Linked Life Data

17678502

Source:http://linkedlifedata.com/resource/pubmed/id/17678502

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
2007-8-6
pubmed:abstractText
In recent years, plants have become an attractive alternative for the production of recombinant proteins. However, their inability to perform authentic mammalian N-glycosylation may cause limitations for the production of therapeutics. A major concern is the presence of beta1,2-xylose and core alpha1,3-fucose residues on complex N-linked glycans, as these N-glycan epitopes are immunogenic in mammals. In our attempts towards the humanization of plant N-glycans, we have generated an Arabidopsis thaliana knockout line that synthesizes complex N-glycans lacking immunogenic xylose and fucose epitopes. Here, we report the expression of a monoclonal antibody in these glycan-engineered plants that carry a homogeneous mammalian-like complex N-glycan pattern without beta1,2-xylose and core alpha1,3-fucose. Plant and Chinese hamster ovary (CHO)-derived immunoglobulins (IgGs) exhibited no differences in electrophoretic mobility and enzyme-linked immunosorbent specificity assays. Our results demonstrate the feasibility of a knockout strategy for N-glycan engineering of plants towards mammalian-like structures, thus providing a significant improvement in the use of plants as an expression platform.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
1467-7652
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
5
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
657-63
pubmed:meshHeading
pubmed:year
2007
pubmed:articleTitle
Production of a monoclonal antibody in plants with a humanized N-glycosylation pattern.
pubmed:affiliation
Institute of Applied Genetics and Cell Biology, BOKU-Wien, Austria.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't