Please use this identifier to cite or link to this item:
https://doi.org/10.1016/S0166-0934(97)00151-1
DC Field | Value | |
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dc.title | The production of recombinant dengue virus E protein using Escherichia coli and Pichia pastoris | |
dc.contributor.author | Sugrue, R.J. | |
dc.contributor.author | Cui, T. | |
dc.contributor.author | Xu, Q. | |
dc.contributor.author | Fu, J. | |
dc.contributor.author | Cheong Chan, Y. | |
dc.date.accessioned | 2014-11-28T02:53:29Z | |
dc.date.available | 2014-11-28T02:53:29Z | |
dc.date.issued | 1997-12 | |
dc.identifier.citation | Sugrue, R.J., Cui, T., Xu, Q., Fu, J., Cheong Chan, Y. (1997-12). The production of recombinant dengue virus E protein using Escherichia coli and Pichia pastoris. Journal of Virological Methods 69 (1-2) : 159-169. ScholarBank@NUS Repository. https://doi.org/10.1016/S0166-0934(97)00151-1 | |
dc.identifier.issn | 01660934 | |
dc.identifier.uri | http://scholarbank.nus.edu.sg/handle/10635/112126 | |
dc.description.abstract | The dengue virus envelope protein was expressed as a GST fusion protein using E. coli and P. pastoris as expression hosts. In E. coli the recombinant E protein is expressed initially as a soluble 81 kDa GST fusion protein. Treatment of the fusion protein with thrombin released a 55 kDa protein, which is the expected size for correctly processed, non-glycosylated recombinant E protein. The antiserum from animals immunised with this recombinant E protein was found to specifically recognise the dengue virus E protein in virus-infected cells, thus demonstrating the immunogenic nature of the recombinant E protein. This expression system allowed production of up to 2 mg of purified recombinant E protein from a 1 l bacterial culture. In contrast, expression of this GST fusion protein in P. pastoris is associated with extensive proteolytic degradation of the recombinant E protein. However, this proteolytic degradation was not observed in the truncated E protein sequences which were expressed. One of these recombinant fusion proteins, GST E401 was secreted into the culture medium at levels of up to 100 μg/l of growth medium. | |
dc.description.uri | http://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1016/S0166-0934(97)00151-1 | |
dc.source | Scopus | |
dc.subject | Envelope protein | |
dc.subject | Escherichia coli | |
dc.subject | Flavivirus | |
dc.subject | Glutathione s-transferse | |
dc.subject | Pichia pastoris | |
dc.type | Article | |
dc.contributor.department | INSTITUTE OF MOLECULAR & CELL BIOLOGY | |
dc.description.doi | 10.1016/S0166-0934(97)00151-1 | |
dc.description.sourcetitle | Journal of Virological Methods | |
dc.description.volume | 69 | |
dc.description.issue | 1-2 | |
dc.description.page | 159-169 | |
dc.description.coden | JVMED | |
dc.identifier.isiut | 000071972600017 | |
Appears in Collections: | Staff Publications |
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