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| Proteomics |
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With the publication of the complete genome sequences of
several trypanosomatids (T. brucei, T. cruzi, L. major,
L. infantum and L. brasiliensis) a proteomic
analysis of complete trypanosomes or their subcellular constituents
has become possible. Through collaborations with colleagues
in the de Duve institute (Drs. Vertommen and Rider) and
abroad, detailed proteomic analyses have been performed
on the different life-cycle stages of both T. cruzi
and L. donovani, and on subcellular fractions
of T. brucei. Analysis of highly purified glycosomes
has revealed that these organelles do not only contain several
enzymes of purine salvage, as previously reported, but they
possess a whole battery of enzymes that allow them to synthesize
nucleoside monophosphates from either their corresponding
free bases or their corresponding nucleosides.
People involved in the subject:
- Fred Opperdoes
- Paul Michels
- Jean-Pierre Szikora
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Vertommen D, Van Roy
J, Szikora JP, Rider MH, Michels PA, Opperdoes FR.
Differential expression of glycosomal and mitochondrial
proteins in the two major life-cycle stages of Trypanosoma
brucei. Mol Biochem Parasitol. 2008 Apr;158(2):189-201.
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Rosenzweig D, Smith
D, Opperdoes F, Stern S, Olafson RW, Zilberstein D.
Retooling Leishmania metabolism: from sand fly gut
to human macrophage. FASEB J. 2008 Feb;22(2):590-602.
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Atwood JA 3rd, Weatherly
DB, Minning TA, Bundy B, Cavola C, Opperdoes FR, Orlando
R, Tarleton RL. The Trypanosoma cruzi proteome. Science.
2005 Jul 15;309(5733):473-6.
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