rdf:type |
|
lifeskim:mentions |
umls-concept:C0033684,
umls-concept:C0206679,
umls-concept:C0521026,
umls-concept:C0683598,
umls-concept:C1149404,
umls-concept:C1514873,
umls-concept:C1546857,
umls-concept:C1552644,
umls-concept:C1556066,
umls-concept:C1619636,
umls-concept:C1823153,
umls-concept:C2349976
|
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-meshheading:11882996-Amino Acids,
pubmed-meshheading:11882996-Animals,
pubmed-meshheading:11882996-Binding Sites,
pubmed-meshheading:11882996-Cercopithecus aethiops,
pubmed-meshheading:11882996-Drug Resistance, Viral,
pubmed-meshheading:11882996-Fibroblasts,
pubmed-meshheading:11882996-Herpesvirus 1, Human,
pubmed-meshheading:11882996-Humans,
pubmed-meshheading:11882996-Interferon-alpha,
pubmed-meshheading:11882996-Interferon-beta,
pubmed-meshheading:11882996-Mice,
pubmed-meshheading:11882996-Mice, Knockout,
pubmed-meshheading:11882996-Phenylalanine,
pubmed-meshheading:11882996-Valine,
pubmed-meshheading:11882996-Vero Cells,
pubmed-meshheading:11882996-Viral Proteins,
pubmed-meshheading:11882996-Virus Replication,
pubmed-meshheading:11882996-eIF-2 Kinase
|
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.
|