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Volumn 17, Issue 5, 2010, Pages 784-792

Efficacy of a potential trivalent vaccine based on Hc fragments of botulinum toxins A, B, and E produced in a cell-free expression system

Author keywords

[No Author keywords available]

Indexed keywords

BOTULINUM TOXIN A; BOTULINUM TOXIN B; BOTULINUM TOXIN E; PROTEIN DISULFIDE ISOMERASE; RECOMBINANT PROTEIN; TRIPLE VACCINE;

EID: 77951985187     PISSN: 15566811     EISSN: 1556679X     Source Type: Journal    
DOI: 10.1128/CVI.00496-09     Document Type: Article
Times cited : (52)

References (58)
  • 4
    • 0025314995 scopus 로고
    • The complete sequence of botulinum neurotoxin type a and comparison with other clostridial neurotoxins
    • Binz, T., H. Kurazono, M. Wille, J. Frevert, K. Wernars, and H. Nieman. 1990. The complete sequence of botulinum neurotoxin type A and comparison with other clostridial neurotoxins. J. Biol. Chem. 265:9153-9158.
    • (1990) J. Biol. Chem. , vol.265 , pp. 9153-9158
    • Binz, T.1    Kurazono, H.2    Wille, M.3    Frevert, J.4    Wernars, K.5    Nieman, H.6
  • 5
    • 33744923162 scopus 로고    scopus 로고
    • Recombinant C fragment of botulinum neurotoxin B serotype (rBoNTB (Hc)) immune response and protection in the rhesus monkey
    • Boles, J., M. West, V. Montgomery, R. Tammariello, M. Pitt, P. Gibbs, L. Smith, and R. LeClaire. 2006. Recombinant C fragment of botulinum neurotoxin B serotype (rBoNTB (Hc)) immune response and protection in the rhesus monkey. Toxicon 47:877-884.
    • (2006) Toxicon , vol.47 , pp. 877-884
    • Boles, J.1    West, M.2    Montgomery, V.3    Tammariello, R.4    Pitt, M.5    Gibbs, P.6    Smith, L.7    LeClaire, R.8
  • 6
    • 0033748727 scopus 로고    scopus 로고
    • Development of vaccines for prevention of botulism
    • Byrne, M. P., and L. A. Smith. 2000. Development of vaccines for prevention of botulism. Biochimie 82:955-966.
    • (2000) Biochimie , vol.82 , pp. 955-966
    • Byrne, M.P.1    Smith, L.A.2
  • 7
    • 0034056247 scopus 로고    scopus 로고
    • Fermentation, purification, and efficacy of a recombinant vaccine candidate against botulinum type F from Pichia pastoris
    • Byrne, M. P., R.W. Titball, J. Holley, and L. A. Smith. 2000. Fermentation, purification, and efficacy of a recombinant vaccine candidate against botulinum type F from Pichia pastoris. Protein Expr. Purif. 18:327-337.
    • (2000) Protein Expr. Purif. , vol.18 , pp. 327-337
    • Byrne, M.P.1    Titball, R.W.2    Holley, J.3    Smith, L.A.4
  • 8
    • 23244440886 scopus 로고    scopus 로고
    • An economical method for cell-free protein synthesis using glucose and nucleoside monophosphates
    • Calhoun, K. A., and J. R. Swartz. 2005. An economical method for cell-free protein synthesis using glucose and nucleoside monophosphates. Biotechnol. Prog. 21:1146-1153.
    • (2005) Biotechnol. Prog. , vol.21 , pp. 1146-1153
    • Calhoun, K.A.1    Swartz, J.R.2
  • 9
    • 0029039466 scopus 로고
    • Protective vaccination with a recombinant fragment of Clostridium botulinum neurotoxin serotype A expressed from a synthetic gene in Escherichia coli
    • Clayton, M. A., M. J. Clayton, R. D. Brown, and J. L. Middlebrook. 1995. Protective vaccination with a recombinant fragment of Clostridium botulinum neurotoxin serotype A expressed from a synthetic gene in Escherichia coli. Infect. Immun. 63:2738-2742.
