Abstract
BackgroundLeishmania spp., in the course of their parasitic life cycle, encounter two vastly different environments: the gut of sandflies and the phagosomes of mammalian macrophages. During transmission into a mammal, the parasites are exposed to increased ambient temperature as well as to different carbon sources. Molecular chaperones or heat shock proteins are implicated in the necessary adaptations which involve the ordered differentiation from the flagellated, extracellular promastigote to the intracellular amastigote stage.ResultsHere, we show that the Leishmania donovani co-chaperonin, CPN10, is synthesised to a significantly increased concentration during in vitro differentiation to the amastigote stage. We show by fluorescence microscopy and by immunogold electron microscopy that, like its putative complex partner CPN60.2, CPN10 is localised to the single, tubular mitochondrion of the parasites and, moreover, that it co-precipitates with CPN60.2, the major mitochondrial chaperonin of Leishmania spp..ConclusionOur data indicate an increased requirement for CPN10 in the context of mitochondrial protein folding during or early in the mammalian stage of this pathogen. Moreover, they confirm the CPN60.2 as bona fide mitochondrial GroEL homologue in L. donovani and the postulated interaction of eukaryotic chaperonins, CPN60 and CPN10.
Highlights
Leishmania spp., in the course of their parasitic life cycle, encounter two vastly different environments: the gut of sandflies and the phagosomes of mammalian macrophages
To better understand mitochondrial protein chaperoning during the leishmanial life cycle, we identified the CPN10 gene of Leishmania donovani, determined its abundance in the two life cycle stages, and analysed the subcellular localisation of the gene product and its association with CPN60.2
Oligonucleotides CPN10.1 to CPN10.4 were designed according to the codon bias of Leishmania spp
Summary
Leishmania spp., in the course of their parasitic life cycle, encounter two vastly different environments: the gut of sandflies and the phagosomes of mammalian macrophages. Molecular chaperones or heat shock proteins are implicated in the necessary adaptations which involve the ordered differentiation from the flagellated, extracellular promastigote to the intracellular amastigote stage. The kinetoplast is part of a tubular, single mitochondrion that shows little morphological likeness to the mitochondria of Crown Group Eukaryota. The parasites of the genus Leishmania exist in two morphologically distinct life cycle stages. The amastigote, a rounded, intracellular form, with no protruding flagellum, persists in the phagosomes of mammalian macrophages and at temperatures of up to 39°C. The difference of temperatures in the two environments triggers the respective stage development [1], and poses a challenge to the system of protein chaperones. At least two heat shock proteins, Hsp100 and CPN60.2, show significantly induced abundance during the amastigote stage [2,3,4]
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