Receptors on red cells for Plasmodium falciparum and their interaction with merozoites
- 13 November 1984
- journal article
- research article
- Published by The Royal Society in Philosophical Transactions of the Royal Society of London. B, Biological Sciences
- Vol. 307 (1131) , 189-200
- https://doi.org/10.1098/rstb.1984.0119
Abstract
The red cell sialoglycoproteins (glycophorins, $\alpha$(A), $\delta$(B) and $\beta$ and $\gamma$(C)) play a crucial role in the invasion of human red cells by merozoites of Plasmodium falciparum. Red cells deficient in any of the glycophorins, including $\beta$ (also known as glycoconnectin), resist infection by this parasite to varying degrees. These cells and other naturally occurring well-characterized glycophorin variants provide extremely powerful tools to dissect the role of these molecules in invasion. The binding of merozoites to human red cells appears analogous to the binding of wheatgerm agglutinin to sialoglycoconjugates. In both systems O- and N-linked oligosaccharides may be involved. Membrane lipid has not been implicated as a receptor for merozoites, but may instead non-specifically modify binding, as may electrostatic and hydrophobic interactions. The results of data using monoclonal antibodies and lectins, although possibly helpful in identifying specific determinants, must be interpreted with caution. Overall the data suggest that the red cell receptors for all strains of P. falciparum tested to date are located on the glycophorins. Accordingly these putative receptors have been used to affinity-purify complementary parasite components which may yet prove to be of protective immunological significance in a vaccine.
This publication has 41 references indexed in Scilit:
- Individuals lacking the Gerbich blood-group antigen have alterations in the human erythrocyte membrane sialoglycoproteins β and γBiochemical Journal, 1984
- Two individuals with elliptocytic red cells apparently lack three minor erythrocyte membrane sialoglycoproteinsBiochemical Journal, 1984
- Erythrocyte sialoglycoproteins and Plasmodium falciparum invasionTransactions of the Royal Society of Tropical Medicine and Hygiene, 1983
- Inhibition of malarial invasion of red cells by chemical and immunochemical linking of spectrin moleculesBritish Journal of Haematology, 1983
- Susceptibility to invasion by Plasmodium falciparum of some human erythrocytes carrying rare blood group antigensBritish Journal of Haematology, 1983
- Control of malaria virulence by alpha 1-acid glycoprotein (orosomucoid), an acute-phase (inflammatory) reactant.Proceedings of the National Academy of Sciences, 1983
- Structure, biosynthesis and functions of glycoprotein glycansCellular and Molecular Life Sciences, 1982
- Monoclonal antibodies to human erythrocytesEuropean Journal of Immunology, 1982
- Mechanism of Host Specificity in Malarial InfectionNature, 1973
- The Gerbich Blood Group System, Especially in MelanesiansVox Sanguinis, 1972