Simple jQuery Dropdowns
Please use this identifier to cite or link to this item:
Title: Enhancement of recombinant soluble dengue virus 2 envelope domain III protein production in Escherichia coli trxB and gor double mutant
Authors: Wanida Saejung
Chunya Puttikhunt
Tanapan Prommool
Punchapat Sojikul
Ryoji Tanaka
Kazuhito Fujiyama
Prida Malasit
Tatsuji Seki
Osaka University
Thailand National Center for Genetic Engineering and Biotechnology
Mahidol University
Faculty of Medicine, Thammasat University
Keywords: Biochemistry, Genetics and Molecular Biology;Chemical Engineering
Issue Date: 1-Oct-2006
Citation: Journal of Bioscience and Bioengineering. Vol.102, No.4 (2006), 333-339
Abstract: The dengue virus is currently the most important flavivirus causing human diseases in the tropical and subtropical regions of the world. The envelope protein domain III of dengue virus type 2 (D2EIII), which induces protective and neutralizing antibodies, was expressed as an N-terminal fusion to a hexa-histidine tag in Escherichia coli. The expression of recombinant D2EIII of 103 amino acids in the soluble form can be achieved using suitable host strains, such as Origami, at a low induction temperature of 18°C. The enhanced production of the soluble protein could be attributed to the thioredoxin reductase (trxB) and glutathione reductase (gor) double mutations in the Origami genome. The soluble and refolded D2EIII proteins were recognized by different antibodies including human patient antiserum. The immunization of rats with soluble D2EIII protein elicited the production of antibodies that could recognize the D2EIII protein in the D2EIII precursor protein and in C-terminal truncated dengue envelope protein type 1-4. Thus, this protein production system is suitable for the production of authentic recombinant dengue proteins that may be used in the diagnosis of the dengue virus infection or in vaccine development. © 2006 The Society for Biotechnology, Japan.
ISSN: 13891723
Appears in Collections:Scopus 2006-2010

Files in This Item:
There are no files associated with this item.

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.