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Science 17 March 1989:
Vol. 243. no. 4897, pp. 1469 - 1471
DOI: 10.1126/science.2467377
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Articles

Science, Vol 243, Issue 4897, 1469-1471
Copyright © 1989 by American Association for the Advancement of Science

articles

Identification of a platelet membrane glycoprotein as a falciparum malaria sequestration receptor

CF Ockenhouse, NN Tandon, C Magowan, GA Jamieson, and JD Chulay

Department of Immunology, Walter Reed Army Institute of Research, Washington, DC 20307.

Infections with the human malaria parasite Plasmodium falciparum are characterized by sequestration of erythrocytes infected with mature forms of the parasite. Sequestration of infected erythrocytes appears to be critical for survival of the parasite and to mediate immunopathological abnormalities in severe malaria. A leukocyte differentiation antigen (CD36) was previously suggested to have a role in sequestration of malaria-infected erythrocytes. CD36 was purified from platelets, where it is known as GPIV, and was shown to be a receptor for binding of infected erythrocytes. Infected erythrocytes adhered to CD36 immobilized on plastic; purified CD36 exhibited saturable, specific binding to infected erythrocytes; and purified CD36 or antibodies to CD36 inhibited and reversed binding of infected erythrocytes to cultured endothelial cells and melanoma cells in vitro. The portion of the CD36 molecule that reverses cytoadherence may be useful therapeutically for rapid reversal of sequestration in cerebral malaria.


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