5 research outputs found
<i>PFPI</i>-like genes are expressed in <i>Leishmania major</i> but are pseudogenes in other <i>Leishmania</i> species
<i>Pyrococcus furiosus</i> protease I (PFPI) is a multimeric cysteine peptidase from <i>P. furiosus</i>. Genome analyses indicate that orthologues are present in rather few other organisms, including <i>Dictyostelium discoideum</i> and several bacteria, Archaea and plants. An open reading frame (ORF) coding for a PFPI-like protein (PFP1) was identified in <i>Leishmania</i> major and <i>Leishmania mexican</i> and full-length spliced and polyadenylated <i>PFP1</i> mRNA detected for both species. Vestiges of a PFPI-like gene could also be identified in <i>Leishmania braziliensis</i> and <i>Leishmania infantum</i>, but no ORF remains owing to the presence of frame-shifts and stop codons. No evidence for a <i>PFPI</i>-like gene could be found in the syntenic region of <i>Trypanosoma brucei</i> or <i>Trypanosoma cruzi</i>, raising the possibility that the <i>PFPI</i>-like genes were acquired by a lateral gene transfer event after the divergence of trypanosomes and <i>Leishmania</i>. The gene may have subsequently degenerated into a pseudogene in some <i>Leishmania</i> species, owing to the loss of relevant biological function. However, antibodies raised against <i>L. mexicana</i> recombinant protein detected PFP1 in promastigote extracts of <i>L. major</i>, but not in <i>L. Mexicana</i> promastigote or amastigote extracts. The expression of <i>PFP1</i> in <i>L. major</i> suggests that PFP1 might contribute to the disease tropism that distinguishes this <i>Leishmania</i> species from others