Key result
Enterovirus 71 infection induces the cleavage of Far-upstream element-binding protein 2 (FBP2), a negative regulator of viral translation, via proteasome, autophagy, and caspase activity.
EV71 infection promotes its own translation by cleaving FBP2, a host negative regulator, via multiple cellular degradation pathways.
EV71 FBP2 cleavage in cells may alter viral translation; leaves open any role in human disease or therapy.
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.
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Chen et al. (2013) studied Enterovirus 71 infection. Enterovirus 71 (EV71) infection vs. UV-inactivated virus particles was evaluated on FBP2 cleavage. Enterovirus 71 infection induces the cleavage of Far-upstream element-binding protein 2 (FBP2), a negative regulator of viral translation, via proteasome, autophagy, and caspase activity.
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