Matches in UGent Biblio for { <https://biblio.ugent.be/publication/409442#aggregation> ?p ?o. }
Showing items 1 to 44 of
44
with 100 items per page.
- aggregation classification "A1".
- aggregation creator B337332.
- aggregation creator B337333.
- aggregation creator B337334.
- aggregation creator B337335.
- aggregation creator B337336.
- aggregation creator B337337.
- aggregation creator B337338.
- aggregation creator person.
- aggregation creator person.
- aggregation creator person.
- aggregation creator person.
- aggregation creator person.
- aggregation creator person.
- aggregation date "2007".
- aggregation format "application/pdf".
- aggregation hasFormat 409442.bibtex.
- aggregation hasFormat 409442.csv.
- aggregation hasFormat 409442.dc.
- aggregation hasFormat 409442.didl.
- aggregation hasFormat 409442.doc.
- aggregation hasFormat 409442.json.
- aggregation hasFormat 409442.mets.
- aggregation hasFormat 409442.mods.
- aggregation hasFormat 409442.rdf.
- aggregation hasFormat 409442.ris.
- aggregation hasFormat 409442.txt.
- aggregation hasFormat 409442.xls.
- aggregation hasFormat 409442.yaml.
- aggregation isPartOf urn:issn:0027-8424.
- aggregation language "eng".
- aggregation rights "I have transferred the copyright for this publication to the publisher".
- aggregation subject "Biology and Life Sciences".
- aggregation title "Aberrant localization and underglycosylation of highly accumulating single-chain Fv-Fc antibodies in transgenic Arabidopsis seeds".
- aggregation abstract "Production of high-value recombinant proteins in transgenic seeds is an attractive and economically feasible alternative to conventional systems based on mammalian cells and bacteria. In contrast to leaves, seeds allow high-level accumulation of recombinant proteins in a relatively small volume and a stable environment. We demonstrate that single-chain variable fragment (scFv)-Fc antibodies, with N-terminal signal sequence and C-terminal KDEL tag, can accumulate to very high levels as bivalent IgG-like antibodies in Arabidopsis thaliana seeds and illustrate that a plant-produced anti-hepatitis A virus scFv-Fc has similar antigen-binding and in vitro neutralizing activities as the corresponding full-length IgG. As expected, most scFv-Fc produced in seeds contained only oligomannose-type N-glycans, but, unexpectedly, 35-40% was never glycosylated. A portion of the scFv-Fc was found in endoplasmic reticulum (ER)-derived compartments delimited by ribosome-associated membranes. Additionally, consistent with the glycosylation data, large amounts of the recombinant protein were deposited in the periplasmic space, implying a direct transport from the ER to the periplasmic space between the plasma membrane and the cell wall. Aberrant localization of the ER chaperones calreticulin and binding protein (BiP) and the endogenous seed storage protein cruciferin in the periplasmic space suggests that overproduction of recombinant scFv-Fc disturbs normal ER retention and protein-sorting mechanisms in the secretory pathway.".
- aggregation authorList BK633675.
- aggregation endPage "1435".
- aggregation issue "4".
- aggregation startPage "1430".
- aggregation volume "104".
- aggregation aggregates 3067666.
- aggregation isDescribedBy 409442.
- aggregation similarTo pnas.0609997104.
- aggregation similarTo LU-409442.