Abstract
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.
Original language | English (US) |
---|---|
Pages (from-to) | 1-7 |
Number of pages | 7 |
Journal | Virology |
Volume | 436 |
Issue number | 1 |
DOIs | |
State | Published - Feb 5 2013 |
Externally published | Yes |
Fingerprint
Keywords
- DDX3
- Flavivirus
- GW182
- LSM1
- P-body
- RNAi
- West Nile virus
ASJC Scopus subject areas
- Virology
Cite this
P-body components LSM1, GW182, DDX3, DDX6 and XRN1 are recruited to WNV replication sites and positively regulate viral replication. / Chahar, Harendra S.; Chen, Shuiping; Manjunath, N.
In: Virology, Vol. 436, No. 1, 05.02.2013, p. 1-7.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - P-body components LSM1, GW182, DDX3, DDX6 and XRN1 are recruited to WNV replication sites and positively regulate viral replication
AU - Chahar, Harendra S.
AU - Chen, Shuiping
AU - Manjunath, N.
PY - 2013/2/5
Y1 - 2013/2/5
N2 - 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.
AB - 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.
KW - DDX3
KW - Flavivirus
KW - GW182
KW - LSM1
KW - P-body
KW - RNAi
KW - West Nile virus
UR - http://www.scopus.com/inward/record.url?scp=84872197323&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=84872197323&partnerID=8YFLogxK
U2 - 10.1016/j.virol.2012.09.041
DO - 10.1016/j.virol.2012.09.041
M3 - Article
C2 - 23102969
AN - SCOPUS:84872197323
VL - 436
SP - 1
EP - 7
JO - Virology
JF - Virology
SN - 0042-6822
IS - 1
ER -