    • (1995) Infect. Immun. , vol.63 , pp. 2738-2742
    • Clayton, M.A.1    Clayton, M.J.2    Brown, R.D.3    Middlebrook, J.L.4
  • 10
    • 77951991497 scopus 로고    scopus 로고
    • Making bioprocess scale-up more robust
    • DePalma, A. 2009. Making bioprocess scale-up more robust. Genet. Eng. Biotechnol. News 29:44-47.
    • (2009) Genet. Eng. Biotechnol. News , vol.29 , pp. 44-47
    • DePalma, A.1
  • 12
    • 1242319564 scopus 로고    scopus 로고
    • In vitro synthesis of fully functional EmrE, a multidrug transporter, and study of its oligomeric state
    • Elbaz, Y., S. Steiner-Mordoch, T. Danieli, and S. Schuldiner. 2004. In vitro synthesis of fully functional EmrE, a multidrug transporter, and study of its oligomeric state. Proc. Natl. Acad. Sci. U. S. A. 101:1519-1524.
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 1519-1524
    • Elbaz, Y.1    Steiner-Mordoch, S.2    Danieli, T.3    Schuldiner, S.4
  • 13
    • 0023272674 scopus 로고
    • Immunization of mice against tetanus with fragments of tetanus toxin synthesized in Escherichia coli
    • Fairweather, N. F., V. A. Lyness, and D. J. Maskell. 1987. Immunization of mice against tetanus with fragments of tetanus toxin synthesized in Escherichia coli. Infect. Immun. 55:2541-2545.
    • (1987) Infect. Immun. , vol.55 , pp. 2541-2545
    • Fairweather, N.F.1    Lyness, V.A.2    Maskell, D.J.3
  • 14
    • 0012664409 scopus 로고    scopus 로고
    • The expression of disulfide bonded protein in cell-free protein expression
    • A. S. Spirin (ed.), Springer, Berlin, Germany
    • Fernholz, E., K. Zaiss, H. Besir, and W. Mutter. 2002. The expression of disulfide bonded protein in cell-free protein expression, p. 175-179. In A. S. Spirin (ed.), Cell-free translation systems. Springer, Berlin, Germany.
    • (2002) Cell-free Translation Systems , pp. 175-179
    • Fernholz, E.1    Zaiss, K.2    Besir, H.3    Mutter, W.4
  • 15
    • 75449125388 scopus 로고
    • Studies on immunity of Clostridium botulinum. IX. Immunologic response of man to purified pentavalent ABCDE botulinum toxoid
    • Fiock, M., M. A. Cardella, and N. F. Gearringer. 1963. Studies on immunity of Clostridium botulinum. IX. Immunologic response of man to purified pentavalent ABCDE botulinum toxoid. J. Immunol. 90:697-702.
    • (1963) J. Immunol. , vol.90 , pp. 697-702
    • Fiock, M.1    Cardella, M.A.2    Gearringer, N.F.3
  • 16
    • 0037468510 scopus 로고    scopus 로고
    • Maltodextrin-binding proteins from diverse bacteria and archaea are potent solubility enhancers
    • Fox, J. D., K. M. Routzahn, M. H. Bucher, and D. S. Waugh. 2003. Maltodextrin-binding proteins from diverse bacteria and archaea are potent solubility enhancers. FEBS Lett. 537:53-57.
    • (2003) FEBS Lett. , vol.537 , pp. 53-57
    • Fox, J.D.1    Routzahn, K.M.2    Bucher, M.H.3    Waugh, D.S.4
  • 17
    • 37349010476 scopus 로고    scopus 로고
    • Synthesis and characterization of a functional intact IgG in a prokaryotic cell-free expression system
    • Frey, S., M. Haslbeck, O. Hainzl, and J. Buchner. 2008. Synthesis and characterization of a functional intact IgG in a prokaryotic cell-free expression system. Biol. Chem. 389:37-45.
