Linked Life Data

19918885

Source:http://linkedlifedata.com/resource/pubmed/id/19918885

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2010-2-15
pubmed:abstractText
Human 29IJ6 IgG was expressed in silkworm using a Bombyx mori nucleopolyhedrovirus (BmNPV) bacmid system. The mean amounts of 296IJ6 IgG produced in larval hemolymph and whole pupae were 30.1 microg/larva and 78.0 microg/pupa, respectively. The use of molecular chaperones including calreticulin (CRT), calnexin (CNX), and immunoglobulin heavy chain binding protein (BiP, GRP78) improved the production of 296IJ6 IgG secretion in the larvae fivefold. The total yield of recombinant 29IJ6 IgG was 239 microg/mL when coexpressed with CRT. However, the overexpression of molecular chaperones had negative effects on secretion. The N-linked glycans of secreted 296IJ6 IgG in silkworm hemolymph were dominated by paucimannose structures. Small amounts of GlcNAc residues linked to the Manalpha1,3 branch were detected. When molecular chaperones were coexpressed, the compositions of N-linked glycans in the IgG1 produced were unchanged compared with those produced without them. This suggests that N-glycosylation is controlled by a regulatory function in the Golgi apparatus even though the post-translational modification of 296IJ6 IgG was assisted by the coexpression of molecular chaperones. Therefore, if the glycosylation pathways that coexpress N-acetylglucosaminyltransferase, galactosyltransferase, and sialyltransferase could be improved, silkworm larvae might prove a useful system for producing human antibodies.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
1520-6033
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
26
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
232-8
pubmed:dateRevised
2011-5-26
pubmed:meshHeading
pubmed:articleTitle
Improved secretion of molecular chaperone-assisted human IgG in silkworm, and no alterations in their N-linked glycan structures.
pubmed:affiliation
Integrated Bioscience Section, Graduate School of Science and Technology, Shizuoka University, Shizuoka 422-8529, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't