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Infection and Immunity, July 2000, p. 3923-3926, Vol. 68, No. 7
0019-9567/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Identification of Glycosaminoglycan Binding Domains in Plasmodium falciparum Erythrocyte Membrane Protein 1 of a Chondroitin Sulfate A-Adherent Parasite

John C. Reeder,1,* Anthony N. Hodder,1 James G. Beeson,1 and Graham V. Brown2

Walter and Eliza Hall Institute of Medical Research, Parkville, Victoria 3050,1 and Department of Medicine, University of Melbourne, Parkville, Victoria 3052,2 Australia

Received 22 February 2000/Accepted 15 April 2000

Accumulation of Plasmodium falciparum-infected erythrocytes in the placenta is a key feature of maternal malaria. This process is mediated in part by the parasite ligand P. falciparum erythrocyte membrane protein 1 (PfEMP1) at the surface of the infected erythrocyte interacting with the host receptor chondroitin sulfate A (CSA) on the placental lining. We have localized CSA binding activity to two adjacent domains in PfEMP1 of an adherent parasite line and shown the presence of at least three active glycosaminoglycan binding sites. A putative CSA binding sequence was identified in one domain, but nonlinear binding motifs are also likely to be present, since binding activity in the region was shown to be dependent on conformation. Characterization of this binding region provides an opportunity to investigate further its potential as a target for antiadhesion therapy.

* Corresponding author. Present address: Papua New Guinea Institute of Medical Research, PO Box 60, Goroka EHP 441, Papua New Guinea. Phone: 675-732-1469. Fax: 675-732-1198. E-mail: imrgka{at}datec.com.pg.

Infection and Immunity, July 2000, p. 3923-3926, Vol. 68, No. 7
0019-9567/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


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