Abstract
Far-upstream element-binding protein 2 (FBP2) is an internal ribosomal entry site (IRES) trans-acting factor (ITAF) that negatively regulates enterovirus 71 (EV71) translation. This study shows that EV71 infection cleaved FBP2. Live EV71 and the EV71 replicon (but not UV-inactivated virus particles) induced FBP2 cleavage, suggesting that viral replication results in FBP2 cleavage. The results also showed that virus-induced proteasome, autophagy, and caspase activity co-contribute to EV71-induced FBP2 cleavage. Using FLAG-fused FBP2, we mapped the potential cleavage fragments of FBP2 in infected cells. We also found that FBP2 altered its function when its carboxyl terminus was cleaved. This study presents a mechanism for virus-induced cellular events to cleave a negative regulator for viral IRES-driven translation.
Original language | English |
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Pages (from-to) | 3828-3838 |
Number of pages | 11 |
Journal | Journal of Virology |
Volume | 87 |
Issue number | 7 |
DOIs | |
Publication status | Published - Apr 2013 |
ASJC Scopus subject areas
- Microbiology
- Immunology
- Insect Science
- Virology