Linked Life Data

18288598

Source:http://linkedlifedata.com/resource/pubmed/id/18288598

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2008-3-20
pubmed:abstractText
The nonstructural protein 1 (NS1) of flavivirus has two N-glycosylation sites that are thought to be important for viral replication. Effects of NS1 glycosylation site mutations on viral replication have been reported in several flaviviruses, but the results have differed. In this report, we examined the role of glycosylation site of NS1 on the replication of dengue type 1 virus (DENV-1). DENV-1 production was not detectable when full-length DENV-1 RNA, which has an N-glycosylation site Asn130-to-Ala (Asn130Ala) mutation in NS1, was transfected into mammalian and mosquito cells. However, replication and secretion of recombinant DENV-1 with the NS1 Asn130Ala mutation were recovered by exogenously expressed wild-type DENV-1 NS1. A growth kinetics experiment showed that propagation of wild-type DENV-1 was prevented by NS1 Asn130Ala mutant expression in trans. Our results suggest that Asn130 of the DENV-1 NS1 is important for viral replication in both mammalian and mosquito cells.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0920-8569
pubmed:author
pubmed:issnType
Print
pubmed:volume
36
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
323-9
pubmed:meshHeading
pubmed:year
2008
pubmed:articleTitle
Characterization of Asn130-to-Ala mutant of dengue type 1 virus NS1 protein.
pubmed:affiliation
Laboratory of Vector Borne Viruses, Department of Virology 1, National Institute of Infectious Diseases, 1-23-1 Toyama, Shinjuku, Tokyo 162-8640, Japan. stajima@nih.go.jp
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't