Band 3-glycophorin A association in erythrocyte membranes demonstrated by combining protein diffusion measurements with antibody-induced cross-linking

Nigg, Erich A.; Bron, Claude; Girardet, M.; Cherry, Richard J.

doi:10.1021/bi00550a024

Cited by 142 publications

(42 citation statements)

References 59 publications

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“…Whether the MSP1-band 3 interaction plays a primary role in a dominant sialic acid-independent invasion pathway across P. falciparum lines remains to be seen. Association between band 3 and GPA in the human RBC membrane has been shown (44,45). In this regard, an RBC invasion mechanism in which the parasites use band 3 and GPA in a cooperative or complementary manner could be possible.…”

Section: Discussionmentioning

confidence: 99%

Band 3 is a host receptor binding merozoite surface protein 1 during thePlasmodium falciparuminvasion of erythrocytes

Goel

Chen

et al. 2003

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

200

217

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We report the molecular identification of a sialic acid-independent host–parasite interaction in the Plasmodium falciparum malaria parasite invasion of RBCs. Two nonglycosylated exofacial regions of human band 3 in the RBC membrane were identified as a crucial host receptor binding the C-terminal processing products of merozoite surface protein 1 (MSP1). Peptides derived from the receptor region of band 3 inhibited the invasion of RBCs by P. falciparum. A major segment of the band 3 receptor (5ABC) bound to native MSP142 and blocked the interaction of native MSP142 with intact RBCs in vitro. Recombinant MSP119 (the C-terminal domain of MSP142) bound to 5ABC as well as RBCs. The binding of both native MSP142 and recombinant MSP119 was not affected by the neuraminidase treatment of RBCs, but sensitive to chymotrypsin treatment. In addition, recombinant MSP138 showed similar interactions with the band 3 receptor and RBCs, although the interaction was relatively weak. These findings suggest that the chymotrypsin-sensitive MSP1–band 3 interaction plays a role in a sialic acid-independent invasion pathway and reveal the function of MSP1 in the Plasmodium invasion of RBCs

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Section: Discussionmentioning

confidence: 99%

Band 3 is a host receptor binding merozoite surface protein 1 during thePlasmodium falciparuminvasion of erythrocytes

Goel

Chen

et al. 2003

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

200

217

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“…To date, there are several studies that suggest how glycophorin A may associate with the skeletal proteins. Nigg et al (41) performed protein rotational diffusion measurements, which suggest a noncovalent association of the intramembranous portion of glycophorin A with that of band 3. Because band 3 is known to bind to protein 2.1, which in turn is bound to spectrin, it is possible that it is through this band 3 association that glycophorin A affects the skeleton.…”

Section: Discussionmentioning

confidence: 99%

Erythrocyte membrane rigidity induced by glycophorin A-ligand interaction. Evidence for a ligand-induced association between glycophorin A and skeletal proteins.

Chasis¹,

Mohandas²,

Shohet³

1985

J. Clin. Invest.

112

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Erythrocyte skeletal proteins are known to play an important role in determining membrane deformability. In order to see whether transmembrane proteins also influence deformability and, if so, whether this influence is mediated by an interaction with the membrane skeleton, we examined the effect on deformability of ligands specific for transmembrane proteins. We found membrane deformability markedly reduced in erythrocytes that were pretreated with glycophorin A-specific ligands. In contrast, ligands specific for band 3 and A and B blood group antigens had no effect. The increase in membrane rigidity appeared to depend upon a transmembrane event and not upon a rigidity-inducing lattice on the outside surface of the cell in that a monovalent Fab of antiglycophorin IgG caused decreased deformability. We therefore looked for a ligand-induced association of glycophorin and the skeletal proteins and found, in Triton X-100-insoluble residues, a partitioning of glycophorin with the skeletal proteins only after preincubation with a ligand specific for glycophorin. We then studied cells and resealed membranes with skeletal protein abnormalities. In spectrin-deficient and protein 4.1-deficient erythrocytes and in 2,3-diphosphoglycerate-treated resealed membranes, the antiglycophorin IgG was only one-third as effective in decreasing deformability as it was in normal cells. Thus, normal skeletal proteins appear to be essential for liganded glycophorin to affect membrane deformability maximally. Taken together, these observations indicate that there is a ligand-induced interaction between glycophorin A and skeletal proteins and that this interaction can directly influence membrane deformability.

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“…Abundant evidence implicates the RBC membrane skeleton in controlling band 3 lateral mobility. Disruption of spectrin-ankyrin and ankyrin-band 3 linkages causes band 3 mobility to increase (21)(22)(23)(24), as does treatment with proteases to remove the cytoplasmic domain of band 3 (25,26) or treatment with ATP or 2,3-DPG (27) at levels that are sufficient to destabilize isolated RBC membrane skeletons (28) Band 3 rotational mobility has been studied in normal RBC ghosts (26,(34)(35)(36)(37)(38)(39)(40)(41)(42)(43)(44), abnormal RBC ghosts (45,46), and intact RBCs (19,31,37).2 Rapidly rotating, slowly rotating, and rotationally immobile forms of band 3 appear to coexist in the membrane. At 37°C in normal RBC membranes, 20-25% of band 3 molecules rotate with correlation times (r) < 250 Ms, 50-75% rotate with r 1-3 ms, and 5-25% are rotationally immobile on the time scale of the experiment (19,37,40 About half of the rapidly rotating band 3 molecules may rotate with correlation times of 25-30 ,ts; this population could represent band 3 dimers rotating free of constraints other than the viscosity of the lipid bilayer (37).…”

Section: Introductionmentioning

confidence: 99%

Differential control of band 3 lateral and rotational mobility in intact red cells.

Corbett¹,

Agre²,

Palek³

et al. 1994

J. Clin. Invest.

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Measurements of integral membrane protein lateral mobility and rotational mobility have been separately used to investigate dynamic protein-protein and protein-lipid interactions that underlie plasma membrane structure and function. In model bilayer membranes, the mobilities of reconstituted proteins depend on the size of the diffusing molecule and the viscosity of the lipid bilayer. There are no direct tests, however, of the relationship between mechanisms that control protein lateral mobility and rotational mobility in intact biological membranes. We have measured the lateral and rotational mobility of band 3 in spectrin-deficient red blood cells from patients with hereditary spherocytosis and hereditary pyropoikilocytosis. Our data suggest that band 3 lateral mobility is regulated by the spectrin content of the red cell membrane. In contrast, band 3 rotational mobility is unaffected by changes in spectrin content. Band 3 lateral mobility and rotational mobility must therefore be controlled by different molecular mechanisms. (J. Clin. Invest. 1994. 94:683-688.) Key words: erythrocyte membrane * hereditary spherocytosis -hereditary pyropoikilocytosis fluorescence photobleaching recovery polarized fluorescence depletion

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Band 3-glycophorin A association in erythrocyte membranes demonstrated by combining protein diffusion measurements with antibody-induced cross-linking

Cited by 142 publications

References 59 publications

Band 3 is a host receptor binding merozoite surface protein 1 during thePlasmodium falciparuminvasion of erythrocytes

Band 3 is a host receptor binding merozoite surface protein 1 during thePlasmodium falciparuminvasion of erythrocytes

Erythrocyte membrane rigidity induced by glycophorin A-ligand interaction. Evidence for a ligand-induced association between glycophorin A and skeletal proteins.

Differential control of band 3 lateral and rotational mobility in intact red cells.

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