T. Blisnick et al., Pfsbp 1, a Maurer's cleft Plasmodium falciparum protein, is associated with the erythrocyte skeleton, MOL BIOCH P, 111(1), 2000, pp. 107-121
Antibodies from hyperimmune monkey sera, selected by absorption to Plasmodi
um falciparum-infected erythrocytes, and elution at acidic pH, allowed us t
o characterize a novel parasite protein, Pfsbp1 (P. falciparum skeleton bin
ding protein 1). Pfsbp1 is an integral membrane protein of parasite-induced
membranous structures associated with the erythrocyte plasma membrane and
referred to as Maurer's clefts. The carboxy-terminal domain of Pfsbp1, expo
sed within the cytoplasm of the host cell, interacts with a 35 kDa erythroc
yte skeletal protein and might participate in the binding of the Maurer's c
lefts to the erythrocyte submembrane skeleton. Antibodies to the carboxy- a
nd amino-terminal domains of Pfsbp1 labelled similar vesicular structures i
n the cytoplasm of Plasmodium chabaudi and Plasmodium berghei-infected muri
ne erythrocytes, suggesting that the protein is conserved among malaria spe
cies, consistent with an important role of Maurer's cleft-like structures i
n the intraerythrocytic development of malaria parasites. (C) 2000 Elsevier
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