Thrombospondin binds falciparum malaria parasitized erythrocytes and may mediate cytoadherence.

Abstract:

:Plasmodium falciparum infected erythrocytes containing mature trophozoites and schizonts sequester along venular endothelium and are not in the peripheral circulation of patients with malaria. Knobs appear on infected erythrocytes and are the points of attachment to endothelium. Sequestration may protect the parasite from splenic destruction and may play a role in the pathogenesis of cerebral malaria. Correlates of sequestration have been developed in vitro using cultured human endothelium and an amelanotic melanoma cell line. Knobless strains (K-) of P. falciparum fail to sequester in vivo and to bind to cells in vitro. We now present evidence that the receptor for cytoadherence is the glycoprotein, thrombospondin. Aotus monkey or human erythrocytes containing knobby (K+) but not Aotus erythrocytes containing knobless strains of P. falciparum bind to immobilized thrombospondin. Neither binds to the adhesive proteins laminin, fibronectin, factor VIII/von Willebrand factor or vitronectin. Both soluble thrombospondin and anti-thrombospondin antibodies inhibit binding of parasitized Aotus erythrocytes to immobilize thrombospondin and to melanoma cells which secrete thrombospondin.

journal_name

Nature

journal_title

Nature

authors

Roberts DD,Sherwood JA,Spitalnik SL,Panton LJ,Howard RJ,Dixit VM,Frazier WA,Miller LH,Ginsburg V

doi

10.1038/318064a0

subject

Has Abstract

pub_date

1985-11-07 00:00:00

pages

64-6

issue

6041

eissn

0028-0836

issn

1476-4687

journal_volume

318

pub_type

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