Interaction between cFLIPL and Itch,a ubiquitin ligase,is obstructed in Trypanosoma cruzi‐infected human cells |
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Authors: | Eri Murata Muneaki Hashimoto Takashi Aoki |
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Institution: | Department of Molecular and Cellular Parasitology, Juntendo University School of Medicine, 2‐1‐1 Hongo, Bunkyo‐ku, Tokyo, 113‐8421, Japan |
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Abstract: | 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 cFLIPL, a mammalian inhibitor of death receptor signaling. Here it is shown that ubiquitination of cFLIPL, 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 cFLIPL, was found to be equivalent in T. cruzi‐infected and in uninfected cells. However, co‐immunoprecipitation analysis showed that the interaction between cFLIPL 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 cFLIPL, eventually resulting in the inhibition of apoptosis of T. cruzi‐infected cells. |
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Keywords: | cFLIPL Itch Trypanosoma cruzi ubiquitin |
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