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Interaction between cFLIP L and Itch, a ubiquitin ligase, is obstructed in Trypanosoma cruzi ‐infected human cells
Author(s) -
Murata Eri,
Hashimoto Muneaki,
Aoki Takashi
Publication year - 2008
Publication title -
microbiology and immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.664
H-Index - 70
eISSN - 1348-0421
pISSN - 0385-5600
DOI - 10.1111/j.1348-0421.2008.00073.x
Subject(s) - biology , trypanosoma cruzi , ubiquitin ligase , ubiquitin , chagas disease , microbiology and biotechnology , virology , immunology , biochemistry , parasite hosting , gene , world wide web , computer science
Death receptor‐mediated host cell apoptosis, a defense strategy for elimination by the immune system of parasite‐infected cells, is inhibited by Trypanosoma cruzi , the causative agent of Chagas' disease. It has previously been reported by us that, in infected cells, T. cruzi upregulates and exploits cFLIP L , a mammalian inhibitor of death receptor signaling. Here it is shown that ubiquitination of cFLIP L, leading to proteasomal degradation, is inhibited in parasite‐infected cells. The extent of expression of Itch, a protein thought to be an ubiquitin ligase for cFLIP L , was found to be equivalent in T. cruzi ‐infected and in uninfected cells. However, co‐immunoprecipitation analysis showed that the interaction between cFLIP L and Itch is strongly inhibited in T. cruzi ‐infected cells. This unique parasite strategy, which has not been reported in any other pathogen‐infected cells, may allow the host cell to accumulate cFLIP L , eventually resulting in the inhibition of apoptosis of T. cruzi ‐infected cells.