Polyphosphorylated phosphoinositides (PIPs) are potent second messengers, which trigger a wide variety of signaling and trafficking events in most eukaryotic cells. However, the role and metabolism of PIPs in malaria parasite Plasmodium have remained largely unexplored. Our present studies suggest that PfPI3K, a novel phosphatidylinositol-3-kinase (PI3K) in Plasmodium falciparum, is exported to the host erythrocyte by the parasite in an active form. PfPI3K is a versatile enzyme as it can generate various 3′-phosphorylated PIPs. In the parasite, PfPI3K was localized in vesicular compartments near the membrane and in its food vacuole. PI3K inhibitors wortmannin and LY294002 were effective against PfPI3K and were used to study PfPI3K function. We found that PfPI3K is involved in endocytosis from the host and trafficking of hemoglobin in the parasite. The inhibition of PfPI3K resulted in entrapment of hemoglobin in vesicles in the parasite cytoplasm, which prevented its transport to the food vacuole, the site of hemoglobin catabolism. As a result, hemoglobin digestion, which is a source of amino acids necessary for parasite growth, was attenuated and caused the inhibition of parasite growth.

We have previously demonstrated thatToxoplasma gondii has a tyrosine-based sorting system, which mediates protein targeting to the lysosome-like rhoptry secretory organelle. We now show that rhoptry protein targeting is also dependent on a dileucine motif and occurs from a post-Golgi endocytic organelle to mature rhoptries in an adaptin-dependent fashion. TheT. gondii AP-1 adaptin complex is implicated in this transport because the μ1 chain of T. gondii AP-1 (a) was localized to multivesicular endosomes and the limiting and luminal membranes of the rhoptries; (b) bound to endocytic tyrosine motifs in rhoptry proteins, but not in proteins from dense granule secretory organelles; (c) when mutated in predicted tyrosine-binding motifs, led to accumulation of the rhoptry protein ROP2 in a post-Golgi multivesicular compartment; and (d) when depleted via antisense mRNA, resulted in accumulation of multivesicular endosomes and immature rhoptries. These are the first results to implicate AP-1 in transport from a post-Golgi compartment to a mature secretory organelle and substantially expand the role for AP-1 in anterograde protein transport.

In this present study, silver nanoparticles (Ag/AgCl NPs) were synthesized using an aqueous leaf extract of Oedera genistifolia as a reducing agent. The biosynthesized Ag/AgCl NPs was characterized by UV-visible spectrophotometry, transform infrared spectroscopy (FTIR), scanning electron microscopy (SEM), energy dispersive X-ray spectroscopy (EDX), transmission electron microscopy (TEM), X-ray diffraction (XRD), and thermogravimetric analysis (TGA). In addition, sequel to antibacterial assay, the cytotoxic effect of the phytofabricated Ag/AgCl NPs was assessed against the HeLa cell line (human cervix adenocarcinoma). The results of the characterization of the synthesized Ag/AgCl NPs indicate the successful synthesis using plant extract as a reducing agent, with UV-Vis spectra between 290–360 nm. TEM results showed that Ag/AgCl NPs was spherical in shape with an average size of 34.2 nm. EDX analysis revealed that the particles were predominantly composed of carbon, oxygen, chlorine, and silver, while FTIR identified major phytochemical compounds, which could be responsible for bio-reducing and capping potential. XRD analysis showed the crystallinity of Ag/AgCl NPs, with a face-centred cubic structure. The studied Ag/AgCl NPs had no cytotoxic effect on HeLa cells and exhibited antibacterial activity (minimum inhibitory concentration (MIC) 0.25–1 mg/mL; minimum bactericidal concentration (MBC) 2–16 mg/mL) against both the Gram-negative and Gram-positive bacteria investigated. Findings from this study suggest that this plant as a good candidate for producing new antibacterial drugs.