Plasmodium falciparum: pfalhesin and CD36 form an adhesin/receptor pair that is responsible for the pH-dependent portion of cytoadherence/sequestration.
The cytoadherent behavior of two Plasmodium falciparum (human malaria) cell lines, FCR-3 and ITO4 (a cell line with elevated ICAM-1 adherence), was studied using CHO cells transfected with CD36 or ICAM-1 receptors as target cells. ICAM-1-mediated adherence was found to be relatively pH insensitive, whereas CD36-mediated adherence was pH sensitive and inhibited by monoclonal antibodies and peptides based on a region found in human band 3 protein and named pfalhesin. Immobilized pfalhesin was used as an affinity matrix to purify CD36 from extracts of C32 amelanotic melanoma cells, which have ICAM-1 as well as CD36 receptors, and bind both parasite cell lines. We conclude that pfalhesin and CD36 constitute an adhesin/receptor pair.
Crandall
I
I
Department of Biology, University of California, Riverside 92521.
Land
K M
KM
Sherman
I W
IW
D000595:Amino Acid Sequence; D000818:Animals; D001457:Anion Exchange Protein 1, Erythrocyte / Q000502:physiology*; D015703:Antigens, CD / Q000502:physiology*; D018955:CD36 Antigens; D016466:CHO Cells; D002448:Cell Adhesion; D015815:Cell Adhesion Molecules / Q000502:physiology; D006224:Cricetinae; D004912:Erythrocytes / Q000469:parasitology*; D006801:Humans; D006863:Hydrogen-Ion Concentration; D015151:Immunoblotting; D018799:Intercellular Adhesion Molecule-1; D018328:Melanoma, Amelanotic; D008969:Molecular Sequence Data; D010963:Plasmodium falciparum / Q000502:physiology*; D014407:Tumor Cells, Cultured
D001457:Anion Exchange Protein 1, Erythrocyte; D015703:Antigens, CD; D018955:CD36 Antigens; D015815:Cell Adhesion Molecules; C086125:pfalhesin; D018799:Intercellular Adhesion Molecule-1