| Improved secretion of molecular chaperone-assisted human IgG in silkworm, and no alterations in their N-linked glycan structures. | |
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MedLine Citation:
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PMID: 19918885 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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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. |
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Authors:
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Takashi Dojima; Takuya Nishina; Tatsuya Kato; Tsuyoshi Uno; Hirokazu Yagi; Koichi Kato; Hiroshi Ueda; Enoch Y Park |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't |
Journal Detail:
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Title: Biotechnology progress Volume: 26 ISSN: 1520-6033 ISO Abbreviation: Biotechnol. Prog. Publication Date: 2010 Jan-Feb |
Date Detail:
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Created Date: 2010-02-15 Completed Date: 2010-05-24 Revised Date: 2011-05-26 |
Medline Journal Info:
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Nlm Unique ID: 8506292 Medline TA: Biotechnol Prog Country: United States |
Other Details:
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Languages: eng Pagination: 232-8 Citation Subset: IM |
Affiliation:
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Integrated Bioscience Section, Graduate School of Science and Technology, Shizuoka University, Shizuoka 422-8529, Japan. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Animals Bombyx / chemistry, metabolism* Calnexin / biosynthesis, chemistry Calreticulin / biosynthesis, chemistry Golgi Apparatus / metabolism Heat-Shock Proteins / biosynthesis, chemistry Humans Immunoglobulin G / biosynthesis*, chemistry Molecular Chaperones / biosynthesis*, chemistry Nucleopolyhedrovirus / metabolism Polysaccharides / chemistry*, metabolism Recombinant Proteins / biosynthesis |
| Chemical | |
Reg. No./Substance:
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0/Calreticulin; 0/Heat-Shock Proteins; 0/Immunoglobulin G; 0/Molecular Chaperones; 0/Polysaccharides; 0/Recombinant Proteins; 0/molecular chaperone GRP78; 139873-08-8/Calnexin |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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