- About this Journal
- Abstracting and Indexing
- Aims and Scope
- Annual Issues
- Article Processing Charges
- Articles in Press
- Author Guidelines
- Bibliographic Information
- Citations to this Journal
- Contact Information
- Editorial Board
- Editorial Workflow
- Free eTOC Alerts
- Publication Ethics
- Reviewers Acknowledgment
- Submit a Manuscript
- Subscription Information
- Table of Contents
BioMed Research International
Volume 2013 (2013), Article ID 343195, 6 pages
High-Level Expression of Functionally Active Dengue-2 Non-Structural Antigen 1 Production in Escherichia coli
1Department of Biotechnology, Anna University, BIT Campus, Tiruchirappalli 620 024, India
2Centre for Research in Medical Entomology (CRME) (WHO Collaborating Centre for Lymphatic Filariasis and Dengue), Indian Council of Medical Research, Chinna Chokkikulam, Madurai 625 002, India
Received 30 April 2013; Revised 2 August 2013; Accepted 6 August 2013
Academic Editor: Decheng Yang
Copyright © 2013 S. Gowri Sankar et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
- D. Guha-Sapir and B. Schimmer, “Dengue fever: new paradigms for a changing epidemiology,” Emerging Themes in Epidemiology, vol. 2, p. 12005, 2005.
- R. V. Gibbons and D. W. Vaughn, “Dengue: an escalating problem,” British Medical Journal, vol. 324, no. 7353, pp. 1563–1566, 2002.
- B. D. Lindenbach and C. M. Rice, “Molecular biology of flaviviruses,” Advances in Virus Research, vol. 59, pp. 23–61, 2003.
- A. Sampath and R. Padmanabhan, “Molecular targets for flavivirus drug discovery,” Antiviral Research, vol. 81, no. 1, pp. 6–15, 2009.
- P. R. Young, P. A. Hilditch, C. Bletchly, and W. Halloran, “An antigen capture enzyme-linked immunosorbent assay reveals high levels of the dengue virus protein NS1 in the sera of infected patients,” Journal of Clinical Microbiology, vol. 38, no. 3, pp. 1053–1057, 2000.
- M. Flamand, F. Megret, M. Mathieu, J. Lepault, F. A. Rey, and V. Deubel, “Dengue virus type 1 nonstructural glycoprotein NS1 is secreted from mammalian cells as a soluble hexamer in a glycosylation-dependent fashion,” Journal of Virology, vol. 73, no. 7, pp. 6104–6110, 1999.
- C.-F. Lin, H.-Y. Lei, A.-L. Shiau et al., “Antibodies from dengue patient sera cross-react with endothelial cells and induce damage,” Journal of Medical Virology, vol. 69, no. 1, pp. 82–90, 2003.
- S. G. Sankar, K. J. Dhananjeyan, R. Paramasivan, V. Thenmozhi, B. K. Tyagi, and S. J. Vennison, “Evaluation and use of NS1 IgM antibody detection for acute dengue virus diagnosis: report from an outbreak investigation,” Clinical Microbiology and Infection, vol. 18, no. 1, pp. E8–E10, 2012.
- H. P. Sørensen and K. K. Mortensen, “Soluble expression of recombinant proteins in the cytoplasm of Escherichia coli,” Microbial Cell Factories, vol. 4, article 1, 2005.
- B. J. Olson and J. Markwell, “Assays for determination of protein concentration,” in Current Protocols in Protein Science, J. E. Coligan, B. M. Dunn, B. W. Speicher, P. T. Wingfield, and H. L. Ploegh, Eds., pp. 3.4.12–3.4.13, John Wiley & Sons, New York, NY, USA, 2007.
- R. S. Lanciotti, C. H. Calisher, D. J. Gubler, G.-J. Chang, and A. V. Vorndam, “Rapid detection and typing of dengue viruses from clinical samples by using reverse transcriptase-polymerase chain reaction,” Journal of Clinical Microbiology, vol. 30, no. 3, pp. 545–551, 1992.
- A. K. I. Falconar, “Antibody responses are generated to immunodominant ELK/KLE-type motifs on the nonstructural-1 glycoprotein during live dengue virus infections in mice and humans: Implications for diagnosis, pathogenesis, and vaccine design,” Clinical and Vaccine Immunology, vol. 14, no. 5, pp. 493–504, 2007.
- D. V. Goeddel, “Systems for heterologous gene expression,” Methods in Enzymology, vol. 185, pp. 3–7, 1990.
