PMID- 12490397
OWN - NLM
STAT- MEDLINE
DCOM- 20030116
LR  - 20190714
IS  - 0042-6822 (Print)
IS  - 0042-6822 (Linking)
VI  - 303
IP  - 2
DP  - 2002 Nov 25
TI  - Chimeric arteriviruses generated by swapping of the M protein ectodomain rule out 
      a role of this domain in viral targeting.
PG  - 364-73
AB  - Arteriviruses are enveloped, positive-strand RNA viruses for which the two major 
      envelope proteins GP(5) and M occur as disulfide-linked heterodimers. These were 
      assumed to serve the viral targeting functions, but recent ectodomain swapping 
      studies with equine arteritis virus (EAV) indicate that the GP(5) protein does 
      not determine arteriviral tropism. Here, we focused on the short, 13- to 
      18-residue ectodomain of the M protein. Using an infectious cDNA clone of the 
      Lelystad virus isolate of porcine reproductive and respiratory syndrome virus 
      (PRRSV), we substituted the genomic sequence encoding the M ectodomain by that of 
      murine lactate dehydrogenase-elevating virus, EAV, and the US PRRSV-isolate, 
      VR2332. Viable viruses with a chimeric M protein were obtained in all three 
      cases, but for the latter two only after removal of the genomic overlap between 
      the M and GP(5) genes. Characterization of the chimeric viruses revealed that 
      they could be distinguished immunologically from wild-type virus, that they were 
      genetically stable in vitro, but that they were impaired in their growth, 
      reaching lower titers than the parental virus. The latter appeared to be due to 
      an increased particle-to-infectivity ratio of the chimeric virus particles. 
      Interestingly, the chimeric viruses had retained their ability to infect porcine 
      cells and had not acquired tropism for cells susceptible to the viruses from 
      which the foreign ectodomains were derived. We conclude that the surface 
      structures composed by the arterivirus M and GP(5) ectodomains do not determine 
      viral tropism.
FAU - Verheije, M H
AU  - Verheije MH
AD  - Division of Endemic Diseases, Department of Infectious Diseases and Food Chain 
      Quality, Institute for Animal Science and Health, Lelystad, The Netherlands. 
      h.verheije@vet.uu.nl
FAU - Welting, T J M
AU  - Welting TJ
FAU - Jansen, H T
AU  - Jansen HT
FAU - Rottier, P J M
AU  - Rottier PJ
FAU - Meulenberg, J J M
AU  - Meulenberg JJ
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Virology
JT  - Virology
JID - 0110674
RN  - 0 (Recombinant Fusion Proteins)
RN  - 0 (Viral Envelope Proteins)
RN  - 0 (Viral Matrix Proteins)
RN  - 0 (glycoprotein 5, PRRSV)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Arterivirus/genetics/immunology/*physiology
MH  - Base Sequence
MH  - Equartevirus/physiology
MH  - Lactate dehydrogenase-elevating virus/physiology
MH  - Molecular Sequence Data
MH  - Open Reading Frames
MH  - Porcine respiratory and reproductive syndrome virus/physiology
MH  - Recombinant Fusion Proteins/*physiology
MH  - Swine
MH  - Transfection
MH  - Viral Envelope Proteins/physiology
MH  - Viral Matrix Proteins/chemistry/*physiology
EDAT- 2002/12/20 04:00
MHDA- 2003/01/17 04:00
CRDT- 2002/12/20 04:00
PHST- 2002/12/20 04:00 [pubmed]
PHST- 2003/01/17 04:00 [medline]
PHST- 2002/12/20 04:00 [entrez]
AID - S0042682202917113 [pii]
AID - 10.1006/viro.2002.1711 [doi]
PST - ppublish
SO  - Virology. 2002 Nov 25;303(2):364-73. doi: 10.1006/viro.2002.1711.