Linked Life Data

17197048

Source:http://linkedlifedata.com/resource/pubmed/id/17197048

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2007-3-20
pubmed:abstractText
Shiga toxins are ribosome-inactivating proteins many of which are antiviral. Shiga toxin-producing Escherichia coli (STEC) may be pathogenic to humans, but are carried without ill effects by ruminants. We hypothesize that STEC have antiviral activity in ruminants, and showed previously that the non-toxic subunit A of Shiga toxin 1 (StxA1) acts selectively on cells infected with bovine leukemia virus, without harming normal cells, and that the numbers of intestinal STEC are inversely correlated with viral load in bovine leukemia virus-infected sheep. The purpose of the present study was to characterize StxA1 activity against a second bovine retrovirus, bovine immunodeficiency virus (BIV). Flow cytometry showed that StxA1 treatment induced apoptosis in BIV-infected cells but not in uninfected cells and immunoblot analysis showed that StxA1 curtailed synthesis of Gag p26 protein. A systematic electron microscopy description of BIV infection in fetal bovine lung fibroblasts showed an orderly sequence of changes in cell membrane, endoplasmic reticulum, Golgi, nucleus, and mitochondria, and suggested that the infected cells produce the virus within multivesicular bodies (MVBs). StxA1 interfered with all manifestations of BIV-induced transformation of infected cells into BIV-producing units. BIV-infected cells provided a suitable experimental system for investigation of the mechanism of Stx-antiviral activity.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0168-1702
pubmed:author
pubmed:issnType
Print
pubmed:volume
125
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
29-41
pubmed:dateRevised
2011-9-26
pubmed:meshHeading
pubmed:year
2007
pubmed:articleTitle
The non-toxic A subunit of Shiga toxin type 1 prevents replication of bovine immunodeficiency virus in infected cells.
pubmed:affiliation
Department of Microbiology, Molecular Biology, and Biochemistry, University of Idaho, Moscow, ID 83844-3052, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't, Research Support, N.I.H., Extramural