Source:http://linkedlifedata.com/resource/pubmed/id/17179169
Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
|
pubmed:dateCreated |
2007-2-19
|
pubmed:abstractText |
In this study, we show that introduction of human N-acetylglucosaminyltransferase (GnT)-III gene into tobacco plants leads to highly efficient synthesis of bisected N-glycans. Enzymatically released N-glycans from leaf glycoproteins of wild-type and transgenic GnT-III plants were profiled by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF-MS) in native form. After labeling with 2-aminobenzamide, profiling was performed using normal-phase high-performance liquid chromatography with fluorescence detection, and glycans were structurally characterized by MALDI-TOF/TOF-MS and reverse-phase nano-liquid chromatography-MS/MS. These analyses revealed that most of the complex-type N-glycans in the plants expressing GnT-III were bisected and carried at least two terminal N-acetylglucosamine (GlcNAc) residues in contrast to wild-type plants, where a considerable proportion of N-glycans did not contain GlcNAc residues at the nonreducing end. Moreover, we have shown that the majority of N-glycans of an antibody produced in a plant expressing GnT-III is also bisected. This might improve the efficacy of therapeutic antibodies produced in this type of transgenic plant.
|
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Acetylglucosamine,
http://linkedlifedata.com/resource/pubmed/chemical/Antibodies,
http://linkedlifedata.com/resource/pubmed/chemical/N-Acetylglucosaminyltransferases,
http://linkedlifedata.com/resource/pubmed/chemical/Polysaccharides,
http://linkedlifedata.com/resource/pubmed/chemical/beta-1,4-mannosyl-glycoprotein...
|
pubmed:status |
MEDLINE
|
pubmed:month |
Mar
|
pubmed:issn |
0959-6658
|
pubmed:author |
pubmed-author:BakkerHansH,
pubmed-author:BoschDirkD,
pubmed-author:DeelderAndré MAM,
pubmed-author:FlorackDion E ADE,
pubmed-author:HelsperJohannes P F GJP,
pubmed-author:HokkeCornelis HCH,
pubmed-author:KoelemanCarolien A MCA,
pubmed-author:RouwendalGerard J AGJ,
pubmed-author:StoopenGeert MGM,
pubmed-author:WuhrerManfredM,
pubmed-author:van DieIrmaI
|
pubmed:issnType |
Print
|
pubmed:volume |
17
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
334-44
|
pubmed:meshHeading |
pubmed-meshheading:17179169-Acetylglucosamine,
pubmed-meshheading:17179169-Antibodies,
pubmed-meshheading:17179169-Carbohydrate Sequence,
pubmed-meshheading:17179169-Gene Expression,
pubmed-meshheading:17179169-Humans,
pubmed-meshheading:17179169-Molecular Sequence Data,
pubmed-meshheading:17179169-N-Acetylglucosaminyltransferases,
pubmed-meshheading:17179169-Plants, Genetically Modified,
pubmed-meshheading:17179169-Polysaccharides,
pubmed-meshheading:17179169-Spectrometry, Mass, Matrix-Assisted Laser...,
pubmed-meshheading:17179169-Tobacco,
pubmed-meshheading:17179169-Transgenes
|
pubmed:year |
2007
|
pubmed:articleTitle |
Efficient introduction of a bisecting GlcNAc residue in tobacco N-glycans by expression of the gene encoding human N-acetylglucosaminyltransferase III.
|
pubmed:affiliation |
Business Unit Bioscience, Plant Research International BV, Wageningen University and Research Centre, Droevendaalsesteeg 1 6708 PB Wageningen, The Netherlands. gerard.rouwendal@wur.nl
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|