PMID- 16160177
OWN - NLM
STAT- MEDLINE
DCOM- 20051021
LR  - 20181113
IS  - 0022-538X (Print)
IS  - 1098-5514 (Electronic)
IS  - 0022-538X (Linking)
VI  - 79
IP  - 19
DP  - 2005 Oct
TI  - Envelope protein requirements for the assembly of infectious virions of porcine 
      reproductive and respiratory syndrome virus.
PG  - 12495-506
AB  - Virions of porcine reproductive and respiratory syndrome virus (PRRSV) contain 
      six membrane proteins: the major proteins GP5 and M and the minor proteins GP2a, 
      E, GP3, and GP4. Here, we studied the envelope protein requirements for PRRSV 
      particle formation and infectivity using full-length cDNA clones in which the 
      genes encoding the membrane proteins were disrupted by site-directed mutagenesis. 
      By transfection of RNAs transcribed from these cDNAs into BHK-21 cells and 
      analysis of the culture medium using ultracentrifugation, 
      radioimmunoprecipitation, and real-time reverse transcription-PCR, we observed 
      that the production of viral particles is dependent on both major envelope 
      proteins; no particles were released when either the GP5 or the M protein was 
      absent. In contrast, particle production was not dependent on the minor envelope 
      proteins. Remarkably, in the absence of any one of the latter proteins, the 
      incorporation of all other minor envelope proteins was affected, indicating that 
      these proteins interact with each other and are assembled into virions as a 
      multimeric complex. Independent evidence for such complexes was obtained by 
      coexpression of the minor envelope proteins in BHK-21 cells using a Semliki 
      Forest virus expression system. By analyzing the maturation of their N-linked 
      oligosaccharides, we found that the glycoproteins were each retained in the 
      endoplasmic reticulum unless expressed together, in which case they were 
      collectively transported through the Golgi complex to the plasma membrane and 
      were even detected in the extracellular medium. As the PRRSV particles lacking 
      the minor envelope proteins are not infectious, we hypothesize that the virion 
      surface structures formed by these proteins function in viral entry by mediating 
      receptor binding and/or virus-cell fusion.
FAU - Wissink, E H J
AU  - Wissink EH
AD  - Animal Sciences Group (Wageningen UR), Infectious Diseases Division, Edelhertweg 
      15, P.O. Box 65, 8200 AB Lelystad, The Netherlands.
FAU - Kroese, M V
AU  - Kroese MV
FAU - van Wijk, H A R
AU  - van Wijk HA
FAU - Rijsewijk, F A M
AU  - Rijsewijk FA
FAU - Meulenberg, J J M
AU  - Meulenberg JJ
FAU - Rottier, P J M
AU  - Rottier PJ
LA  - eng
PT  - Journal Article
PL  - United States
TA  - J Virol
JT  - Journal of virology
JID - 0113724
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Viral Envelope Proteins)
RN  - 0 (glycoprotein 5, PRRSV)
SB  - IM
MH  - Animals
MH  - Cell Line
MH  - Cricetinae
MH  - Immunoprecipitation
MH  - Membrane Glycoproteins/analysis
MH  - Mutagenesis, Site-Directed
MH  - Nucleocapsid/chemistry
MH  - Polymerase Chain Reaction
MH  - Porcine respiratory and reproductive syndrome virus/genetics/growth & 
      development/*physiology
MH  - Ultracentrifugation
MH  - Viral Envelope Proteins/genetics/metabolism/*physiology
MH  - *Virus Assembly
PMC - PMC1211556
EDAT- 2005/09/15 09:00
MHDA- 2005/10/22 09:00
PMCR- 2005/10/01
CRDT- 2005/09/15 09:00
PHST- 2005/09/15 09:00 [pubmed]
PHST- 2005/10/22 09:00 [medline]
PHST- 2005/09/15 09:00 [entrez]
PHST- 2005/10/01 00:00 [pmc-release]
AID - 79/19/12495 [pii]
AID - 1514-04 [pii]
AID - 10.1128/JVI.79.19.12495-12506.2005 [doi]
PST - ppublish
SO  - J Virol. 2005 Oct;79(19):12495-506. doi: 10.1128/JVI.79.19.12495-12506.2005.