Trypanosoma cruzi: High ribosomal resistance to trichosanthin inactivation

Trypanosoma cruzi is the parasite causing Chagas Disease. Several results already published suggest that T. cruzi ribosomes have remarkable differences with their mammalian counterparts. In the present work, we showed that trypanosomatid (T. cruzi and Crithidia fasciculata) ribosomes are highly resi...

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Bibliographic Details
Published in:Experimental parasitology 2008-03, Vol.118 (3), p.442-447
Main Authors: Juri Ayub, Maximiliano, Ma, Kit-Wan, Shaw, Pang-Chui, Wong, Kam-Bo
Format: Article
Language:English
Subjects:
Animals
Antiparasitic Agents - pharmacology
Biological and medical sciences
Chagas Disease
Crithidia fasciculata
Crithidia fasciculata - drug effects
Crithidia fasciculata - ultrastructure
Drug Resistance
Fundamental and applied biological sciences. Psychology
Life cycle. Host-agent relationship. Pathogenesis
Liver - ultrastructure
Protein Biosynthesis - drug effects
Protein synthesis
Protozoa
Rats
Ribosome-inactivating protein (RIP)
Ribosomes - drug effects
Trichosanthin
Trichosanthin - pharmacology
Trypanosoma
Trypanosoma cruzi
Trypanosoma cruzi - drug effects
Trypanosoma cruzi - ultrastructure
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Summary:Trypanosoma cruzi is the parasite causing Chagas Disease. Several results already published suggest that T. cruzi ribosomes have remarkable differences with their mammalian counterparts. In the present work, we showed that trypanosomatid (T. cruzi and Crithidia fasciculata) ribosomes are highly resistant to inactivation by trichosanthin (TCS), which is active against mammalian ribosomes. Differential resistance is an intrinsic feature of the ribosomal particles, as demonstrated by using assays where the only variable was the ribosomes source. Because we have recently described that TCS interacts with the acidic C-terminal end of mammalian ribosomal P proteins, we assayed the effect of a TCS variant, which is unable to interact with P proteins, on trypanosomatid ribosomes. This mutant showed similar shifting of IC50 values on rat, T. cruzi and C. fasciculata ribosomes, suggesting that the resistance mechanism might involve other ribosomal components rather than the C-terminal end of P proteins.
ISSN:0014-4894
1090-2449
DOI:10.1016/j.exppara.2007.09.002