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Changes in the blood group Wright antigens are associated with a mutation
at amino acid 658 in human erythrocyte band 3: a site of interaction
between band 3 and glycophorin A under certain conditions [see comments]
LJ Bruce, SM Ring, DJ Anstee, ME Reid, S Wilkinson and MJ Tanner
Department of Biochemistry, School of Medical Sciences, University of
Bristol, UK.
The Wright (Wr) blood group antigens, Wra and Wrb, have been suggested to
be determined by alleles of the same gene. The Wrb antigen appears to
involve both red blood cell (RBC) band 3 and glycophorin A (GPA). We have
examined the cDNA sequences of the band 3 and GPA of one of the two known
Wr(a+b-) individuals. We show that this individual is homozygous for the
mutation Glu658-->Lys in band 3, but has normal GPA. Putative
heterozygotes with Wr(a+b+) RBCs have both Glu and Lys at residue 658 of
band 3, whereas the common Wr(a-b+) RBC phenotype only have band 3 with
Glu658. The Wra and Wrb antigens are determined by the amino acid at
residue 658 of band 3 and are antithetical. Examination of the amino acid
sequence and Wrb antigen expression of GPA-related hybrid glycophorins
suggests that Arg61 of GPA interacts with Glu658 of band 3 to form the Wrb
antigen. We suggest that the interaction is stabilized by the presence of
anti-Wrb antibodies and that this site of association between GPA and band
3 may be responsible for the previously reported ability of anti-GPA
antibodies to decrease the deformability of RBCs.
Volume 85,
Issue 2,
pp. 541-547,
01/15/1995
Copyright © 1995 by The American Society of Hematology

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