Linked Life Data

11400096

Source:http://linkedlifedata.com/resource/pubmed/id/11400096

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2001-6-11
pubmed:abstractText
The major advantages of using the baculovirus-insect cell system for recombinant protein production are its ability to produce large amounts of recombinant proteins and its ability to provide eucaryotic modifications, such as glycosylation. However, the glycans linked to recombinant glycoproteins produced by this system typically differ from those found on native mammalian products. This is an important problem because glycans on mammalian glycoproteins can influence their functions in many different ways. The inability of baculovirus-infected insect cells to produce glycans identical to those found on native mammalian glycoproteins is due, in part, to the absence of functional levels of certain glycosyltransferases in insect cells. Thus, the purpose of this study was to engineer these activities into Tn-5B1-4, an established insect cell line that is widely used as a host for baculovirus-mediated protein production. Expression plasmids were constructed in which cDNAs encoding mammalian beta1,4-galactosyltransferase and alpha2,6-sialyltransferase were placed under the transcriptional control of a baculovirus immediate early promoter. These plasmids were then used to isolate two different transgenic Tn-5B1-4 derivatives and the biological and biochemical properties of these cell lines were examined. The results show that both of the engineered insect cell lines have improved glycoprotein-processing capabilities, relative to the parental cell line.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0006-3592
pubmed:author
pubmed:copyrightInfo
Copyright 2001 John Wiley & Sons, Inc.
pubmed:issnType
Print
pubmed:day
5
pubmed:volume
74
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
230-9
pubmed:dateRevised
2011-8-1
pubmed:meshHeading
pubmed:year
2001
pubmed:articleTitle
Improved glycosylation of a foreign protein by Tn-5B1-4 cells engineered to express mammalian glycosyltransferases.
pubmed:affiliation
Department of Molecular Biology, University of Wyoming, P.O. Box 3944, Laramie, WY 82071-3944, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S.