PMID- 20696193
OWN - NLM
STAT- MEDLINE
DCOM- 20110225
LR  - 20211020
IS  - 1872-7492 (Electronic)
IS  - 0168-1702 (Print)
IS  - 0168-1702 (Linking)
VI  - 154
IP  - 1-2
DP  - 2010 Dec
TI  - The PRRSV replicase: exploring the multifunctionality of an intriguing set of 
      nonstructural proteins.
PG  - 61-76
LID - 10.1016/j.virusres.2010.07.030 [doi]
AB  - Our knowledge about the structure and function of the nonstructural proteins 
      (nsps) encoded by the arterivirus replicase gene has advanced in recent years. 
      The continued characterization of the nsps of the arterivirus prototype equine 
      arteritis virus has not only corroborated several important functional 
      predictions, but also revealed various novel features of arteriviral replication. 
      For porcine reproductive and respiratory syndrome virus (PRRSV), based on 
      bioinformatics predictions and experimental studies, a processing map for the 
      pp1a and pp1ab replicase polyproteins has been developed. Crystal structures have 
      been resolved for two of the PRRSV nonstructural proteins that possess proteinase 
      activity (nsp1alpha and nsp4). The functional characterization of the key enzymes for 
      arterivirus RNA synthesis, the nsp9 RNA polymerase and nsp10 helicase, has been 
      initiated. In addition, progress has been made on nsp functions relating to the 
      regulation of subgenomic mRNAs synthesis (nsp1), the induction of 
      replication-associated membrane rearrangements (nsp2 and nsp3), and an intriguing 
      replicative endoribonuclease (nsp11) for which the natural substrate remains to 
      be identified. The role of nsps in viral pathogenesis and host immunity is also 
      being explored, and specific nsps (including nsp1alpha/beta, nsp2, nsp4, nsp7, and 
      nsp11) have been implicated in the modulation of host immune responses to PRRSV 
      infection. The nsp3-8 region was identified as containing major virulence 
      factors, although mechanistic information is scarce. The biological significance 
      of PRRSV nsps in virus-host interactions and the technical advancements in 
      engineering the PRRSV genome by reverse genetics are also reflected in recent 
      developments in the area of vaccines and diagnostic assays.
CI  - Copyright (c) 2010 Elsevier B.V. All rights reserved.
FAU - Fang, Ying
AU  - Fang Y
AD  - Department of Veterinary and Biomedical Science/Department of Bio-microbiology, 
      South Dakota State University, Brookings, SD 57007-1396, USA. 
      ying.fang@sdstate.edu
FAU - Snijder, Eric J
AU  - Snijder EJ
LA  - eng
PT  - Journal Article
PT  - Review
DEP - 20100807
PL  - Netherlands
TA  - Virus Res
JT  - Virus research
JID - 8410979
RN  - 0 (Viral Nonstructural Proteins)
RN  - EC 2.7.7.48 (RNA-Dependent RNA Polymerase)
SB  - IM
MH  - Host-Pathogen Interactions
MH  - Porcine respiratory and reproductive syndrome 
      virus/*enzymology/immunology/pathogenicity/*physiology
MH  - RNA-Dependent RNA Polymerase/chemistry/genetics/*metabolism
MH  - Viral Nonstructural Proteins/chemistry/genetics/*metabolism
MH  - *Virus Replication
PMC - PMC7114499
EDAT- 2010/08/11 06:00
MHDA- 2011/02/26 06:00
PMCR- 2010/08/07
CRDT- 2010/08/11 06:00
PHST- 2010/04/07 00:00 [received]
PHST- 2010/07/07 00:00 [revised]
PHST- 2010/07/31 00:00 [accepted]
PHST- 2010/08/11 06:00 [entrez]
PHST- 2010/08/11 06:00 [pubmed]
PHST- 2011/02/26 06:00 [medline]
PHST- 2010/08/07 00:00 [pmc-release]
AID - S0168-1702(10)00276-5 [pii]
AID - 10.1016/j.virusres.2010.07.030 [doi]
PST - ppublish
SO  - Virus Res. 2010 Dec;154(1-2):61-76. doi: 10.1016/j.virusres.2010.07.030. Epub 
      2010 Aug 7.