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The membrane characteristics of Plasmodium falciparum ‐infected and ‐uninfected heterozygous α 0 thalassaemic erythrocytes
Author(s) -
Williams Thomas N.,
Weatherall David J.,
Newbold Christopher I.
Publication year - 2002
Publication title -
british journal of haematology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.907
H-Index - 186
eISSN - 1365-2141
pISSN - 0007-1048
DOI - 10.1046/j.1365-2141.2002.03610.x
Subject(s) - plasmodium falciparum , biology , cd36 , red blood cell , antibody , malaria , receptor , immunology , biochemistry
Summary. The α thalassaemias are the commonest known human genetic disorders. Although they have almost certainly risen to their current frequencies through natural selection by malaria, the precise mechanism of malaria protection remains unknown. We have investigated the characteristics of red blood cells (RBCs) from individuals heterozygous for α 0 thalassaemia (–/αα) from a range of perspectives. On the basis of the hypothesis that defects in membrane transport could be relevant to the mechanism of malaria protection, we investigated sodium and potassium transport and the activity of the Plamodium falciparum ‐induced choline channel but found no significant differences in –/αα RBCs. Using flow cytometry, we found that thalassaemic P. falciparum ‐infected RBCs (IRBCs) bound 44% more antibody from immune plasma than control IRBCs. This excess binding was abrogated by predigestion of IRBCs with trypsin but was not directed at the variant surface molecule PfEMP1. Furthermore, we found no evidence for altered cytoadhesion of α‐thalassaemic IRBCs to the endothelial receptors intercellular adhesion molecule‐1 (ICAM‐1), CD36 or thrombospondin. We hypothesize that altered red‐cell membrane band 3 protein may be a target for enhanced antibody binding to α‐thalassaemic IRBCs and could be involved in the mechanism of malaria protection.