PMID- 21976648
OWN - NLM
STAT- MEDLINE
DCOM- 20120123
LR  - 20211020
IS  - 1098-5514 (Electronic)
IS  - 0022-538X (Print)
IS  - 0022-538X (Linking)
VI  - 85
IP  - 24
DP  - 2011 Dec
TI  - Cellular poly(c) binding proteins 1 and 2 interact with porcine reproductive and 
      respiratory syndrome virus nonstructural protein 1beta and support viral 
      replication.
PG  - 12939-49
LID - 10.1128/JVI.05177-11 [doi]
AB  - Porcine reproductive and respiratory syndrome virus (PRRSV) infection of swine 
      results in substantial economic losses to the swine industry worldwide. 
      Identification of cellular factors involved in PRRSV life cycle not only will 
      enable a better understanding of virus biology but also has the potential for the 
      development of antiviral therapeutics. The PRRSV nonstructural protein 1 (nsp1) 
      has been shown to be involved in at least two important functions in the infected 
      hosts: (i) mediation of viral subgenomic (sg) mRNA transcription and (ii) 
      suppression of the host's innate immune response mechanisms. To further our 
      understanding of the role of the viral nsp1 in these processes, using nsp1beta, a 
      proteolytically processed functional product of nsp1 as bait, we have identified 
      the cellular poly(C)-binding proteins 1 and 2 (PCBP1 and PCBP2) as two of its 
      interaction partners. The interactions of PCBP1 and PCBP2 with nsp1beta were 
      confirmed both by coimmunoprecipitation in infected cells and/or in 
      plasmid-transfected cells and also by in vitro binding assays. During PRRSV 
      infection of MARC-145 cells, the cytoplasmic PCBP1 and PCBP2 partially colocalize 
      to the viral replication-transcription complexes. Furthermore, recombinant 
      purified PCBP1 and PCBP2 were found to bind the viral 5' untranslated region 
      (5'UTR). Small interfering RNA (siRNA)-mediated silencing of PCBP1 and PCBP2 in 
      cells resulted in significantly reduced PRRSV genome replication and 
      transcription without adverse effect on initial polyprotein synthesis. Overall, 
      the results presented here point toward an important role for PCBP1 and PCBP2 in 
      regulating PRRSV RNA synthesis.
FAU - Beura, Lalit K
AU  - Beura LK
AD  - Morrison Research Center, 4240 Fair Street, East Campus, University of 
      Nebraska-Lincoln, Lincoln, NE 68583-0900, USA.
FAU - Dinh, Phat X
AU  - Dinh PX
FAU - Osorio, Fernando A
AU  - Osorio FA
FAU - Pattnaik, Asit K
AU  - Pattnaik AK
LA  - eng
PT  - Journal Article
PT  - Research Support, U.S. Gov't, Non-P.H.S.
DEP - 20111005
PL  - United States
TA  - J Virol
JT  - Journal of virology
JID - 0113724
RN  - 0 (5' Untranslated Regions)
RN  - 0 (RNA, Viral)
RN  - 0 (RNA-Binding Proteins)
RN  - 0 (Viral Nonstructural Proteins)
SB  - IM
MH  - 5' Untranslated Regions
MH  - Animals
MH  - Cell Line
MH  - Gene Silencing
MH  - *Host-Pathogen Interactions
MH  - Immunoprecipitation
MH  - Porcine respiratory and reproductive syndrome virus/*pathogenicity
MH  - Protein Binding
MH  - Protein Interaction Mapping
MH  - RNA, Viral/metabolism
MH  - RNA-Binding Proteins/*metabolism
MH  - Swine
MH  - Viral Nonstructural Proteins/*metabolism
MH  - *Virus Replication
PMC - PMC3233143
EDAT- 2011/10/07 06:00
MHDA- 2012/01/24 06:00
PMCR- 2012/06/01
CRDT- 2011/10/07 06:00
PHST- 2011/10/07 06:00 [entrez]
PHST- 2011/10/07 06:00 [pubmed]
PHST- 2012/01/24 06:00 [medline]
PHST- 2012/06/01 00:00 [pmc-release]
AID - JVI.05177-11 [pii]
AID - 5177-11 [pii]
AID - 10.1128/JVI.05177-11 [doi]
PST - ppublish
SO  - J Virol. 2011 Dec;85(24):12939-49. doi: 10.1128/JVI.05177-11. Epub 2011 Oct 5.