Electron microscopy of sporozoites of the rodent malaria parasite, Plasmodium berghei, reveals electron-dense multilaminate membranous whorls within components of the rhoptry-microneme complex after fixation with tannic acid in conjunction with glutaraldehyde. This multilaminate material, which has a dark line to dark line periodicity of approximately 5 nm, appears to be secreted from the sporozoite since it is also found adhering to the sporozoite's external surface. The material may function in sporozoite gliding motility and in invasion of host cells.ALARIA, which remains one of the most important paramodium berghei. V. In vitro effects of immune serum on sporozoites. Milit. Med., 134: 1183-1 190. 25. Vanderberg, J. P., Rhodin, J. & Yoeli, M. 1967. Electron microscopic and histochemical studies of sporozoite formation in Plasmodium berghei.
A monoclonal antibody directed against the circumsporozoite protein on the surface of Plasmodium berghei sporozoites inhibited sporozoite motility in vitro. These immobilized sporozoites could adhere to but not invade target cultured cells. Other sporozoite-immobilizing agents also inhibited sporozoite invasion into cultured cells and did not prevent sporozoite adherence. These results indicate that sporozoite invasiveness is associated with 859 on July 4, 2020 by guest http://iai.asm.org/ Downloaded from
Plasmodium falciparum-infected red blood cells (RBCs) are characterized by increases in the activity of glycolytic enzymes. Because nicotinamide adenine dinucleotide (NAD) and NAD phosphate (NADP) are cofactors in the reactions of glycolysis and pentose phosphate shunt, we have examined NAD and NADP content in P. falciparum-infected RBCs. Although NADP content was not significantly altered, NAD content was increased approximately 10-fold in infected RBCs (66% parasitemia) compared with uninfected control RBCs. To determine the mechanism for the increase in NAD content, we examined the activity of several NAD biosynthetic enzymes. It is known that normal human RBCs make NAD exclusively from nicotinic acid and lack the capacity to make NAD from nicotinamide. We demonstrate that infected RBCs have readily detectable nicotinamide phosphoribosyltransferase (NPRT), the first enzyme in the NAD biosynthetic pathway that uses nicotinamide, and abundant nicotinamide deamidase, the enzyme that converts nicotinamide to nicotinic acid, thereby indicating that infected RBCs can make NAD from nicotinamide. In addition, infected RBCs have a threefold increase in nicotinic acid phosphoribosyltransferase (NAPRT), the first enzyme in the NAD biosynthetic pathway that uses nicotinic acid. Thus, the increase in NAD content in P falciparum-infected RBCs appears to be mediated by increases in NAD synthesis from both nicotinic acid and nicotinamide.
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