    • (2008) Biol. Chem. , vol.389 , pp. 37-45
    • Frey, S.1    Haslbeck, M.2    Hainzl, O.3    Buchner, J.4
  • 18
    • 38449099301 scopus 로고    scopus 로고
    • Development of cell-free protein synthesis platforms for disulfide bonded proteins
    • Goerke, A. R., and J. R. Swartz. 2008. Development of cell-free protein synthesis platforms for disulfide bonded proteins. Biotechnol. Bioeng. 99:351-367.
    • (2008) Biotechnol. Bioeng. , vol.99 , pp. 351-367
    • Goerke, A.R.1    Swartz, J.R.2
  • 19
    • 0034666747 scopus 로고    scopus 로고
    • Cloning, expression and evaluation of a recombinant sub-unit vaccine against Clostridium botulinum type F toxin
    • Holley, J. L., M. Elmore, M. Mauchline, N. Minton, and R. W. Titball. 2000. Cloning, expression and evaluation of a recombinant sub-unit vaccine against Clostridium botulinum type F toxin. Vaccine 19:288-297.
    • (2000) Vaccine , vol.19 , pp. 288-297
    • Holley, J.L.1    Elmore, M.2    Mauchline, M.3    Minton, N.4    Titball, R.W.5
  • 20
    • 1542720448 scopus 로고    scopus 로고
    • Mimicking the Escherichia coli cytoplasmic environment activates long-lived and efficient cell-free protein synthesis
    • Jewett, M. C., and J. R. Swartz. 2004. Mimicking the Escherichia coli cytoplasmic environment activates long-lived and efficient cell-free protein synthesis. Biotechnol. Bioeng. 86:19-26.
    • (2004) Biotechnol. Bioeng. , vol.86 , pp. 19-26
    • Jewett, M.C.1    Swartz, J.R.2
  • 21
    • 0037070555 scopus 로고    scopus 로고
    • Expression of Fab fragment of catalytic antibody 6D9 in an Escherichia coli in vitro coupled transcription/translation system
    • Jiang, X., Y. Ookubo, I. Fujii, H. Nakano, and T. Yamane. 2002. Expression of Fab fragment of catalytic antibody 6D9 in an Escherichia coli in vitro coupled transcription/translation system. FEBS Lett. 514:290-294.
    • (2002) FEBS Lett. , vol.514 , pp. 290-294
    • Jiang, X.1    Ookubo, Y.2    Fujii, I.3    Nakano, H.4    Yamane, T.5
  • 22
    • 0028954219 scopus 로고
    • A long-lived batch reaction system of cell-free protein synthesis
    • Kawarasaki, Y., T. Kawai, H. Nakano, and T. Yamane. 1995. A long-lived batch reaction system of cell-free protein synthesis. Anal. Biochem. 226:320-324.
    • (1995) Anal. Biochem. , vol.226 , pp. 320-324
    • Kawarasaki, Y.1    Kawai, T.2    Nakano, H.3    Yamane, T.4
  • 23
    • 0032923295 scopus 로고    scopus 로고
    • Cell-free production and stable-isotope labeling of milligram quantities of proteins
    • DOI 10.1016/S0014-5793(98)01620-2, PII S0014579398016202
    • Kigawa, T., T. Yabuki, Y. Yoshida, M. Tsutsui, Y. Ito, T. Shibata, and S. Yokoyama. 1999. Cell-free production and stable-isotope labeling of milligram quantities of proteins. FEBS Lett. 442:15-19. (Pubitemid 29065369)
    • (1999) FEBS Letters , vol.442 , Issue.1 , pp. 15-19
    • Kigawa, T.1    Yabuki, T.2    Yoshida, Y.3    Tsutsui, M.4    Ito, Y.5    Shibata, T.6    Yokoyama, S.7
  • 24
    • 4644350549 scopus 로고    scopus 로고
    • Cell-free expression of proteins containing multiple disulfide bonds
    • J. Swartz (ed.), Springer-Verlag, Heidelberg, Germany
    • Kim, D. M., E. Fernholz, and J. Swartz. 2003. cell-free expression of proteins containing multiple disulfide bonds, p. 125-131. In J. Swartz (ed.), cell-free protein expression. Springer-Verlag, Heidelberg, Germany.
