Proteins containing WD40 domains play important roles in the formation of multiprotein complexes. Little is known about WD40 proteins in the malaria parasite. This report contains the initial description of a WD40 protein that is unique to the genus Plasmodium and possibly closely related genera.
View Article and Find Full Text PDFThe malarial parasite remodels the host erythrocyte following invasion. Well-known examples are adhesive proteins inserted into the host erythrocyte membrane, which function as virulence factors. The modification of the host erythrocyte may be mediated by a specialized domain of the endoplasmic reticulum, or export compartment (PEC).
View Article and Find Full Text PDFMerozoite release from infected erythrocytes is a complex process, which is still not fully understood. Such process was characterised at ultra-structural level in this work by labelling erythrocyte membrane with a fluorescent lipid probe and subsequent photo-conversion into an electron-dense precipitate. A lipophilic DiIC(16) probe was inserted into the infected erythrocyte surface and the transport of this phospholipid analogue through the erythrocyte membrane was followed up during 48 h of the asexual erythrocyte cycle.
View Article and Find Full Text PDFMonoclonal antibodies recognizing proteins localized to a unique subcellular compartment within the malaria parasite are described in this report. These monoclonal antibodies recognize Plasmodium falciparum proteins of 68, 45 and 22 kDa proteins which are also conserved in rodent Plasmodium species. Co-localization studies indicate that these proteins are located in a brefeldin A-induced compartment which was previously proposed to be an early step in the export of proteins from the parasite into the infected erythrocyte.
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