Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2002-3-8
pubmed:abstractText
Herpes simplex viruses (HSV) are resistant to the antiviral action of interferon. However, the underlying mechanisms are not well understood. In this report, we show that unlike that of wild-type HSV-1, replication of the gamma 1 34.5 null mutants was significantly inhibited by exogenous interferon-alpha in cells devoid of interferon-alpha/beta genes. Using a series of gamma 1 34.5 deletion mutants, the domain required for interferon resistance was mapped to the region containing amino acids 146 to 263 in the gamma 1 34.5 protein. Interestingly, Val193 Glu and Phe195 Leu substitutions in the protein phosphatase 1 interacting motif of the gamma 1 34.5 protein rendered HSV-1 sensitive to interferon-alpha. Furthermore, gamma 1 34.5 null mutants were sensitive to interferon-alpha/beta in PKR+/+ but not in PKR-/- mouse embryo fibroblasts. These findings provide evidence that the gamma 1 34.5 protein contributes to HSV-1 resistance to interferon-alpha/beta by inhibiting PKR function.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0042-6822
pubmed:author
pubmed:issnType
Print
pubmed:day
10
pubmed:volume
290
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
115-20
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
2001
pubmed:articleTitle
Val193 and Phe195 of the gamma 1 34.5 protein of herpes simplex virus 1 are required for viral resistance to interferon-alpha/beta.
pubmed:affiliation
Department of Microbiology and Immunology, College of Medicine, University of Illinois at Chicago, 835 South Wolcott Avenue, Chicago, Illinois 60612, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.