    • (2003) Cell-free Protein Expression , pp. 125-131
    • Kim, D.M.1    Fernholz, E.2    Swartz, J.3
  • 25
    • 0034681011 scopus 로고    scopus 로고
    • Expression-independent consumption of substrates in cell-free expression system from Escherichia coli
    • Kim, R. G., and C. Y. Choi. 2001. Expression-independent consumption of substrates in cell-free expression system from Escherichia coli. J. Biotechnol. 84:27-32.
    • (2001) J. Biotechnol. , vol.84 , pp. 27-32
    • Kim, R.G.1    Choi, C.Y.2
  • 26
    • 33748307399 scopus 로고    scopus 로고
    • Cell-free expression as an emerging technique for the large scale production of integral membrane protein
    • Klammt, C., S. Daniel, F. Lohr, B. Schneider, V. Dotsch, and F. Bernhard. 2006. Cell-free expression as an emerging technique for the large scale production of integral membrane protein. FEBS J. 273:4141-4153.
    • (2006) FEBS J. , vol.273 , pp. 4141-4153
    • Klammt, C.1    Daniel, S.2    Lohr, F.3    Schneider, B.4    Dotsch, V.5    Bernhard, F.6
  • 27
    • 62649097660 scopus 로고    scopus 로고
    • Immunological characterization of the subunits of type A botulinum neurotoxin and different components of its associated proteins
    • Kukreja, R., T. W. Chang, S. Cai, P. Lindo, S. Riding, Y. Zhou, E. Ravichandran, and B. R. Singh. 2009. Immunological characterization of the subunits of type A botulinum neurotoxin and different components of its associated proteins. Toxicon 53:616-624.
    • (2009) Toxicon , vol.53 , pp. 616-624
    • Kukreja, R.1    Chang, T.W.2    Cai, S.3    Lindo, P.4    Riding, S.5    Zhou, Y.6    Ravichandran, E.7    Singh, B.R.8
  • 28
    • 0033520494 scopus 로고    scopus 로고
    • Sequence homology and structural analysis of the clostridial neurotoxins
    • Lacy, D. B., and R. C. Stevens. 1999. Sequence homology and structural analysis of the clostridial neurotoxins. J. Mol. Biol. 291:1091-1104.
    • (1999) J. Mol. Biol. , vol.291 , pp. 1091-1104
    • Lacy, D.B.1    Stevens, R.C.2
  • 29
    • 0028784961 scopus 로고
    • Expression of a large, nontoxic fragment of botulinum neurotoxin serotype A and its use as an immunogen
    • LaPenotiere, H. F., M. A. Clayton, and J. L. Middlebrook. 1995. Expression of a large, nontoxic fragment of botulinum neurotoxin serotype A and its use as an immunogen. Toxicon 33:1383-1386.
    • (1995) Toxicon , vol.33 , pp. 1383-1386
    • LaPenotiere, H.F.1    Clayton, M.A.2    Middlebrook, J.L.3
  • 30
    • 53149099323 scopus 로고    scopus 로고
    • In vitro translation of type a Clostridium botulinum neurotoxin heavy chain and analysis of its binding to rat synaptosomes
    • Li, L., and R. Singh. 1999. In vitro translation of type a Clostridium botulinum neurotoxin heavy chain and analysis of its binding to rat synaptosomes. J. Protein Chem. 18:89-95.
    • (1999) J. Protein Chem. , vol.18 , pp. 89-95
    • Li, L.1    Singh, R.2
  • 31
    • 0034681174 scopus 로고    scopus 로고
    • A highly efficient and robust cell-free protein synthesis system prepared from wheat embryos: Plants apparently contain a suicide system directed at ribosomes
    • Madin, K., T. Sawasaki, T. Ogasawara, and Y. Endo. 2000. A highly efficient and robust cell-free protein synthesis system prepared from wheat embryos: plants apparently contain a suicide system directed at ribosomes. Proc. Natl. Acad. Sci. U. S. A. 97:559-564.
