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dc.contributor.authorWanida Saejungen_US
dc.contributor.authorChunya Puttikhunten_US
dc.contributor.authorTanapan Prommoolen_US
dc.contributor.authorPunchapat Sojikulen_US
dc.contributor.authorRyoji Tanakaen_US
dc.contributor.authorKazuhito Fujiyamaen_US
dc.contributor.authorPrida Malasiten_US
dc.contributor.authorTatsuji Sekien_US
dc.contributor.otherOsaka Universityen_US
dc.contributor.otherThailand National Center for Genetic Engineering and Biotechnologyen_US
dc.contributor.otherMahidol Universityen_US
dc.contributor.otherFaculty of Medicine, Thammasat Universityen_US
dc.date.accessioned2018-08-20T06:49:41Z-
dc.date.available2018-08-20T06:49:41Z-
dc.date.issued2006-10-01en_US
dc.identifier.citationJournal of Bioscience and Bioengineering. Vol.102, No.4 (2006), 333-339en_US
dc.identifier.issn13891723en_US
dc.identifier.other2-s2.0-33751257489en_US
dc.identifier.urihttps://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=33751257489&origin=inwarden_US
dc.identifier.urihttp://repository.li.mahidol.ac.th/dspace/handle/123456789/22970-
dc.description.abstractThe 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.en_US
dc.rightsMahidol Universityen_US
dc.source.urihttps://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=33751257489&origin=inwarden_US
dc.subjectBiochemistry, Genetics and Molecular Biologyen_US
dc.subjectChemical Engineeringen_US
dc.titleEnhancement of recombinant soluble dengue virus 2 envelope domain III protein production in Escherichia coli trxB and gor double mutanten_US
dc.typeArticleen_US
dc.rights.holderSCOPUSen_US
dc.identifier.doi10.1263/jbb.102.333en_US
Appears in Collections:Scopus 2006-2010

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