The soluble form of two N-terminal domains of the poliovirus receptor is sufficient for blocking viral infection.
Virus Res
; 25(1-2): 51-61, 1992 Sep 01.
Article
em En
| MEDLINE
| ID: mdl-1329376
ABSTRACT
By means of deleting a C-terminal portion of the open reading frame of the poliovirus receptor cDNA, and by vaccinia virus-mediated overexpression we have produced a protein corresponding to the first two N-terminal Ig-like domains of the poliovirus receptor. This protein that lacked the third Ig-like domain, the transmembrane region and most of the intracellular C-terminal tail was detected in the medium of vaccinia virus infected cells. The properties of the truncated PVR cDNA were further characterized by in vitro translation and modification. The molecular weight of the unmodified protein was found to be 27 kDa; translation in the presence of dog pancreas microsomes led to an increase in molecular weights which we attribute to N-glycosylation. Upon incubation with poliovirus at 37 degrees C, the vaccinia-virus generated protein specifically reduced infectivity of poliovirus. Sucrose gradients of poliovirus particles derived after incubation with the protein showed the induction of a slower sedimenting particle (135S). Our experiments suggest that the two N-terminal domains of the poliovirus receptor in soluble form are sufficient for the conversion of poliovirus into a non-infectious particle.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Receptores Virais
/
Poliovirus
Limite:
Animals
/
Humans
Idioma:
En
Revista:
Virus Res
Assunto da revista:
VIROLOGIA
Ano de publicação:
1992
Tipo de documento:
Article