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PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
2009-8-11
pubmed:abstractText
The envelope glycoproteins Gn and Gc are major determinants in the assembly of Tomato spotted wilt virus (TSWV) particles at the Golgi complex. In this article, the ER-arrest of singly expressed Gc and the transport of both glycoproteins to the Golgi upon coexpression have been analyzed.While preliminary results suggest that the arrest of Gc at the ER (endoplasmic reticulum) did not appear to result from improper folding, transient expression of chimeric Gc, in which the transmembrane domain (TMD) and/or cytoplasmic tail (CT) were swapped for those from Gn, showed that the TMD of Gn was sufficient to allow ER exit and transport to the Golgi. Expression of both glycoproteins in the presence of overexpressed Sar1p specific guanosine nucleotide exchange factor Sec12p, resulted in ER-retention demonstrating that the viral glycoproteins are transported to the Golgi in a COPII (coat protein II)-dependent manner. Inhibition of ER Golgi transport by brefeldin A (BFA) had a similar effect on the localization of Gn. However, inhibition of ER (endoplasmic reticulum) to Golgi transport of coexpressed Gc and Gn by overexpression of Sec12p or by BFA revealed distinct localization patterns, i.e. diffuse ER localization versus concentration at specific spots.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
1600-0854
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
10
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
664-72
pubmed:meshHeading
pubmed:year
2009
pubmed:articleTitle
Requirements for ER-arrest and sequential exit to the golgi of Tomato spotted wilt virus glycoproteins.
pubmed:affiliation
Wageningen University, Laboratory of Virology, 6709 PD Wageningen, The Netherlands.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't