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Small hepatitis B surface antigen interacts with and modulates enoylâ[euro]"coenzyme A hydratase expression in hepatoma cells

Enoylâ[euro]"coenzyme A hydratase (ECHS1) is a key enzyme in the metabolism of fatty acids in mitochondria. We previously reported that hepatitis B surface antigen (HBsAg) interacted with ECHS1 in a yeast two-hybrid system. In the current study, we further examined their interaction by using GS...

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Published in:Archives of virology 2013-05, Vol.158 (5), p.1065
Main Authors: Gong, Xianqiong, Zhu, Yueyong, Dong, Jing, Chen, Jing, You, Jia, Zheng, Qi, Rao, Zilan, Mao, Qianguo, Jiang, Jiaji
Format: Article
Language:English
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Summary:Enoylâ[euro]"coenzyme A hydratase (ECHS1) is a key enzyme in the metabolism of fatty acids in mitochondria. We previously reported that hepatitis B surface antigen (HBsAg) interacted with ECHS1 in a yeast two-hybrid system. In the current study, we further examined their interaction by using GST pull-down and co-immunoprecipitation assays. The results confirmed that small hepatitis B surface antigen (SHBs) interacted with ECHS1. Furthermore, confocal imaging showed that SHBs and ECHS1 co-localized in HepG2 cells. To clarify the biological function of the interaction, human hepatoma cell lines that transiently and stably expressed SHBs were generated. The expression of SHBs led to a significant decrease in ECHS1 protein levels. ECHS1 protein levels were reduced to 48.44 ±Â 7.12 % in Huh7 cells transiently expressing SHBs, and to 54.97 ±Â 3.54 % in HepG2 cells stably expressing SHBs. In conclusion, our findings suggest that SHBs interacts with ECHS1 and regulates ECHS1 protein levels in hepatoma cells.[PUBLICATION ABSTRACT]
ISSN:0304-8608
1432-8798
DOI:10.1007/s00705-012-1581-7