Controlled expression of cholera toxin B subunit from Vibrio cholerae in Escherichia coli

Pakistan Journal of Biological Sciences

Volumn 11, Issue 13, 2008, Pages 1718-1722

  Haryanti, T ^a   Mariana, N S ^a   Latifah, S Y ^a   Yusoff, K ^a   Raha, Abdul Rahim ^a  

^a UNIVERSITY PUTRA MALAYSIA   (Malaysia)

Author keywords

Cloning; ctxB gene; E. Coli; Expression; Vibrio cholerae

Indexed keywords

ESCHERICHIA COLI; VIBRIO CHOLERAE;

CHOLERA TOXIN;

ARTICLE; ESCHERICHIA COLI; GENE EXPRESSION; GENE VECTOR; GENETICS; METABOLISM; VIBRIO CHOLERAE;

CHOLERA TOXIN; ESCHERICHIA COLI; GENE EXPRESSION; GENETIC VECTORS; VIBRIO CHOLERAE;

EID: 54049112279     PISSN: 10288880     EISSN: 18125735     Source Type: Journal    
DOI: 10.3923/pjbs.2008.1718.1722     Document Type: Article

References (26)

1. Bergerot, I., C. Ploix, J. Petersen, V. Moulin, C. Rask, N. Fabien, M. Lindblad, A. Mayer, C. Czerkinsky, J. Holmgren and C. Thivolet, 1997. A cholera toxoid-insulin conjugate as an oral vaccine against spontaneous autoimmune diabetes. Proc. Natl. Acad. Sci., 94: 4610-4614.
2. Bergquist, C., E.L. Johansson, T. Lagergard, J. Holmgren and A. Rudin, 1997. Intranasal vaccination of humans with recombinant cholera toxin B subunit induces systemic and local antibody responses in the upper respiratory tract and the vagina. Infect. Immun., 65: 2676-2684.
3. Bimboim, H.C. and J. Doly, 1979. A rapid alkaline extraction procedure for screening recombinant plasmid DNA. Nucleic Acids Res., 7: 1513-1523.
4. Boomershine, W.P., M.L. Stephen Raj, V. Gopalan and M.P. Fostera, 2003. Preparation of uniformly labeled NMR samples in Escherichia coli under the tight control of the araBAD promoter: Expression of an archaeal homolog of the RNase P Rpp29 protein. Protein Express Punf., 28: 246-251.
5. Briles, D.E., E. Ades, J.C. Paton, J.S. Sampson, G.M. Carlone, R.C. Huebner, A. Virolainen, E. Swiatlo and S.K. Hollingshead, 2000. Intranasal immunization of mice with a mixture of the pneumococcal proteins PsaA and PspA is highly protective against nasopharyngeal carriage of Streptococcus pneumoniae. Infect. Immun., 68: 796-800.
6. BAD. Immunotechnology, 3: 217-226.
7. de Mattos Arêas, A.P, M.L.S. de Oliveira, C.R.R. Ramos, M.E. Sbrogio-Almeida, I, Raw and P. Lee Hoa, 2002. Synthesis of cholera toxin B subunit gene: Cloning and expression of a functional 6XHis-tagged protein in Escherichia coli. Protein Express Purif., 25: 481-487.
8. Guzman, L.M., D. Belin, M.J. Carson and J. Beckwith, 1995. Tight regulation, modulation and high-level expression by vectors containing the arabinose PBAD promoter. J. Bacteriol., 177: 4121-4130.
9. Hagiwara, Y, K. Komase, Z. Chen, K. Matsuo, Y. Suzuki, C. Aizawa, T. Kurata and S. Tamura, 1999. Mutants of cholera toxin as an effective and safe adjuvant for nasal influenza vaccine. Vaccine, 17: 2918-2926.
10. Johnson, C.M. and R.F. Schleif, 1995. In vivo induction kinetics of the arabinose promoters in Escherichia coli. J. Bacteriol., 177: 3438-3442.
