Publication: Chondroitin sulfate a is a cell surface receptor for Plasmodium falciparum-infected erythrocytes
Issued Date
1995-07-01
Resource Type
ISSN
15409538
00221007
00221007
Other identifier(s)
2-s2.0-0029041333
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Mahidol University
Rights Holder(s)
SCOPUS
Bibliographic Citation
Journal of Experimental Medicine. Vol.182, No.1 (1995), 15-20
Suggested Citation
Stephen J. Rogerson, Sansanee C. Chaiyaroj, Ken Ng, John C. Reeder, Graham V. Brown Chondroitin sulfate a is a cell surface receptor for Plasmodium falciparum-infected erythrocytes. Journal of Experimental Medicine. Vol.182, No.1 (1995), 15-20. doi:10.1084/jem.182.1.15 Retrieved from: https://repository.li.mahidol.ac.th/handle/20.500.14594/17293
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Title
Chondroitin sulfate a is a cell surface receptor for Plasmodium falciparum-infected erythrocytes
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Abstract
Adherence of Plasmodium fakiparum-infected erythrocytes to cerebral postcapillary venular endothelium is believed to be a critical step in the development of cerebral malaria. Some of the possible receptors mediating adherence have been identified, but the process of adherence in vivo is poorly understood. We investigated the role of carbohydrate ligands in adherence, and we identified chondroitin sulfate (CS) as a specific receptor for P. falciparum-infected erythrocytes. Parasitized cells bound to Chinese hamster ovary (CHO) cells and C32 melanoma cells in a chondroitin sulfate-dependent manner, whereas glycosylation mutants lacking chondroitin sulfate A (CSA) supported little or no binding. Chondroitinase treatment of wild-type CHO cells reduced binding by up to 90%. Soluble CSA inhibited binding to CHO cells by 99.2 ± 0.2% at 10 mg/ml and by 72.5 ± 3.8% at 1 mg/ml, whereas a range of other glycosaminoglycans such as heparan sulfate had no effect. Parasite lines selected for increased binding to CHO cells and most patient isolates bound specifically to immobilized CSA. We conclude that P. falciparum can express or expose proteins at the surface of the infected erythrocyte that mediate specific binding to CSA. This mechanism of adherence may contribute to the pathogenesis of P. J-lciparum malaria, but has wider implications as an example of an infectious agent with the capacity to bind specifically to cell-associated or immobilized CS. © 1995, Rockefeller University Press., All rights reserved.