Eimeria falciformis.

species (>1700) are widespread causative agents of coccidiosis in animals. Most species reproduce in the intestinal epithelial cells of distinct hosts. infects the cecum of for its asexual and sexual reproduction.

Apically-located P4-ATPase1-Lem1 complex internalizes phosphatidylserine and regulates motility-dependent invasion and egress in .

The membrane asymmetry regulated by P4-ATPases is crucial for the functioning of eukaryotic cells. The underlying spatial translocation or flipping of specific lipids is usually assured by respective P4-ATPases coupled to conforming non-catalytic subunits. Our previous work has identified five P4-ATPases (P4-ATPase1-5) and three non-catalytic partner proteins (Lem1-3) in the intracellular protozoan pathogen, .

Aminoglycerophospholipid flipping and P4-ATPases in Toxoplasma gondii.

Lipid flipping in the membrane bilayers is a widespread eukaryotic phenomenon that is catalyzed by assorted P4-ATPases. Its occurrence, mechanism, and importance in apicomplexan parasites have remained elusive, however. Here we show that Toxoplasma gondii, an obligate intracellular parasite with high clinical relevance, can salvage phosphatidylserine (PtdSer) and phosphatidylethanolamine (PtdEtn) but not phosphatidylcholine (PtdCho) probes from its milieu.

The protozoan parasite encodes a gamut of phosphodiesterases during its lytic cycle in human cells.

Cyclic nucleotide signaling is pivotal to the asexual reproduction of , however little do we know about the phosphodiesterase enzymes in this widespread obligate intracellular parasite. Here, we identified 18 phosphodiesterases (PDE1-18) in the parasite genome, most of which form apicomplexan-specific clades and lack archetypal regulatory motifs often found in mammalian PDEs. Genomic epitope-tagging in the tachyzoite stage showed the expression of 11 phosphodiesterases with diverse subcellular distributions.

Chimeras of P4-ATPase and Guanylate Cyclase in Pathogenic Protists.

Apicomplexan parasites harbor chimeric proteins embodying P4-type ATPase and guanylate cyclase domains. Such proteins - serving as the actuator of cGMP signaling in this group of important pathogens - are indeed unusual in terms of their sheer size, modus operandi, and evolutionary repurposing. Much like the mythological Sphinx, a human-lion chimeric creature that posed challenging riddles, the P4-type ATPase-guanylate cyclase chimeras present both structural and functional conundrums.

An unusual and vital protein with guanylate cyclase and P4-ATPase domains in a pathogenic protist.

cGMP signaling is one of the master regulators of diverse functions in eukaryotes; however, its architecture and functioning in protozoans remain poorly understood. Herein, we report an exclusive guanylate cyclase coupled with N-terminal P4-ATPase in a common parasitic protist, This bulky protein (477-kD), termed ATPase-GC to fairly reflect its envisaged multifunctionality, localizes in the plasma membrane at the apical pole of the parasite, whereas the corresponding cGMP-dependent protein kinase (PKG) is distributed in the cytomembranes. ATPase-GC is refractory to genetic deletion, and its CRISPR/Cas9-assisted disruption aborts the lytic cycle of Besides, Cre/loxP-mediated knockdown of ATPase-GC reduced the synthesis of cGMP and inhibited the parasite growth due to impairments in the motility-dependent egress and invasion events.

A plant/fungal-type phosphoenolpyruvate carboxykinase located in the parasite mitochondrion ensures glucose-independent survival of .

is considered to be one of the most successful intracellular pathogens, because it can reproduce in varied nutritional milieus, encountered in diverse host cell types of essentially any warm-blooded organism. Our earlier work demonstrated that the acute (tachyzoite) stage of depends on cooperativity of glucose and glutamine catabolism to meet biosynthetic demands. Either of these two nutrients can sustain the parasite survival; however, what determines the metabolic plasticity has not yet been resolved.

Identification of genomic heterogeneity among Lactococcus lactis strains by plasmid profiling, PFGE and 16S rDNA sequence analysis.

Lactococcus lactis strains are used commonly as starters, which contribute to desirable flavour and texture properties known as strain-specific, in dairy industry. Genomic heterogeneity of 30 L. lactis strains originating from Turkey and characterized phenotypically were investigated in this study.