Abstract
HEREDITARY ovalocytosis is common in some areas of Melanesia and South East Asia where malaria is endemic. These red cells resist invasion by malarial parasites in vitro1,2 and ovalocytic individuals are less parasitized than normal3. This has been attributed to the greater rigidity of ovalocytic red cells4,5. It has been suggested that South East Asian ovalocytosis results from the heterozygous presence of an altered membrane anion transporter (band 3)6,7. We have used the polymerase chain reaction to clone the abnormal band 3 complementary DNA from an ovalocytic of Indian origin8 and found two changes from the normal protein: a point mutation (Lys56-→Glu) and the deletion of the sequence AFSPQVLAA (residues 400–408), but no evidence for an N-terminal extension7. The deletion is also found in the abnor-mal band 3 of South East Asian ovalocytes9 and seems to be responsible for the unusual properties of the ovalocytic red cell. We show here that the membrane domain of the abnormal ovalocyte band 3 has a substantially altered structure and that the protein is defective in anion transport activity. The changed transport properties of the red cells may have a role in the reduced para-sitaemia of ovalocytic individuals.
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Schofield, A., Reardon, D. & Tanner, M. Defective anion transport activity of the abnormal band 3 in hereditary ovalocytic red blood cells. Nature 355, 836–838 (1992). https://doi.org/10.1038/355836a0
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DOI: https://doi.org/10.1038/355836a0
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