- S. C. Makrides, “Strategies for achieving high-level expression of genes in Escherichia coli,” Microbiological Reviews, vol. 60, no. 3, pp. 512–538, 1996.
- A. P. J. Middelberg, “Preparative protein refolding,” Trends in Biotechnology, vol. 20, no. 10, pp. 437–443, 2002.
- H. P. Sørensen, H. U. Sperling-Petersen, and K. K. Mortensen, “Dialysis strategies for protein refolding: preparative streptavidin production,” Protein Expression and Purification, vol. 31, no. 1, pp. 149–154, 2003.
- A. Villaverde and M. M. Carrió, “Protein aggregation in recombinant bacteria: biological role of inclusion bodies,” Biotechnology Letters, vol. 25, no. 17, pp. 1385–1395, 2003.
- T. J. Chambers, C. S. Hahn, R. Galler, and C. M. Rice, “Flavivirus genome organization, expression, and replication,” Annual Review of Microbiology, vol. 44, pp. 649–688, 1990.
- B. D. Lindenbach and C. M. Rice, “Trans-complementation of yellow fever virus NS1 reveals a role in early RNA replication,” Journal of Virology, vol. 71, no. 12, pp. 9608–9617, 1997.
- J.-L. Huang, J.-H. Huang, R.-H. Shyu et al., “High-level expression of recombinant dengue viral NS-1 protein and its potential use as a diagnostic antigen,” Journal of Medical Virology, vol. 65, no. 3, pp. 553–560, 2001.
- L. Lazaro-Olán, G. Mellado-Sánchez, J. García-Cordero et al., “Analysis of antibody response in human dengue patients from the Mexican coast using recombinant antigens,” Vector-Borne and Zoonotic Diseases, vol. 8, no. 1, pp. 69–79, 2008.
- D. Das, S. Mongkolaungkoon, and M. R. Suresh, “Super induction of dengue virus NS1 protein in E. coli,” Protein Expression and Purification, vol. 66, no. 1, pp. 66–72, 2009.
- J. H. Amorim, B. F. M. M. Porchia, A. Balan et al., “Refolded dengue virus type 2 NS1 protein expressed in Escherichia coli preserves structural and immunological properties of the native protein,” Journal of Virological Methods, vol. 167, no. 2, pp. 186–192, 2010.
- J.-M. Zhou, Y.-X. Tang, D.-Y. Fang et al., “Secreted expression and purification of dengue 2 virus full-length nonstructural glycoprotein NS1 in Pichia pastoris,” Virus Genes, vol. 33, no. 1, pp. 27–32, 2006.
- C. Wei, B. Tang, Y. Zhang, and K. Yang, “Oxidative refolding of recombinant prochymosin,” Biochemical Journal, vol. 340, no. 1, pp. 345–351, 1999.
- J.-Q. Guo, S.-Y. You, L. Li, Y.-Z. Zhang, J.-N. Huang, and C.-Y. Zhang, “Construction and high-level expression of a single-chain Fv antibody fragment specific for acidic isoferritin in Escherichia coli,” Journal of Biotechnology, vol. 103, no. 3, pp. 285–286, 2003.
- E. R. LaVallie, E. A. DiBlasio, S. Kovacic, K. L. Grant, P. F. Schendel, and J. M. McCoy, “A thioredoxin gene fusion expression system that circumvents inclusion body formation in the E. coli cytoplasm,” Bio/Technology, vol. 11, no. 2, pp. 187–193, 1993.
- R. Kern, A. Malki, A. Holmgren, and G. Richarme, “Chaperone properties of Escherichia coli thioredoxin and thioredoxin reductase,” Biochemical Journal, vol. 371, no. 3, pp. 965–972, 2003.
- P. Jurado, V. De Lorenzo, and L. A. Fernández, “Thioredoxin fusions increase folding of single chain Fv antibodies in the cytoplasm of Escherichia coli: evidence that chaperone activity is the prime effect of thioredoxin,” Journal of Molecular Biology, vol. 357, no. 1, pp. 49–61, 2006.
- R. B. Lobell and R. F. Schleif, “DNA looping and unlooping by AraC protein,” Science, vol. 250, no. 4980, pp. 528–532, 1990.
- L.-M. Guzman, D. Belin, M. J. Carson, and J. Beckwith, “Tight regulation, modulation, and high-level expression by vectors containing the arabinose P(BAD) promoter,” Journal of Bacteriology, vol. 177, no. 14, pp. 4121–4130, 1995.