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 559-564
    • Madin, K.1    Sawasaki, T.2    Ogasawara, T.3    Endo, Y.4
  • 32
    • 0024787893 scopus 로고
    • Expression of tetanus toxin fragment C in E. coli: High level expression by removing rare codons
    • Makoff, A. J., M. D. Oxer, M. A. Romanos, N. F. Fairweather, and S. Ballantine. 1989. Expression of tetanus toxin fragment C in E. coli: high level expression by removing rare codons. Nucleic Acids Res. 17:10191-10202.
    • (1989) Nucleic Acids Res. , vol.17 , pp. 10191-10202
    • Makoff, A.J.1    Oxer, M.D.2    Romanos, M.A.3    Fairweather, N.F.4    Ballantine, S.5
  • 33
    • 0031559892 scopus 로고    scopus 로고
    • Direct expression of PCR products in a cell-free transcription/ translation system: Synthesis of antibacterial peptide cecropin
    • Martemyanov, K. A., A. S. Spirin, and A. T. Gudkov. 1997. Direct expression of PCR products in a cell-free transcription/translation system: synthesis of antibacterial peptide cecropin. FEBS Lett. 414:268-270.
    • (1997) FEBS Lett. , vol.414 , pp. 268-270
    • Martemyanov, K.A.1    Spirin, A.S.2    Gudkov, A.T.3
  • 34
    • 4644317426 scopus 로고    scopus 로고
    • Expression-PCR: From gene pools to purified proteins within 1 day
    • J. Swartz (ed.), Springer-Verlag, Heidelberg, Germany
    • Merk, H., D. Meschkat, and W. Stiege. 2003. Expression-PCR: from gene pools to purified proteins within 1 day, p. 15-23. In J. Swartz (ed.), Cell-free protein expression. Springer-Verlag, Heidelberg, Germany.
    • (2003) Cell-free Protein Expression , pp. 15-23
    • Merk, H.1    Meschkat, D.2    Stiege, W.3
  • 35
    • 0028876404 scopus 로고
    • Protection strategies against botulinum toxin
    • Middlebrook, J. L. 1995. Protection strategies against botulinum toxin. Adv. Exp. Med. Biol. 383:93-98.
    • (1995) Adv. Exp. Med. Biol. , vol.383 , pp. 93-98
    • Middlebrook, J.L.1
  • 36
    • 0034050548 scopus 로고    scopus 로고
    • Overexpression of trigger factor prevents aggregation of recombinant proteins in Escherichia coli
    • Nishihara, K., M. Kanemori, H. Yanagi, and T. Yura. 2000. Overexpression of trigger factor prevents aggregation of recombinant proteins in Escherichia coli. Appl. Environ. Microbiol. 66:884-889.
    • (2000) Appl. Environ. Microbiol. , vol.66 , pp. 884-889
    • Nishihara, K.1    Kanemori, M.2    Yanagi, H.3    Yura, T.4
  • 39
    • 0025758727 scopus 로고
    • Expression of tetanus toxin fragment C in yeast: Gene synthesis is required to eliminate fortuitous polyadenylation sites in AT-rich DNA
    • Romanos, M. A., A. J. Makoff, N. F. Fairweather, K. M. Beesley, D. E. Slater, F. B. Rayment, M. M. Payne, and J. J. Clare. 1991. Expression of tetanus toxin fragment C in yeast: gene synthesis is required to eliminate fortuitous polyadenylation sites in AT-rich DNA. Nucleic Acids Res. 19:1461-1467.
    • (1991) Nucleic Acids Res. , vol.19 , pp. 1461-1467
    • Romanos, M.A.1    Makoff, A.J.2    Fairweather, N.F.3    Beesley, K.M.4    Slater, D.E.5    Rayment, F.B.6    Payne, M.M.7    Clare, J.J.8
  • 41
    • 0031772527 scopus 로고    scopus 로고
    • Development of recombinant vaccines for botulinum neurotoxin
    • Smith, L. A. 1998. Development of recombinant vaccines for botulinum neurotoxin. Toxicon 36:1539-1548.
