PMID- 19580983
OWN - NLM
STAT- MEDLINE
DCOM- 20090831
LR  - 20211020
IS  - 1096-0341 (Electronic)
IS  - 0042-6822 (Print)
IS  - 0042-6822 (Linking)
VI  - 391
IP  - 2
DP  - 2009 Sep 1
TI  - Host cell proteins interacting with the 3' end of TGEV coronavirus genome 
      influence virus replication.
PG  - 304-14
LID - 10.1016/j.virol.2009.06.006 [doi]
AB  - Coronavirus RNA synthesis is performed by a multienzymatic replicase complex 
      together with cellular factors. This process requires the specific recognition of 
      RNA cis-acting signals located at the ends of the viral genome. To identify 
      cellular proteins involved in coronavirus RNA synthesis, transmissible 
      gastroenteritis coronavirus (TGEV) genome ends, harboring essential cis-acting 
      signals for replication, were used as baits for RNA affinity protein 
      purification. Ten proteins were preferentially pulled down with either the 5' or 
      3' ends of the genome and identified by proteomic analysis. Nine of them, 
      including members of the heterogeneous ribonucleoprotein family of proteins 
      (hnRNPs), the poly(A)-binding protein (PABP), the p100 transcriptional 
      co-activator protein and two aminoacyl-tRNA synthetases, showed a preferential 
      binding to the 3' end of the genome, whereas only the polypyrimidine 
      tract-binding protein (PTB) was preferentially pulled down with the 5' end of the 
      genome. The potential function of the 3' end-interacting proteins in virus 
      replication was studied by analyzing the effect of their silencing using a 
      TGEV-derived replicon and the infectious virus. Gene silencing of PABP, hnRNP Q, 
      and glutamyl-prolyl-tRNA synthetase (EPRS) caused a significant 2 to 3-fold 
      reduction of viral RNA synthesis. Interestingly, the silencing of glyceraldehyde 
      3-phosphate dehydrogenase (GAPDH), initially used as a control gene, caused a 2 
      to 3-fold increase in viral RNA synthesis in both systems. These data suggest 
      that PABP, hnRNP Q, and EPRS play a positive role in virus infection that could 
      be mediated through their interaction with the viral 3' end, and that GAPDH has a 
      negative effect on viral infection.
FAU - Galan, Carmen
AU  - Galan C
AD  - Department of Molecular and Cell Biology, Centro Nacional de Biotecnologia, CSIC, 
      C/Darwin 3, Cantoblanco, 28049 Madrid, Spain.
FAU - Sola, Isabel
AU  - Sola I
FAU - Nogales, Aitor
AU  - Nogales A
FAU - Thomas, Benjamin
AU  - Thomas B
FAU - Akoulitchev, Alexandre
AU  - Akoulitchev A
FAU - Enjuanes, Luis
AU  - Enjuanes L
FAU - Almazan, Fernando
AU  - Almazan F
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20090705
PL  - United States
TA  - Virology
JT  - Virology
JID - 0110674
RN  - 0 (Proteins)
RN  - 0 (Proteome)
RN  - 0 (RNA, Viral)
SB  - IM
MH  - Cell Line
MH  - Chromatography, Affinity/methods
MH  - Coronavirus/*physiology
MH  - Hepatocytes/chemistry
MH  - *Host-Pathogen Interactions
MH  - Humans
MH  - Mass Spectrometry/methods
MH  - Protein Binding
MH  - Proteins/isolation & purification/*metabolism
MH  - Proteome/analysis
MH  - RNA, Viral/*metabolism
MH  - *Virus Replication
PMC - PMC7118768
EDAT- 2009/07/08 09:00
MHDA- 2009/09/01 06:00
PMCR- 2009/07/05
CRDT- 2009/07/08 09:00
PHST- 2009/04/27 00:00 [received]
PHST- 2009/05/25 00:00 [revised]
PHST- 2009/06/03 00:00 [accepted]
PHST- 2009/07/08 09:00 [entrez]
PHST- 2009/07/08 09:00 [pubmed]
PHST- 2009/09/01 06:00 [medline]
PHST- 2009/07/05 00:00 [pmc-release]
AID - S0042-6822(09)00349-3 [pii]
AID - 10.1016/j.virol.2009.06.006 [doi]
PST - ppublish
SO  - Virology. 2009 Sep 1;391(2):304-14. doi: 10.1016/j.virol.2009.06.006. Epub 2009 
      Jul 5.