11. Kozuka, S, Y. Yasuda, M. Isaka, N. Masaki, T. Taniguchi, K. Matano, A. Moriyama, K. Ohkuma, N. Goto, S. Udaka and K. Tochikubo, 2000. Efficient extracellular production of recombinant Escherichia coli heat-labile enterotoxin B subunit by using the expression/secretion system of Bacillus brevis and its mucosal immunoadjuvancity. Vaccine, 18: 1730-1737.
12. 4. Nature, 227: 680-685.
13. Lebens, M, V. Shahabi, M. Bäckström, T. Houze, M. Lindblad and J. Holmgren, 1996. Synthesis of hybrid molecules between heat labile enterotoxin and cholera toxin B subunits: Potential for use in a broad-spectrum vaccine. Infect. Immun., 64: 2144-2150.
14. Lee, K.Y., J.D. Hopkins, T.F. O'Brien and M. Syvanen, 1991. Gly-238-Ser substitution changes the substrate specificity of the SHV class A β-lactamases. Prot., 11: 45-51.
15. Lewis, G., I.W. Taylor, A.W. Nienow and C.J. Hewitt, 2004. The application of multi-parameter flow cytometry to the study of recombinant Escherichia coli batch fermentation process. J. Ind. Microbiol. Biotech., 31: 311-322.
16. L'hoir, C., A. Renard and J.A. Martial, 1990. Expression in Escherichia coli of two mutated genes encoding the cholera toxin B subunit. Gene, 89: 47-52.
17. Lobell, R.B. and R.F. Schleif, 1990. DNA looping and unlooping by AraC protein. Science, 250: 528-532.
18. Pascale, J.M., M.M. Shaw, P.J. Durant, A.A. Amador, M.S. Bartlett, J.W. Smith, R.L. Gregory and G.L. McLaughlin, 1999. Intranasal immunization confers protection against murine Pneumocystis carinii lung infection. Infect. Immun., 67: 805-809.
19. Rudin, A., G.C. Riise and J. Holmgren, 1999. Antibody responses in the lower respiratory tract and male urogenital tract in humans after nasal and oral vaccination with cholera toxin B subunit. Infect. Immun., 67: 2884-2890.
20. Sambrook, J., E.F. Fritsch and T. Maniatis, 1989. Molecular Cloning. A Laboratory Manual. 1st Edn. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York.
21. Sanchez, J. and J. Holmgren, 2005. Virulence factors, pathogenesis and vaccine protection in cholera and ETEC diarrhea. Curr. Opin. Immunol., 17: 388-398.
22. Snider, D.P., J.S. Marshall, M.H. Perdue and H. Liang, 1994. Production of IgE antibody and allergic sensitization of intestinal and peripheral tissues after oral immunization with protein Ag and cholera toxin. J. Immunol., 153: 647-657.
23. Tamura, S., Y. Samegai, H. Kurata, T. Nagamine, C. Aizawa and T. Kurata, 1988. Protection against influenza virus infection by vaccine inoculated intranasally with cholera toxin B subunit. Vaccine, 6: 409-413.
24. Tamura, S.I., Y. Shoji, K. Hashigucci, C. Aizawa, T. Kurata, 1994. Effect of cholera toxin adjuvant on IgE antibody response to orally or nasally administered ovalbumin. Vaccine, 12: 1238-1240.
25. Tang-Feldman, Y.J., G. Ackermann, J.P. Henderson, J. Silva Jr. and S.H. Cohen, 2002. One-step cloning and expression of Clostridium difficile toxin B gene (tcdB). Molecular Cellular Probes, 16: 179-183.
26. Wiedermann, U., B. Jahn-Schmid, M. Lindblad, C. Rask, J. Holmgren, D. Kraft and C. Ebner, 1999. Suppressive versus stimulatory effects of allergen/cholera toxoid (CTB) conjugates depending on the nature of the allergen in a murine model of type I allergy. Int. Immunol., 11: 1717-1724.