PMID- 16904148
OWN - NLM
STAT- MEDLINE
DCOM- 20061214
LR  - 20200407
IS  - 0042-6822 (Print)
IS  - 1096-0341 (Electronic)
IS  - 0042-6822 (Linking)
VI  - 355
IP  - 1
DP  - 2006 Nov 10
TI  - The small envelope protein of porcine reproductive and respiratory syndrome virus 
      possesses ion channel protein-like properties.
PG  - 30-43
AB  - The small envelope (E) protein of porcine reproductive and respiratory syndrome 
      virus (PRRSV) is a hydrophobic 73 amino acid protein encoded in the internal open 
      reading frame (ORF) of the bicistronic mRNA2. As a first step towards 
      understanding the biological role of E protein during PRRSV replication, E gene 
      expression was blocked in a full-length infectious clone by mutating the ATG 
      translational initiation to GTG, such that the full-length mutant genomic clone 
      was unable to synthesize the E protein. DNA transfection of PRRSV-susceptible 
      cells with the E gene knocked-out genomic clone showed the absence of virus 
      infectivity. P129-DeltaE-transfected cells however produced virion particles in 
      the culture supernatant, and these particles contained viral genomic RNA, 
      demonstrating that the E protein is essential for PRRSV infection but dispensable 
      for virion assembly. Electron microscopy suggests that the P129-DeltaE virions 
      assembled in the absence of E had a similar appearance to the wild-type 
      particles. Strand-specific RT-PCR demonstrated that the E protein-negative, 
      non-infectious P129-DeltaE virus particles were able to enter cells but further 
      steps of replication were interrupted. The entry of PRRSV has been suggested to 
      be via receptor-mediated endocytosis, and lysomotropic basic compounds and known 
      ion-channel blocking agents both inhibited PRRSV replication effectively during 
      the uncoating process. The expression of E protein in Escherichia coli-mediated 
      cell growth arrests and increased the membrane permeability. Cross-linking 
      experiments in cells infected with PRRSV or transfected with E gene showed that 
      the E protein was able to form homo-oligomers. Taken together, our data suggest 
      that the PRRSV E protein is likely an ion-channel protein embedded in the viral 
      envelope and facilitates uncoating of virus and release of the genome in the 
      cytoplasm.
FAU - Lee, Changhee
AU  - Lee C
AD  - Department of Pathobiology, Ontario Veterinary College, University of Guelph, 
      Guelph, Ontario, Canada N1G 2W1.
FAU - Yoo, Dongwan
AU  - Yoo D
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20060810
PL  - United States
TA  - Virology
JT  - Virology
JID - 0110674
RN  - 0 (Calcium Channel Blockers)
RN  - 0 (RNA, Viral)
RN  - 0 (Viral Envelope Proteins)
SB  - IM
MH  - Animals
MH  - Calcium Channel Blockers/pharmacology
MH  - Cell Line
MH  - Cricetinae
MH  - Gene Deletion
MH  - Genes, Viral
MH  - Humans
MH  - Microscopy, Electron, Transmission
MH  - Mutation
MH  - Porcine respiratory and reproductive syndrome virus/genetics/*physiology
MH  - RNA, Viral/analysis
MH  - Viral Envelope Proteins/genetics/*physiology
MH  - Virion/ultrastructure
MH  - Virus Assembly
MH  - Virus Internalization
MH  - *Virus Replication
PMC - PMC7111972
EDAT- 2006/08/15 09:00
MHDA- 2006/12/15 09:00
PMCR- 2006/08/10
CRDT- 2006/08/15 09:00
PHST- 2006/04/17 00:00 [received]
PHST- 2006/05/04 00:00 [revised]
PHST- 2006/07/10 00:00 [accepted]
PHST- 2006/08/15 09:00 [pubmed]
PHST- 2006/12/15 09:00 [medline]
PHST- 2006/08/15 09:00 [entrez]
PHST- 2006/08/10 00:00 [pmc-release]
AID - S0042-6822(06)00452-1 [pii]
AID - 10.1016/j.virol.2006.07.013 [doi]
PST - ppublish
SO  - Virology. 2006 Nov 10;355(1):30-43. doi: 10.1016/j.virol.2006.07.013. Epub 2006 
      Aug 10.