Abstract
Apoptosis is a type of programmed cell death that regulates cellular homeostasis by removing damaged or unnecessary cells. Its importance in host defenses is highlighted by the observation that many viruses evade, obstruct, or subvert apoptosis, thereby blunting the host immune response. Infection with Flaviviruses such as Japanese encephalitis virus (JEV), Dengue virus (DENV) and West Nile virus (WNV) has been shown to activate several signaling pathways such as endoplasmic reticulum (ER)-stress and AKT/PI3K pathway, resulting in activation or suppression of apoptosis in virus-infected cells. On the other hands, expression of some viral proteins induces or protects apoptosis. There is a discrepancy between induction and suppression of apoptosis during flavivirus infection because the experimental situation may be different, and strong links between apoptosis and other types of cell death such as necrosis may make it more difficult. In this paper, we review the effects of apoptosis on viral propagation and pathogenesis during infection with flaviviruses.
Highlights
It should be noted that the induction of cell death by targeting BCL2 proteins is a promising therapeutic strategy based on the removal of unnecessary cells
It is important for us to understand the consequences of regulation of apoptosis during viral infection, and the viral protein itself
Lessons from the DNA viruses suggest that viruses inhibit apoptosis to achieve efficient propagation in vivo, but apoptosis seems to be induced in virus-infected cells by a host response to clear the infected cells in vitro
Summary
Programmed cell death, is an evolutionarily conserved process essential for the removal of damaged, infected or excess amounts of cells [1,2]. SMAC block the caspase inhibitor, X-linked inhibitor of apoptosis proteins including caspase 9 [5]. BAX anddamage, BH3-onlyBAK, proteins are activated and displace the prosurvival proteins from their interaction with disrupting the mitochondrial outer membrane and releasing cytochrome c, second mitochondria-derived activator of caspases (SMAC), and so on. BAX and BAK, disrupting the mitochondrial outer membrane and releasing cytochrome c, with apoptotic protease-activating factor 1 (APAF1) to activate effector caspases, including caspase 9. Interacts with apoptotic protease-activating factor 1 (APAF1) to activate effector caspases, including Death receptors, such as FAS/CD95 or tumor necrosis factor receptors (TNFR), are activated by their caspase 9.ligands. FAS-associated death domain of protein (FADD)proteins (XIAP) Death receptors, such asofFAS/CD95 or tumor necrosis factor receptors (TNFR), activated by to cytoplasmic domains receptors, resulting in the activation of caspase. Activated caspase 8 cleaves BID to generate truncated BID (tBID), inducing mitochondria-mediated apoptosis
Sign-in/Register to view highlights & summary 
Published Version (
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