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Cytoadherence of knobby and knobless Plasmodium falciparum-infected erythrocytes

Published online by Cambridge University Press:  06 April 2009

W. Ruangjirachuporn
Affiliation:
Department of Immunology, Stockholm University, S-106 91 Stockholm, Sweden Department of Ultrastructure Research, Stockholm University, S-106 91 Stockholm, Sweden
B. A. Afzelius
Affiliation:
Department of Ultrastructure Research, Stockholm University, S-106 91 Stockholm, Sweden
S. Paulie
Affiliation:
Department of Immunology, Stockholm University, S-106 91 Stockholm, Sweden
M. Wahlgren
Affiliation:
Department of Immunology, Stockholm University, S-106 91 Stockholm, Sweden
K. Berzins
Affiliation:
Department of Immunology, Stockholm University, S-106 91 Stockholm, Sweden
P. Perlmann
Affiliation:
Department of Immunology, Stockholm University, S-106 91 Stockholm, Sweden

Extract

Cytoadherence of Plasmodium falciparum-infected erythrocytes to melanoma cells was analysed using strains or isolates of parasites expressing or not expressing knobs (K+ or K phenotype) on the erythrocyte surface. Both K+ and K parasites had the capacity to cytoadhere to melanoma cells. Using a panel of melanoma cell lines with different surface expression of the cytoadherence receptors CD36, thrombospondin and ICAM-1 indicated that CD36 was the major receptor for parasites of both K+ and K phenotypes. Binding competition experiments between K+ and K-infected erythrocytes suggested that K+ cytoadherence is of higher affinity than that of K parasites. However, some K cytoadherence was also found in isolates containing mixed populations of K+ and K parasites. The interaction of the two types of infected erythrocytes with melanoma cells also differed ultrastructurally, erythrocytes of K+ phenotype showing intimate interdigitations with microvilli on the melanoma cells, while erythrocytes of K phenotype displayed more separated interactions with fewer sites of contact and involving only a few melanoma cell microvilli. One and the same infected erythrocyte may co-express the ligand for CD36-mediated cytoadherence and the structures mediating binding of uninfected erythrocytes to form rosettes.

Type
Research Article
Copyright
Copyright © Cambridge University Press 1991

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