A minimal subset of two to three residues in cyclic nucleotide binding (CNB) domains controls nucleoside vs. cyclic nucleotide specificity, repurposing PKA of certain pathogens for novel nucleoside signaling pathways or sensing.

Global relative mRNA and protein abundance in trypanosomatids can be effectively estimated at transcriptomic and proteomic scales based on protein-coding sequences alone.

A conceptual and unifying framework with a critical appraisal of lipid hijacking by microbes cycling between an arthropod vector and a mammalian host is explored.

A catalytically dead paralog activates its cognate enzyme through an allosteric mechanism that combined structural and phylogenomic analysis indicates arose through acquisition of a dimerization domain, suggesting a general model for how complex allostery evolves.

The convergent evolution of yeast Mim1/2 and trypanosomal pATOM36 enable the first demonstration of reciprocal functional rescue of two evolutionary unrelated mitochondrial biogenesis complexes belonging to two different eukaryotic supergroups.

The X-ray structure of the SAS-6 cartwheel hub from Leishmania major demonstrates that SAS-6 can be sufficient to determine centriolar cartwheel symmetry.

The activity, localization, and essentiality of TbFUT1, together with its ability to complement Leishmania parasites lacking the homologous gene, suggest the presence of an uncommon and conserved mitochondrial fucosylation pathway required for kinetoplastid parasites viability.

Why does protein kinase A respond to purine nucleosides in certain pathogens, but not to the cyclic nucleotides that activate this kinase in most other organisms?

The information for mRNAs expression level is set by codon choice in trypanosomes and requires translation to be interpreted into a turnover rate.

Using advanced volume electron microscopy, the ultrastructural and spatial organisation of Leishmania parasites strongly adhered to the gut of its sand fly vector was defined.