In mammalian cells, proteins involved in mRNA silencing and degradation localize 
to discrete cytoplasmic foci called processing or P-bodies. Here we show that 
microscopically visible P-bodies are greatly diminished following West Nile 
viral infection, but the component proteins are not depleted. On the other hand, 
many P-body components including LSM1, GW182, DDX3, DDX6 and XRN1, but not 
others like DCP1a and EDC4 are recruited to the viral replication sites, as 
evidenced by their colocalization at perinuclear region with viral NS3. Kinetic 
studies suggest that the component proteins are first released from P-bodies in 
response to WNV infection within 12 h post-infection, followed by recruitment to 
the viral replication sites by 24-36 h post-infection. Silencing of the 
recruited proteins individually with siRNA interfered with viral replication to 
varying extents suggesting that the recruited proteins are required for 
efficient viral replication. Thus, the P-body proteins might provide novel drug 
targets for inhibiting viral infection.