Two individuals with elliptocytic red cells apparently lack three minor erythrocyte membrane sialoglycoproteins

Anstee, David J.; Parsons, Stephen; Ridgwell, K.; Tanner, M. J. A.; Merry, Anthony H.; Thomson, Eileen E.; Judson, P. A.; Johnson, Pauline; Bates, Sandra R.; Fraser, Iain D. C.

doi:10.1042/bj2180615

Cited by 142 publications

(68 citation statements)

References 11 publications

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“…The common mutation in erythrocyte band 3, resulting in ovalocytosis, was not described at the time of the study by Serjeantson (28), and this omission may have influenced the results. Pasvol et al (29) found reduced invasion of Gerbich erythrocytes, but these cells were also ovalocytic (30). It is possible that hereditary ovalocytosis caused by band-3 mutations influenced the invasion and frequency of infection.…”

Section: Discussionmentioning

confidence: 99%

Characterization of a Plasmodium falciparum erythrocyte-binding protein paralogous to EBA-175

Mayer

Kaneko

Hudson-Taylor

et al. 2001

Proc. Natl. Acad. Sci. U.S.A.

163

132

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A member of a Plasmodium receptor family for erythrocyte invasion was identified on chromosome 13 from the Plasmodium falciparum genome sequence of the Sanger Centre (Cambridge, U.K.). The protein (named BAEBL) has homology to EBA-175, a P. falciparum receptor that binds specifically to sialic acid and the peptide backbone of glycophorin A on erythrocytes. Both EBA-175 and BAEBL localize to the micronemes, organelles at the invasive ends of the parasites that contain other members of the family. Like EBA-175, the erythrocyte receptor for BAEBL is destroyed by neuraminidase and trypsin, indicating that the erythrocyte receptor is a sialoglycoprotein. Its specificity, however, differs from that of EBA-175 in that BAEBL can bind to erythrocytes that lack glycophorin A, the receptor for EBA-175. It has reduced binding to erythrocytes with the Gerbich mutation found in another erythrocyte, sialoglycoprotein (glycophorin C͞D). The interest in BAEBL's reduced binding to Gerbich erythrocytes derives from the high frequency of the Gerbich phenotype in some regions of Papua New Guinea where P. falciparum is hyperendemic.

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Section: Discussionmentioning

confidence: 99%

Characterization of a Plasmodium falciparum erythrocyte-binding protein paralogous to EBA-175

Mayer

Kaneko

Hudson-Taylor

et al. 2001

Proc. Natl. Acad. Sci. U.S.A.

163

132

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“…The number of copies of GPC per red cell varies from 50,000 to 143,000 (45)(46)(47), depending upon the method of estimation. Previously, 80,000 copies of p55 per red cell were estimated by an immunoblotting assay (1) and reflect a minimum estimate.…”

Section: Discussionmentioning

confidence: 99%

The PDZ Domain of Human Erythrocyte p55 Mediates Its Binding to the Cytoplasmic Carboxyl Terminus of Glycophorin C

