Source:http://linkedlifedata.com/resource/pubmed/id/17147624
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
6
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| pubmed:dateCreated |
2006-12-6
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| pubmed:abstractText |
Using plants as production factories for therapeutic proteins requires modification of their N-glycosylation pattern because of the immunogenicity of plant-specific sugar residues. In an attempt towards such humanization, we disrupted the genes for alpha1,3-fucosyltransferase and beta1,2-xylosyltransferase in Physcomitrella patens by homologous recombination. The single Deltafuc-t and Deltaxyl-t plants, as well as the double knockout, lacked transcripts of the corresponding genes, but did not differ from the wild-type moss in morphology, growth, development, and ability to secrete a recombinant protein, the human vascular endothelial growth factor VEGF(121), into the culture medium. N-Glycan analysis, however, revealed the absence of 1,3-fucosyl and/or 1,2-xylosyl residues, respectively. Therefore, the modifications described here represent the key step towards the generation of moss lines suitable for the production of plant-made glycosylated biopharmaceuticals with nonallergenic N-glycans.
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| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:status |
PubMed-not-MEDLINE
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| pubmed:month |
Nov
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| pubmed:issn |
1467-7652
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| pubmed:author | |
| pubmed:issnType |
Electronic
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| pubmed:volume |
2
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
517-23
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| pubmed:year |
2004
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| pubmed:articleTitle |
Targeted knockouts of Physcomitrella lacking plant-specific immunogenic N-glycans.
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| pubmed:affiliation |
University of Freiburg, Plant Biotechnology, Schaenzlestr. 1, 79104 Freiburg, Germany.
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| pubmed:publicationType |
Journal Article
|