    • (1998) Toxicon , vol.36 , pp. 1539-1548
    • Smith, L.A.1
  • 43
    • 38049093742 scopus 로고    scopus 로고
    • Botulinum neurotoxin vaccines: Past, present, and future
    • Smith, L. A., and J. M. Rusnak. 2007. Botulinum neurotoxin vaccines: past, present, and future. Crit. Rev. Immunol. 27:303-318.
    • (2007) Crit. Rev. Immunol. , vol.27 , pp. 303-318
    • Smith, L.A.1    Rusnak, J.M.2
  • 45
    • 0024297305 scopus 로고
    • A continuous cell-free translation system capable of producing polypeptides in high yield
    • Spirin, A. S., V. I. Baranov, L. A. Ryabova, S. Y. Ovodov, and Y. B. Alakhov. 1988. A continuous cell-free translation system capable of producing polypeptides in high yield. Science 242:1162-1164.
    • (1988) Science , vol.242 , pp. 1162-1164
    • Spirin, A.S.1    Baranov, V.I.2    Ryabova, L.A.3    Ovodov, S.Y.4    Alakhov, Y.B.5
  • 46
    • 33745035191 scopus 로고    scopus 로고
    • Developing cell-free biology for industrial applications
    • Swartz, J. 2006. Developing cell-free biology for industrial applications. J. Ind. Microbiol. Biotechnol. 33:476-485.
    • (2006) J. Ind. Microbiol. Biotechnol. , vol.33 , pp. 476-485
    • Swartz, J.1
  • 47
    • 63449094093 scopus 로고    scopus 로고
    • Localization of the sites and characterization of the mechanisms by which anti-light chain antibodies neutralize the actions of the botulinum holotoxin
    • Takahashi, T., S. G. Joshi, F. Al-Saleem, D. Ancharski, A. Singh, Z. Nasser, and L. L. Simpson. 2009. Localization of the sites and characterization of the mechanisms by which anti-light chain antibodies neutralize the actions of the botulinum holotoxin. Vaccine 27:2616-2624.
    • (2009) Vaccine , vol.27 , pp. 2616-2624
    • Takahashi, T.1    Joshi, S.G.2    Al-Saleem, F.3    Ancharski, D.4    Singh, A.5    Nasser, Z.6    Simpson, L.L.7
  • 50
    • 23244462601 scopus 로고    scopus 로고
    • Efficient and scalable method for scaling up cell free protein synthesis in batch mode
    • Voloshin, A. M., and J. R. Swartz. 2005. Efficient and scalable method for scaling up cell free protein synthesis in batch mode. Biotechnol. Bioeng. 91:516-521.
    • (2005) Biotechnol. Bioeng. , vol.91 , pp. 516-521
    • Voloshin, A.M.1    Swartz, J.R.2
  • 51
    • 0027520038 scopus 로고
    • Synthesis of preparative amounts of biologically active interleukin- 6 using a continuous-flow cell-free translation system
    • Volyanik, E. V., A. Dalley, I. A. McKay, I. Leigh, N. S. Williams, and S. A. Bustin. 1993. Synthesis of preparative amounts of biologically active interleukin- 6 using a continuous-flow cell-free translation system. Anal. Biochem. 214:289-294.
    • (1993) Anal. Biochem. , vol.214 , pp. 289-294
    • Volyanik, E.V.1    Dalley, A.2    McKay, I.A.3    Leigh, I.4    Williams, N.S.5    Bustin, S.A.6
  • 52
    • 67649378415 scopus 로고    scopus 로고
    • Production of catalytically inactive BoNT/A1 holoprotein and comparison with BoNT/A1 subunit vaccines against toxin subtypes A1, A2, and A3
    • Webb, R. P., T. J. Smith, P. Wright, J. Brown, and L. A. Smith. 2009. Production of catalytically inactive BoNT/A1 holoprotein and comparison with BoNT/A1 subunit vaccines against toxin subtypes A1, A2, and A3. Vaccine 27:4490-4497.
