PMID- 22258262
OWN - NLM
STAT- MEDLINE
DCOM- 20120611
LR  - 20211021
IS  - 1098-5514 (Electronic)
IS  - 0022-538X (Print)
IS  - 0022-538X (Linking)
VI  - 86
IP  - 7
DP  - 2012 Apr
TI  - Arterivirus minor envelope proteins are a major determinant of viral tropism in 
      cell culture.
PG  - 3701-12
LID - 10.1128/JVI.06836-11 [doi]
AB  - Arteriviruses are enveloped positive-strand RNA viruses for which the attachment 
      proteins and cellular receptors have remained largely controversial. Arterivirus 
      particles contain at least eight envelope proteins, an unusually large number 
      among RNA viruses. These appear to segregate into three groups: major structural 
      components (major glycoprotein GP5 and membrane protein [M]), minor glycoproteins 
      (GP2a, GP3, and GP4), and small hydrophobic proteins (E and the recently 
      discovered ORF5a protein). Biochemical studies previously suggested that the 
      GP5-M heterodimer of porcine reproductive and respiratory syndrome virus (PRRSV) 
      interacts with porcine sialoadhesin (pSn) in porcine alveolar macrophages (PAM). 
      However, another study proposed that minor protein GP4, along with GP2a, 
      interacts with CD163, another reported cellular receptor for PRRSV. In this 
      study, we provide genetic evidence that the minor envelope proteins are the major 
      determinant of arterivirus entry into cultured cells. A PRRSV infectious cDNA 
      clone was equipped with open reading frames (ORFs) encoding minor envelope and E 
      proteins of equine arteritis virus (EAV), the only known arterivirus displaying a 
      broad tropism in cultured cells. Although PRRSV and EAV are only distantly 
      related and utilize diversified transcription-regulating sequences (TRSs), a 
      viable chimeric progeny virus was rescued. Strikingly, this chimeric virus 
      (vAPRRS-EAV2ab34) acquired the broad in vitro cell tropism of EAV, demonstrating 
      that the minor envelope proteins play a critical role as viral attachment 
      proteins. We believe that chimeric arteriviruses of this kind will be a powerful 
      tool for further dissection of the arterivirus replicative cycle, including virus 
      entry, subgenomic RNA synthesis, and virion assembly.
FAU - Tian, Debin
AU  - Tian D
AD  - Department of Swine Infectious Diseases, Shanghai Veterinary Research Institute, 
      Chinese Academy of Agricultural Sciences, Shanghai, China.
FAU - Wei, Zuzhang
AU  - Wei Z
FAU - Zevenhoven-Dobbe, Jessika C
AU  - Zevenhoven-Dobbe JC
FAU - Liu, Runxia
AU  - Liu R
FAU - Tong, Guangzhi
AU  - Tong G
FAU - Snijder, Eric J
AU  - Snijder EJ
FAU - Yuan, Shishan
AU  - Yuan S
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20120118
PL  - United States
TA  - J Virol
JT  - Journal of virology
JID - 0113724
RN  - 0 (Viral Envelope Proteins)
SB  - IM
MH  - Animals
MH  - Arterivirus Infections/*veterinary/virology
MH  - Base Sequence
MH  - Cell Line
MH  - Chlorocebus aethiops
MH  - Equartevirus/genetics/*physiology
MH  - Molecular Sequence Data
MH  - Porcine Reproductive and Respiratory Syndrome/virology
MH  - Porcine respiratory and reproductive syndrome virus/genetics/*physiology
MH  - Swine
MH  - Vero Cells
MH  - Viral Envelope Proteins/genetics/*metabolism
MH  - *Viral Tropism
PMC - PMC3302522
EDAT- 2012/01/20 06:00
MHDA- 2012/06/12 06:00
PMCR- 2012/10/01
CRDT- 2012/01/20 06:00
PHST- 2012/01/20 06:00 [entrez]
PHST- 2012/01/20 06:00 [pubmed]
PHST- 2012/06/12 06:00 [medline]
PHST- 2012/10/01 00:00 [pmc-release]
AID - JVI.06836-11 [pii]
AID - 06836-11 [pii]
AID - 10.1128/JVI.06836-11 [doi]
PST - ppublish
SO  - J Virol. 2012 Apr;86(7):3701-12. doi: 10.1128/JVI.06836-11. Epub 2012 Jan 18.