Linked Life Data

9185591

Source:http://linkedlifedata.com/resource/pubmed/id/9185591

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1997-7-8
pubmed:abstractText
The soluble B18R protein coded by vaccinia virus exerts properties of a type I interferon (IFN)-receptor with broad species specificity. We analyzed neutralizing and binding activity of the B18R protein against several recombinant human type I IFNs. The B18R protein inhibited the antiviral potency of IFN-alpha1, IFN-alpha2, IFN-alpha8/1/8, and IFN-omega on human cells. The N-terminal domain of human type I IFN is involved in the high affinity binding to its cellular receptor. To localize the binding domain(s) of IFN with the B18R protein, competition experiments between B18R, and mapped monoclonal antibodies to IFN-alpha1 and IFN-alpha2 were performed. Surprisingly, our data indicated that the contact area between the B18R protein and IFN comprised in addition to the N-terminal region of IFN-molecule also its C-terminal portion. We suggest that this different pattern of interaction with a ligand might determine the ability of B18R protein to bind type I IFNs of different species.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0042-6822
pubmed:author
pubmed:issnType
Print
pubmed:day
26
pubmed:volume
232
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
86-90
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed:year
1997
pubmed:articleTitle
Analysis of an interaction between the soluble vaccinia virus-coded type I interferon (IFN)-receptor and human IFN-alpha1 and IFN-alpha2.
pubmed:affiliation
Institute of Virology, Slovak Academy of Sciences, Bratislava, Slovakia.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't