulfate fluxes and di-isothiocyano-dihydrostilbene disulphonate
(DIDS) titration curves.
Cells were washed three times at 4°C in 140 mmol/L NaCl, 10 mmol/L
Na phosphate, pH 7.4 (PBS), and three times in 84 mmol/L trisodium
citrate, 1 mmol/L EGTA, pH 6.5, and subjected to assays of
unidirectional disodium 35S-sulfate (ICN, Costa Mesa, CA)
uptake in the absence or in the presence of increasing concentrations
of the anion transport inhibitor DIDS (Molecular Probes, Eugene, OR),
as described.10 Each flux study in RBCs carrying the
studied antigens was performed in parallel using RBCs from unrelated
subjects not carrying the antigens. The dependence of the sulfate
influx on the increasing concentrations of DIDS was obtained using the
linear least squares fit.
Enzyme treatment of intact RBCs.
One volume of washed RBCs was treated with 4 vol of Quantitation of erythrocyte membrane proteins.
Freshly drawn blood anticoagulated in acid citrate/dextrose was shipped
on ice to Boston. Within 48 hours of phlebotomy, erythrocyte ghosts
were prepared using the method of Dodge et al,58 with minor
modifications described in Jarolim et al.8 Erythrocyte membrane proteins were analyzed by sodium dodecyl
sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) followed by
densitometry as described,9 and the relative amounts of RBC
membrane proteins were expressed as ratios of integrated densitometric
peaks of individuals' proteins to the peak of band 3. The biochemical
findings were correlated with the clinical data and the results were
statistically evaluated.
SSCP are detected in three exons.
We detected SSCP polymorphisms in exon 12 in the carrier of the ELO
antigen; in exon 14 for Vga, BOW, Wu, and Bpa;
and in exon 16 for Hga and Moa
(Fig 1).
Sequence analysis of genomic DNA shows seven amino acid
substitutions.
We PCR-amplified and directly sequenced exons containing the SSCPs. The
detected mutations are summarized in Table
2. We have verified the presence of these mutations in additional
unrelated carriers of these seven blood group antigens with the
exception of Vga, for which only related individuals were
available. All seven mutations either create or abrogate restriction
sites (Table 2). In six cases, we used PCR amplification followed by
restriction digestion with an appropriate restriction endonuclease to
confirm the presence of the mutation in additional carriers of the
blood group antigen. Because endonuclease Tth 2 is not commercially available, we directly sequenced genomic DNA from the additional Bp(a+)
subject.
Position of the mutated amino acids in band 3.
Figure 2 schematically depicts the membrane
domain of band 3. The seven newly characterized blood group antigens
are shown in bold. Previously characterized blood group antigens
residing on band 3 are also shown. According to this scheme, six of
seven mutated amino acids are located in the putative first, third, and
fourth ectoplasmic loops of band 3, whereas asparagine 569, which is
mutated to lysine in Bp(a+) subjects, is located at the external end of
the sixth transmembrane segment. Proline 561, mutated to serine in the
BOW-positive subject, is also relatively highly conserved; however, the
degree of evolutionary conservation in the region of the third external
loop shown in Table 2 changes to some extent with variations in the
alignment parameters.
Evolutionary conservation of mutated amino acids.
We aligned the five known AE1 amino acid sequences of the erythroid
band 3 homologues as well as all 12 available sequences from the AE
gene family and evaluated the conservation of individual amino acids.
The results show (Table 2) that most of the mutated amino acids are not
conserved in evolution. The only exception again appears to be the
Bpa antigen (569 Asn Effects of enzyme treatment on RBC agglutinability.
We have digested intact RBCs from the carriers of all seven studied
blood group antigens by trypsin,
Similar quantities of normal and mutant mRNA alleles are detected in
reticulocyte RNA.
We isolated and reverse-transcribed total reticulocyte RNA and
amplified the cDNA as described. The PCR products were digested with
the appropriate restriction endonuclease and electrophoresed in an
ethidium bromide-stained gel. Densitometric scanning of the gel allowed
us to estimate the relative content of mRNA corresponding to the two
band 3 alleles of the heterozygous subjects. Using this
semiquantitative technique, we have not detected significant differences between the content of the two band 3 cDNA alleles, suggesting that the mutations affect neither the transcription of the
band 3 gene alleles nor the subsequent RNA processing (data not shown).
The mutations do not affect band 3 expression and function.
SDS-PAGE electrophoresis showed a normal electrophoretic pattern of
band 3 protein in the carriers of the blood group antigens, including
similar profiles of band 3 glycosylation (not shown). Subsequent
densitometric scanning detected normal content of band 3 and other RBC
membrane proteins. Because band 3 is the principal anion exchange
protein of the RBC membrane, we compared anion fluxes in erythrocytes
from carriers of the studied blood group antigens with those in normal
RBCs. We did not detect significant differences between heterozygotes
for the seven studied antigens and control subjects. Results of the
DIDS titration of sulfate influx in the cells expressing the ELO, Wu,
and Hga antigens are shown in
Fig 3.
As of 1995, 37 low incidence antigens were recognized as being discrete
genetic characteristics unassigned to a particular blood group
system.59 Many of the antibodies to these low incidence antigens occur together in multispecific sera.60 Often
these same sera contain antibodies to glycophorin A determinants or to
Wra, whose antithetical antigen Wrb has been
shown to result from the interaction between glycophorin A and band
3.23,24,36 Thus, we undertook a concerted effort to
identify band 3 polymorphisms recognized by these multispecific sera.
The authors thank the many colleagues who, over many years, sent us
samples of RBCs expressing low incidence antigens. We also thank the
following people who recently responded to requests for blood samples
from selected donors: Ranjan Malde from the National Blood Service
(London and the South East), London, UK; Graham Rowe from the National
Blood Service (Wales), Cardiff, Wales; Judy Martin from the American
Red Cross (Badger Region), Madison, WI; and Marilyn Moulds from Gamma
Biologicals, Inc (Houston, TX). We thank Dr Jiri Zavadil.
Milena Pohlova from the Institute of Hematology and Blood Transfusion
(Prague, Czech Republic) for help with DNA sequencing and for
preparation of the figures.
Submitted May 26, 1998;
accepted August 11, 1998.
Presented in part at the 49th Annual Meeting of the American
Association of Blood Banks, Orlando, FL, October 6-10, 1996. Address reprint requests to P. Jarolim, MD, PhD, Department of
Pathology, Brigham and Women's Hospital, Harvard Medical School, 75 Francis St, Boston, MA 02111; e-mail: pjarolim{at}rics.bwh.harvard.edu.
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Top
Abstract
Introduction
Trp; the third putative loop harbors antigens
Vga (Van Vugt), 555 Tyr
80°C using intensifying screens. The band 3 gene exons
displaying the SSCP were directly sequenced using the Sequenase version
2.0 DNA Sequencing Kit (Amersham, Arlington Heights, IL). We limited
our SSCP screening to exons 11 to 20 of the band 3 gene, because these
10 exons encode the whole membrane domain of band 3 and mutations
causing altered immunogenicity of band 3 are to be expected only in
this portion of band 3.
-chymotrypsin (5 mg/mL) for 1 hour at 37°C. Enzyme-treated cells were washed three
times with PBS. Both treated and untreated antigen-positive RBCs were
tested in parallel with the appropriate antisera.
/HCO
ISBT Working Party on Terminology for Red Cell Surface Antigens.
Vox Sang
69:265, 1995