Leishmania ribosome

The Leishmania ribosome is a large cytosolic ribonucleoprotein complex responsible for synthesizing proteins from mRNA templates in Leishmania parasites. Its structure is highly unusual among eukaryotes, featuring a large subunit (LSU) rRNA split into six major fragments (as opposed to a single 28S rRNA in humans) that interact via specialized protein extensions and rRNA expansion segments[1][5]. This fragmentation is stabilized by unique ribosomal proteins and serves as the functional core for translation. The decoding center exhibits unique post-transcriptional modifications, including pseudouridine, influencing mRNA translation and codon bias selection during the parasite life cycle[2][3][4]. The cytosolic ribosome, not the mitochondrial one, has recently been validated as the main target of the anti-leishmanial drug paromomycin, which binds the decoding center and inhibits protein synthesis[6]. These unique structural and chemical features make the Leishmania ribosome an attractive and selective target for drug discovery aimed at treating leishmaniasis, but simultaneously present therapeutic challenges in selectivity and potential resistance.

Other names

Leishmania cytosolic ribosomeLeishmania donovani ribosomeLeishmania major ribosomeLeishmania ribosomal complex

Inhibition of cytosolic translation by binding the ribosomal decoding center, interfering with mRNA–tRNA interactions and inhibiting peptide synthesis[6] Selective binding to unique rRNA modification sites distinct from human ribosomes[6]