    • (2009) Vaccine , vol.27 , pp. 4490-4497
    • Webb, R.P.1    Smith, T.J.2    Wright, P.3    Brown, J.4    Smith, L.A.5
  • 53
    • 34247325141 scopus 로고    scopus 로고
    • Protection with recombinant Clostridium botulinum C1 and D binding domain subunit (Hc) vaccines against C and D neurotoxins
    • Webb, R. P., T. J. Smith, P. M. Wright, V. A. Montgomery, M. M. Meagher, and L. A. Smith. 2007. Protection with recombinant Clostridium botulinum C1 and D binding domain subunit (Hc) vaccines against C and D neurotoxins. Vaccine 25:4273-4282.
    • (2007) Vaccine , vol.25 , pp. 4273-4282
    • Webb, R.P.1    Smith, T.J.2    Wright, P.M.3    Montgomery, V.A.4    Meagher, M.M.5    Smith, L.A.6
  • 54
    • 0026601357 scopus 로고
    • The complete amino acid sequence of the Clostridium botulinum type E neurotoxin derived by sequence analysis of the encoding gene
    • Whelan, S. M., M. J. Elmore, N. J. Bodsworth, T. Atkinson, and N. P. Minton. 1992. The complete amino acid sequence of the Clostridium botulinum type E neurotoxin derived by sequence analysis of the encoding gene. Eur. J. Biochem. 204:657-667.
    • (1992) Eur. J. Biochem. , vol.204 , pp. 657-667
    • Whelan, S.M.1    Elmore, M.J.2    Bodsworth, N.J.3    Atkinson, T.4    Minton, N.P.5
  • 55
    • 0026721240 scopus 로고
    • Molecular cloning of the Clostridium botulinum structural gene gene encoding the type B neurotoxin and determination of its entire nucleotide sequence
    • Whelan, S. M., M. J. Elmore, N. J. Bodsworth, J. K. Brehm, T. Atkinson, and P. Minton. 1992. Molecular cloning of the Clostridium botulinum structural gene gene encoding the type B neurotoxin and determination of its entire nucleotide sequence. Appl. Environ. Microbiol. 58:2345-2354.
    • (1992) Appl. Environ. Microbiol. , vol.58 , pp. 2345-2354
    • Whelan, S.M.1    Elmore, M.J.2    Bodsworth, N.J.3    Brehm, J.K.4    Atkinson, T.5    Minton, P.6
  • 56
    • 0038475597 scopus 로고    scopus 로고
    • Expression of Hc subunits from Clostridium botulinum types C and D and their evaluation as candidate vaccine antigens in mice
    • Woodward, L. A., H. Arimitsu, R. Hirst, and K. Oguma. 2003. Expression of Hc subunits from Clostridium botulinum types C and D and their evaluation as candidate vaccine antigens in mice. Infect. Immun. 71:2941-2944.
    • (2003) Infect. Immun. , vol.71 , pp. 2941-2944
    • Woodward, L.A.1    Arimitsu, H.2    Hirst, R.3    Oguma, K.4
  • 57
    • 64449088954 scopus 로고    scopus 로고
    • The recombinant Hc subunit of Clostridium botulinum neurotoxin serotype A is an effective botulism vaccine candidate
    • Yu, Y. Z., N. Li, H. Q. Zhu, R. L. Wang, Y. Du, S. Wang, W. Y. Yu, and Z. W. Sun. 2009. The recombinant Hc subunit of Clostridium botulinum neurotoxin serotype A is an effective botulism vaccine candidate. Vaccine 27:2816-2822.
    • (2009) Vaccine , vol.27 , pp. 2816-2822
    • Yu, Y.Z.1    Li, N.2    Zhu, H.Q.3    Wang, R.L.4    Du, Y.5    Wang, S.6    Yu, W.Y.7    Sun, Z.W.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.