Human erythrocyte Band-3 has an altered N terminus in malaria-resistant Melanesian ovalocytosis.
There is a high prevalence of the erythrocyte polymorphism ovalocytosis associated with reduced susceptibility to malaria in Papua New Guinea. The major erythrocyte integral membrane protein, Band-3, showed markedly increased phosphorylation in whole cells or isolated ghosts from ovalocytic individuals. The cytoplasmic domain of the ovalocyte Band-3 was found to be approx. 3 kDa larger than the normocytic protein. The N-terminal sequence of the ovalocytic Band-3 was different from the reported sequence for human Band-3, suggesting that the increased size results from an N-terminal extension. Since this is the region of Band-3 which is phosphorylated and interacts with the red cell cytoskeleton, it is likely that this alteration in ovalocytic Band-3 is the underlying cause of the diverse alterations in ovalocytic cells including increased phosphorylation, increased membrane rigidity, decreased agglutinability by blood group antibodies and refractoriness to invasion by malarial parasites.
Jones
G L
GL
Queensland Institute of Medical Research, Herston, Australia.
Edmundson
H M
HM
Wesche
D
D
Saul
A
A
D001457:Anion Exchange Protein 1, Erythrocyte / Q000276:immunology / Q000378:metabolism*; D000906:Antibodies / Q000276:immunology; D004612:Elliptocytosis, Hereditary / Q000276:immunology / Q000378:metabolism*; D004910:Erythrocyte Membrane / Q000737:chemistry; D007113:Immunity, Innate; D008288:Malaria / Q000097:blood* / Q000276:immunology; D008542:Melanesia; D008565:Membrane Proteins / Q000276:immunology / Q000378:metabolism*; D010449:Peptide Mapping; D010710:Phosphates / Q000378:metabolism; D010748:Phosphopeptides / Q000032:analysis; D010761:Phosphorus Radioisotopes; D010766:Phosphorylation; D015995:Prevalence
D001457:Anion Exchange Protein 1, Erythrocyte; D000906:Antibodies; D008565:Membrane Proteins; D010710:Phosphates; D010748:Phosphopeptides; D010761:Phosphorus Radioisotopes; C018279:sodium phosphate