Thus, in Leishmania, the TOR kinase family has expanded to encompass a unique role in AC function and biology, one that is essential for parasite survival in the mammalian infective stage. Correspondingly, tor3- mutants showed defects in osmoregulation and were sensitive to starvation for glucose but not amino acids, glucose being a limiting nutrient in the parasitophorous vacuole. The loss of virulence was associated with a defect in acidocalcisome formation, as this unique organelle was grossly altered in tor3- mutants and no longer accumulated polyphosphates. Significantly, tor3(-) mutants were unable to survive or replicate in macrophages in vitro, or to induce pathology or establish infections in mice in vivo. In contrast, tor3(-) null mutants were readily obtained while exhibiting somewhat slower growth, tor3(-) maintained normal morphology, rapamycin sensitivity, and differentiation into the animal-infective metacyclic stage. Consistent with the essential roles of TOR complexes in other organisms, we were unable to generate null TOR1 or TOR2 mutants in cultured L. Database mining revealed three TOR kinases in the trypanosomatid parasite Leishmania major, as defined by homology to the phosphoinositide 3-kinase-related kinase (PIKK) family and a signature conserved FKBP12/rapamycin-binding domain.
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