Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-2
pubmed:dateCreated
1992-11-19
pubmed:abstractText
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.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0168-1702
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
25
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
51-61
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1992
pubmed:articleTitle
The soluble form of two N-terminal domains of the poliovirus receptor is sufficient for blocking viral infection.
pubmed:affiliation
Department of Microbiology, State University of New York, Stony Brook 11794.
pubmed:publicationType
Journal Article, In Vitro, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't