Abstract
Infectious bursal disease (IBD) is an acute, highly contagious, and immunosuppressive avian disease caused by IBD virus (IBDV). Our previous report indicates that IBDV VP5 induces apoptosis via interaction with voltage-dependent anion channel 2 (VDAC2). However, the underlying molecular mechanism is still unclear. We report here that receptor of activated protein kinase C 1 (RACK1) interacts with both VDAC2 and VP5 and that they could form a complex. We found that overexpression of RACK1 inhibited IBDV-induced apoptosis in DF-1 cells and that knockdown of RACK1 by small interfering RNA induced apoptosis associated with activation of caspases 9 and 3 and suppressed IBDV growth. These results indicate that RACK1 plays an antiapoptotic role during IBDV infection via interaction with VDAC2 and VP5, suggesting that VP5 sequesters RACK1 and VDAC2 in the apoptosis-inducing process.
Highlights
Infectious bursal disease (IBD) virus (IBDV) viral protein 5 (VP5) protein induces apoptosis in DF-1 cells via interaction with voltage-dependent anion channel 2 (VDAC2)
receptor of activated protein kinase C 1 (RACK1) Interacts with VDAC2 and IBDV VP5—Our previous report indicated that VP5 induced apoptosis in DF-1 cells via interaction with VDAC2, which affected the viral release [25]
Because RACK1 is related to apoptosis (28 –30), we proposed that RACK1 might be involved in VDAC2-mediated apoptosis
Summary
IBDV VP5 protein induces apoptosis in DF-1 cells via interaction with VDAC2. Results: RACK1 inhibits IBDV-induced apoptosis, enhances viral replication, and interacts with both VDAC2 and VP5. Conclusion: RACK1 forms a complex with VDAC2 and VP5, affecting IBDV-induced apoptosis and viral replication. We report here that receptor of activated protein kinase C 1 (RACK1) interacts with both VDAC2 and VP5 and that they could form a complex. We found that overexpression of RACK1 inhibited IBDV-induced apoptosis in DF-1 cells and that knockdown of RACK1 by small interfering RNA induced apoptosis associated with activation of caspases 9 and 3 and suppressed IBDV growth These results indicate that RACK1 plays an antiapoptotic role during IBDV infection via interaction with VDAC2 and VP5, suggesting that VP5 sequesters RACK1 and VDAC2 in the apoptosis-inducing process. Knockdown of RACK1 by siRNA markedly induced the activation of caspases 9 and 3 and suppressed IBDV growth
Sign-in/Register to view highlights & summary Sign-in/Register to access full text options 
Free) 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call
