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. 1984 Sep 1;160(3):788–798. doi: 10.1084/jem.160.3.788

Surface proteins of Plasmodium falciparum merozoites binding to the erythrocyte receptor, glycophorin

PMCID: PMC2187389  PMID: 6206188

Abstract

Invasion of erythrocytes by the malarial parasite is a receptor- mediated process. P. falciparum merozoites recognize and bind to erythrocyte surface sialoglycoproteins, glycophorins A and B, and the glycophorins bind to saturable sites on the merozoite surface. The purpose of the present work was to identify a receptor or ligand molecule on the merozoite surface that mediates binding to the erythrocyte. A fraction containing the sialoglycoproteins was coupled to an acrylamide matrix and incubated with metabolically labeled merozoites. A merozoite protein of 155 kD that labeled prominently with [3H]glycine bound to glycophorin. A minor protein of 130 kD also bound. Both proteins are rich in proline and glycine, poor in methionine, and may be related. The proteins are also stable to heating to 100 degrees C for 10 min. Immunoelectron microscopy demonstrated that the 155 kD and 130 kD proteins are located on the merozoite surface coat. The antibodies significantly inhibited merozoite invasion into erythrocytes and also binding of the proteins to the glycophorin-matrix. The specific binding of the 155-kD and 130-kD proteins to the erythrocyte receptor and the demonstration that they are located on the merozoite surface suggest they could be receptor proteins that mediate binding of the merozoite to the erythrocyte surface.

