In a previous article, we demonstrated that the cytoskeleton of this parasite is extensively glutamylated but, paradoxically, overexpression or inhibition of polyglutamylase expression have limited visible cellular consequences.

In terms of cell death, an apoptotic phenotype has been characterized in Leishmania but the pathways remain unknown, being devoid of key mammal cell death proteins. For example, the major cytoskeletal components of these parasites are microtubules, which form a subpellicular corset. Leishmania are unique unicellular organisms in terms of cytoskeleton organization and mechanisms of cell death. This emphasizes the role of post-translational modifications in cell biology, inducing cell death or cell survival of infectious agents. A balance seems to be established between polyglutamylation and deglutamylation, with imbalance inducing microtubule or other protein modifications characterizing either cell death if polyglutamylation was prioritized, or the cell survival process of autophagy if deglutamylation was prioritized.

We have shown that Leishmania apoptosis was linked to polyglutamylation and hypothesized that the cell survival process autophagy was linked to deglutamylation. In this article, we have studied the role of the post-translational modifications, deglutamylation and polyglutamylation, in Leishmania. And Trypanosomatids have an apoptotic phenotype under cell death conditions, but the pathways involved are devoid of key mammal proteins such as caspases or death receptors, and the triggers involved in apoptotic induction remain unknown. Oddly, the actin network appears structurally and functionally different from other eukaryotic actins. Most of the Trypanosomatid cytoskeleton consists of microtubules, forming different substructures including a subpellicular corset. Trypanosomatids are flagellated protozoan parasites that are very unusual in terms of cytoskeleton organization but also in terms of cell death.

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