Marfatia

Morais-Cabral²,

Kim

et al. 1997

Journal of Biological Chemistry

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The PDZ domain, also known as the GLGF repeat/DHR domain, is an ϳ90-amino acid motif discovered in a recently identified family of proteins termed MAGUKs (membrane-associated guanylate kinase homologues). Sequence comparison analysis has since identified PDZ domains in over 50 proteins. Like SH2 and SH3 domains, the PDZ domains mediate specific protein-protein interactions, whose specificities appear to be dictated by the primary structure of the PDZ domain as well as its binding target. Using recombinant fusion proteins and a blot overlay assay, we show that a single copy of the PDZ domain in human erythrocyte p55 binds to the carboxyl terminus of the cytoplasmic domain of human erythroid glycophorin C. Deletion mutagenesis of 21 amino acids at the amino terminus of the p55 PDZ domain completely abrogates its binding activity for glycophorin C. Using an alanine scan and surface plasmon resonance technique, we identify residues in the cytoplasmic domain of glycophorin C that are critical for its interaction with the PDZ domain. The recognition specificity of the p55 PDZ domain appears to be unique, since the three PDZ domains of hDlg (human lymphocyte homologue of the Drosophila discs large tumor suppressor) do not bind the cytoplasmic domain of glycophorin C. Taken together with our previous studies, these results complete the identification of interacting domains in the ternary complex between p55, glycophorin C, and protein 4.1. Implications of these findings are discussed in terms of binding specificity and the regulation of cytoskeleton-membrane interactions.p55 is a heavily palmitoylated peripheral membrane protein of the red blood cell membrane (1). The primary structure of p55 defines several distinct domains including the PDZ domain, the SH3 domain, the protein 4.1 binding domain, the tyrosine phosphorylation domain, and a carboxyl-terminal guanylate kinase-like domain (2). The domain organization of p55 is similar to a family of proteins termed MAGUKs 1 (membraneassociated guanylate kinase homologues), which appear to play important roles in the regulation of signaling pathways and cytoskeleton-membrane interactions (3-6). Among various protein domains of MAGUKs, the PDZ domain has been a focus of intense scrutiny (5-8). Like the SH2 and SH3 domains, the PDZ domains recruit cytoplasmic proteins to specific submembranous sites. For example, the PDZ 1 ϩ 2 domain, but not the PDZ 3 domain, of PSD-95 and hDlg interacts with the carboxyl terminus of the NMDA receptors and the Shaker type K ϩ channels, and this interaction plays an important role in the clustering of ion channels (5, 6). The PDZ domains have also been shown to interact with other PDZ domains. The PDZ domain of neuronal nitric-oxide synthase binds to the PDZ domain of syntrophin at the sarcolemma in skeletal muscle and to the PDZ 2 domain of PSD-95 at the synaptic junctions of neuronal cells (9, 10). These observations suggest that the primary structures of both the PDZ domain and its target peptide govern the specificity as well as the affin...

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“…There are numerous reports of shape abnormalities in erythrocytes deficient in either of the components (Anstee et al, 1984;Alloisio et al, 1985;Conboy et al, 1986;Reid et al, 1987;McGuire et al, 1988). Nevertheless, direct evidence for protein 4.…”

Section: Discussionmentioning

confidence: 99%

“…Fresh normal erythrocytes were available from Blood Services South West, Southmead Road, Bristol BS1O 5ND, U.K. Fresh Leach-phenotype erythrocytes were obtained from donor PL (Anstee et al, 1984). Leach-phenotype erythrocytes from donors KW (Anstee et al, 1984), SS, JJ and TL (Daniels et al, 1986) Peptide synthesis and coupling to carriers GPC peptides corresponding to amino acid residues 112-128 (Asp-Pro-Ala-Leu-Gln-Asp-Ala-Gly-Asp-Ser-Ser-Arg-Lys-GluTyr-Phe-Ile) (GPC peptide 1), 99-111 (Thr-Glu-Phe-Ala-GluSer-Ala-Asp-Ala-Ala-Leu-Gln-Gly) (GPC peptide 2) and 82-98 (Arg-Tyr-Met-Tyr-Arg-His-Lys-Gly-Thr-Tyr-His-Thr-AsnGlu-Ala-Lys-Gly) (GPC peptide 3) were synthesized using fluoren-9-ylmethoxycarbonyl (Fmoc)-protected amino acids (Atherton et al, 1981), as preactivated pentafluorophenyl esters (Kisfaludy and Schon, 1983), with a continuous-flow solid-phase polyamide resin (Dryland and Sheppard, 1986), on a Milligen 9050 PepSynthesizer.…”

Section: Materials and Methods Materialsmentioning

confidence: 99%

“…Erythrocytes lacking GPC and GPD (Leach phenotype) are elliptocytic (Anstee et al, 1984;Daniels et al, 1986), suggesting that these proteins play a role in regulating the stability and mechanical properties of normal erythrocytes. An attachment to the skeleton is likely, as GPC and GPD remain firmly associated with the skeletal proteins after extraction of erythrocyte membranes with non-ionic detergent (Mueller and Morrison, 1981).…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Localization of the protein 4.1-binding site on human erythrocyte glycophorins C and D

Ltd¹

1994

Biochemical Journal

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Two individuals with elliptocytic red cells apparently lack three minor erythrocyte membrane sialoglycoproteins

Cited by 142 publications

References 11 publications

Characterization of a Plasmodium falciparum erythrocyte-binding protein paralogous to EBA-175

Characterization of a Plasmodium falciparum erythrocyte-binding protein paralogous to EBA-175

The PDZ Domain of Human Erythrocyte p55 Mediates Its Binding to the Cytoplasmic Carboxyl Terminus of Glycophorin C

Localization of the protein 4.1-binding site on human erythrocyte glycophorins C and D

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