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Selected References

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  1. Aikawa M., Miller L. H., Johnson J., Rabbege J. Erythrocyte entry by malarial parasites. A moving junction between erythrocyte and parasite. J Cell Biol. 1978 Apr;77(1):72–82. doi: 10.1083/jcb.77.1.72. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Bendayan M., Roth J., Perrelet A., Orci L. Quantitative immunocytochemical localization of pancreatic secretory proteins in subcellular compartments of the rat acinar cell. J Histochem Cytochem. 1980 Feb;28(2):149–160. doi: 10.1177/28.2.7354212. [DOI] [PubMed] [Google Scholar]
  3. Breuer W. V., Kahane I., Baruch D., Ginsburg H., Cabantchik Z. I. Role of internal domains of glycophorin in Plasmodium falciparum invasion of human erythrocytes. Infect Immun. 1983 Oct;42(1):133–140. doi: 10.1128/iai.42.1.133-140.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Coppel R. L., Cowman A. F., Lingelbach K. R., Brown G. V., Saint R. B., Kemp D. J., Anders R. F. Isolate-specific S-antigen of Plasmodium falciparum contains a repeated sequence of eleven amino acids. Nature. 1983 Dec 22;306(5945):751–756. doi: 10.1038/306751a0. [DOI] [PubMed] [Google Scholar]
  5. Facer C. A. Erythrocyte sialoglycoproteins and Plasmodium falciparum invasion. Trans R Soc Trop Med Hyg. 1983;77(4):524–530. doi: 10.1016/0035-9203(83)90130-x. [DOI] [PubMed] [Google Scholar]
  6. Freeman R. R., Holder A. A. Surface antigens of malaria merozoites. A high molecular weight precursor is processed to an 83,000 mol wt form expressed on the surface of Plasmodium falciparum merozoites. J Exp Med. 1983 Nov 1;158(5):1647–1653. doi: 10.1084/jem.158.5.1647. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Furthmayr H. Glycophorins A, B, and C: a family of sialoglycoproteins. Isolation and preliminary characterization of trypsin derived peptides. J Supramol Struct. 1978;9(1):79–95. doi: 10.1002/jss.400090109. [DOI] [PubMed] [Google Scholar]
  8. Hamaguchi H., Cleve H. Solubilization of human erythrocyte membrane glycoproteins and separation of the MN glycoprotein from a glycoprotein with I, S, and A activity. Biochim Biophys Acta. 1972 Sep 29;278(2):271–280. doi: 10.1016/0005-2795(72)90232-2. [DOI] [PubMed] [Google Scholar]
  9. Holder A. A., Freeman R. R. Biosynthesis and processing of a Plasmodium falciparum schizont antigen recognized by immune serum and a monoclonal antibody. J Exp Med. 1982 Nov 1;156(5):1528–1538. doi: 10.1084/jem.156.5.1528. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Howard R. J., Haynes J. D., McGinniss M. H., Miller L. H. Studies on the role of red blood cell glycoproteins as receptors for invasion by Plasmodium falciparum merozoites. Mol Biochem Parasitol. 1982 Nov;6(5):303–315. doi: 10.1016/0166-6851(82)90063-9. [DOI] [PubMed] [Google Scholar]
  11. Jungery M., Boyle D., Patel T., Pasvol G., Weatherall D. J. Lectin-like polypeptides of P. falciparum bind to red cell sialoglycoproteins. Nature. 1983 Feb 24;301(5902):704–705. doi: 10.1038/301704a0. [DOI] [PubMed] [Google Scholar]
  12. Langreth S. G., Jensen J. B., Reese R. T., Trager W. Fine structure of human malaria in vitro. J Protozool. 1978 Nov;25(4):443–452. doi: 10.1111/j.1550-7408.1978.tb04167.x. [DOI] [PubMed] [Google Scholar]
  13. Miller L. H., McAuliffe F. M., Mason S. J. Erythrocyte receptors for malaria merozoites. Am J Trop Med Hyg. 1977 Nov;26(6 Pt 2):204–208. doi: 10.4269/ajtmh.1977.26.204. [DOI] [PubMed] [Google Scholar]
  14. Nabi Z. F., Rabinovitch M. Inhibition by superoxide dismutase and catalase of the damage of isolated Leishmania mexicana amazonensis by phenazine methosulfate. Mol Biochem Parasitol. 1984 Mar;10(3):297–303. doi: 10.1016/0166-6851(84)90028-8. [DOI] [PubMed] [Google Scholar]
  15. Nardin E. H., Nussenzweig V., Nussenzweig R. S., Collins W. E., Harinasuta K. T., Tapchaisri P., Chomcharn Y. Circumsporozoite proteins of human malaria parasites Plasmodium falciparum and Plasmodium vivax. J Exp Med. 1982 Jul 1;156(1):20–30. doi: 10.1084/jem.156.1.20. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Pasvol G., Wilson R. J., Smalley M. E., Brown J. Separation of viable schizont-infected red cells of Plasmodium falciparum from human blood. Ann Trop Med Parasitol. 1978 Feb;72(1):87–88. doi: 10.1080/00034983.1978.11719283. [DOI] [PubMed] [Google Scholar]
  17. Perkins M. E. Binding of glycophorins to Plasmodium falciparum merozoites. Mol Biochem Parasitol. 1984 Jan;10(1):67–78. doi: 10.1016/0166-6851(84)90019-7. [DOI] [PubMed] [Google Scholar]
  18. Perkins M. E. Receptor mediated endocytosis of the malarial parasite by erythrocytes. Prog Clin Biol Res. 1984;165:361–376. [PubMed] [Google Scholar]
  19. Perkins M. Inhibitory effects of erythrocyte membrane proteins on the in vitro invasion of the human malarial parasite (Plasmodium falciparum) into its host cell. J Cell Biol. 1981 Sep;90(3):563–567. doi: 10.1083/jcb.90.3.563. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Perrin L. H., Dayal R. Immunity to asexual erythrocytic stages of Plasmodium falciparum: role of defined antigens in the humoral response. Immunol Rev. 1982;61:245–269. doi: 10.1111/j.1600-065x.1982.tb00379.x. [DOI] [PubMed] [Google Scholar]
  21. Trager W., Jensen J. B. Human malaria parasites in continuous culture. Science. 1976 Aug 20;193(4254):673–675. doi: 10.1126/science.781840. [DOI] [PubMed] [Google Scholar]
  22. Wilson R. J., McGregor I. A., Wilson M. E. The stability and fractionation of malarial antigens from the blood of Africans infected with Plasmodium falciparum. Int J Parasitol. 1973 Jul;3(4):511–520. doi: 10.1016/0020-7519(73)90048-9. [DOI] [PubMed] [Google Scholar]
  23. Wilson R. J. Serotyping Plasmodium falciparum malaria with S-antigens. Nature. 1980 Apr 3;284(5755):451–452. doi: 10.1038/284451a0. [DOI] [PubMed] [Google Scholar]

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