Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1995-6-9
pubmed:databankReference
pubmed:abstractText
Interferon-gamma functions within the immune system as a potent anti-viral and immunoregulatory cytokine. In order to successfully replicate within a host cell, poxviruses have evolved a number of strategies to counteract the pleiotropic effects of interferon-gamma. In particular, the leporipoxvirus myxoma virus was shown to express an extracellular soluble interferon-gamma receptor homolog, denoted M-T7, which is capable of inhibiting the anti-viral activities of rabbit interferon-gamma (C. Upton, K. Mossman, and G. McFadden, 1992, Science 258, 1369-1372). Here, we demonstrate that expression of soluble interferon-gamma receptor homologs appears to be characteristic of all poxviruses tested, including Shope fibroma virus, vaccinia virus (strains WR and IHDW), ectromelia virus, cowpox virus, and rabbitpox virus. We have cloned, sequenced, and characterized the interferon-gamma binding protein in supernatants from ectromelia virus-infected cells, and demonstrate the capability of this soluble protein to bind human, murine, and rabbit interferon-gamma with similar affinity. We also investigate the properties of the vaccinia virus interferon-gamma binding protein and demonstrate that this protein binds human and rabbit interferon-gamma with similar affinity and binds murine interferon-gamma with a significantly lower relative affinity. The implications of these studies with respect to viral pathogenesis and the evolutionary relationship between a virus and its host are discussed.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0042-6822
pubmed:author
pubmed:issnType
Print
pubmed:day
20
pubmed:volume
208
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
762-9
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed-meshheading:7747448-Amino Acid Sequence, pubmed-meshheading:7747448-Animals, pubmed-meshheading:7747448-Base Sequence, pubmed-meshheading:7747448-Cell Line, pubmed-meshheading:7747448-Cloning, Molecular, pubmed-meshheading:7747448-Cross-Linking Reagents, pubmed-meshheading:7747448-Ectromelia virus, pubmed-meshheading:7747448-Genes, Viral, pubmed-meshheading:7747448-Haplorhini, pubmed-meshheading:7747448-Humans, pubmed-meshheading:7747448-Interferon-gamma, pubmed-meshheading:7747448-Molecular Sequence Data, pubmed-meshheading:7747448-Poxviridae, pubmed-meshheading:7747448-Protein Conformation, pubmed-meshheading:7747448-Receptors, Interferon, pubmed-meshheading:7747448-Sequence Analysis, DNA, pubmed-meshheading:7747448-Sequence Homology, Amino Acid, pubmed-meshheading:7747448-Species Specificity, pubmed-meshheading:7747448-Vaccinia virus, pubmed-meshheading:7747448-Viral Proteins, pubmed-meshheading:7747448-Viral Structural Proteins
pubmed:year
1995
pubmed:articleTitle
Species specificity of ectromelia virus and vaccinia virus interferon-gamma binding proteins.
pubmed:affiliation
Department of Biochemistry, University of Alberta, Edmonton, Canada.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't