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Science 29 March 1985:
Vol. 227. no. 4694, pp. 1593 - 1597
DOI: 10.1126/science.3883491
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Articles

Science, Vol 227, Issue 4694, 1593-1597
Copyright © 1985 by American Association for the Advancement of Science

articles

Isolation of the gene for a glycophorin-binding protein implicated in erythrocyte invasion by a malaria parasite

JV Ravetch, J Kochan, and M Perkins

Plasmodium falciparum, the most lethal of the malarial parasites that infect humans, undergoes three cycles of development in its vertebrate host and elicits stage-specific immune responses. This stage specificity of the immune response has made it difficult to isolate antigens that would be useful in developing a vaccine against malaria. A complementary DNA clone for a glycophorin-binding protein of Plasmodium falciparum merozoites has been isolated and characterized. The protein interacts with glycophorin, the erythrocyte receptor, during invasion of the host cell by the parasite. Antigenic determinants of this protein expressed in Escherichia coli have been used to produce antibodies to a glycophorin-binding protein. The antibodies show schizont-specific immunofluorescence and react with the merozoite protein. The primary sequence of these determinants reveals a 150-nucleotide tandem-repeating sequence coding for a 50-amino-acid repeat. The characterization of the Plasmodium falciparum glycophorin-binding protein represents one approach toward designing serologic agents to block the parasite's development in the vertebrate host.


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Perturbation of red cell membrane structure during intracellular maturation of Plasmodium falciparum.
T. Taraschi, A Parashar, M Hooks, and H Rubin (1986)
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Circumsporozoite protein of Plasmodium vivax: gene cloning and characterization of the immunodominant epitope.
D. Arnot, J. Barnwell, J. Tam, V Nussenzweig, R. Nussenzweig, and V Enea (1985)
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