| Summary: | Calcineurin (CaN) is present in all eukaryotic cells, including intracellular trypanosomatid parasites such as <i>Trypanosoma cruzi</i> (<i>Tc</i>) and <i>Leishmania</i> spp. (<i>L</i>spp). In this study, we performed an in silico analysis of the CaN subunits, comparing them with the human (<i>Hs</i>) and looking their structure, post-translational mechanisms, subcellular distribution, interactors, and secretion potential. The differences in the structure of the domains suggest the existence of regulatory mechanisms and differential activity between these protozoa. Regulatory subunits are partially conserved, showing differences in their Ca<sup>2+</sup>-binding domains and myristoylation potential compared with human CaN. The subcellular distribution reveals that the catalytic subunits <i>Tc</i>CaNA1, <i>Tc</i>CaNA2, <i>L</i>sppCaNA1, <i>L</i>sppCaNA1_var, and <i>L</i>sppCaNA2 associate preferentially with the plasma membrane compared with the cytoplasmic location of <i>Hs</i>CaNAα. For regulatory subunits, <i>Hs</i>CaNB-1 and <i>L</i>sppCaNB associate preferentially with the nucleus and cytoplasm, and <i>Tc</i>CaNB with chloroplast and cytoplasm. Calpain cleavage sites on CaNA suggest differential processing. CaNA and CaNB of these trypanosomatids have the potential to be secreted and could play a role in remote communication. Therefore, this background can be used to develop new drugs for protozoan pathogens that cause neglected disease.
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