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Volumn 18, Issue 12, 2011, Pages 2168-2177

Functional pentameric formation via coexpression of the Escherichia coli heat-labile enterotoxin B subunit and its fusion protein subunit with a neutralizing epitope of ApxIIA exotoxin improves the mucosal immunogenicity and protection against challenge by Actinobacillus pleuropneumoniae

Author keywords

[No Author keywords available]

Indexed keywords

APXIIA NEUTRALIZING EPITOPE EXOTOXIN ESCHERICHIA COLI HEAT LABILE ENTEROTOXIN B FUSION PROTEIN; EPITOPE; ESCHERICHIA COLI ENTEROTOXIN; ESCHERICHIA COLI HEAT LABILE ENTEROTOXIN B; GANGLIOSIDE GM1; UNCLASSIFIED DRUG;

EID: 83455210430     PISSN: 15566811     EISSN: 1556679X     Source Type: Journal    
DOI: 10.1128/CVI.05230-11     Document Type: Article
Times cited : (14)

References (66)
  • 1
    • 0036665063 scopus 로고    scopus 로고
    • Influence of the angiotensin-converting enzyme gene insertion/deletion polymorphism on lipoprotein/lipid response to gemfibrozil
    • DOI 10.1034/j.1399-0004.2002.620106.x
    • Bossé, Y., et al. 2002. Influence of the angiotensin-converting enzyme gene insertion/deletion polymorphism on lipoprotein/lipid response to gemfibrozil. Clin. Genet. 62:45-52. (Pubitemid 36372696)
    • (2002) Clinical Genetics , vol.62 , Issue.1 , pp. 45-52
    • Bosse, Y.1    Vohl, M.-C.2    Dumont, M.3    Brochu, M.4    Bergeron, J.5    Despres, J.-P.6    Prud'homme, D.7
  • 2
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of protein using the principle of protein-dye binding
    • Bradford, M. M. 1976. A rapid and sensitive method for the quantification of microgram quantities of protein using the principle of protein-dye binding. Anal. Biochem. 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 3
    • 79952183287 scopus 로고    scopus 로고
    • Evaluation of the immunogenicity of a transgenic tobacco plant expressing the recombinant fusion protein of GP5 of porcine reproductive and respiratory syndrome virus and B subunit of Escherichia coli heat-labile enterotoxin in pigs
    • Chia, M. Y., et al. 2011. Evaluation of the immunogenicity of a transgenic tobacco plant expressing the recombinant fusion protein of GP5 of porcine reproductive and respiratory syndrome virus and B subunit of Escherichia coli heat-labile enterotoxin in pigs. Vet. Immunol. Immunopathol. 140:215-225.
    • (2011) Vet. Immunol. Immunopathol. , vol.140 , pp. 215-225
    • Chia, M.Y.1
  • 4
    • 0025305320 scopus 로고
    • Construction of a nontoxic fusion peptide for immunization against Escherichia coli strains that produce heat-labile and heat-stable enterotoxins
    • Clements, J. D. 1990. Construction of a nontoxic fusion peptide for immunization against Escherichia coli strains that produce heat-labile and heatstable enterotoxins. Infect. Immun. 58:1159-1166. (Pubitemid 20151772)
    • (1990) Infection and Immunity , vol.58 , Issue.5 , pp. 1159-1166
    • Clements, J.D.1
  • 5
    • 0031842147 scopus 로고    scopus 로고
    • The role of ADP-ribosylation and G(M1)-binding activity in the mucosal immunogenicity and adjuvanticity of the Escherichia coli heat-labile enterotoxin and Vibrio cholerae cholera toxin
    • DOI 10.1046/j.1440-1711.1998.00745.x
    • de Haan, L., W. Verweij, E. Agsteribbe, and J. Wilschut. 1998. The role of ADT-ribosylation and GM1-binding activity in the mucosal immunogenicity and adjuvanticity of the Escherichia coli heat-labile enterotoxin and Vibrio cholerae cholera toxin. Immunol. Cell Biol. 76:270-279. (Pubitemid 28281155)
    • (1998) Immunology and Cell Biology , vol.76 , Issue.3 , pp. 270-279
    • De Haan, L.1    Verweij, W.2    Agsteribbe, E.3    Wilschut, J.4
  • 6
    • 0027392307 scopus 로고
    • Comparative effectiveness of the cholera toxin B subunit and alkaline phosphatase as carriers for oral vaccines
    • Dertzbaugh, M. T., and C. O. Elson. 1993. Comparative effectiveness of the cholera toxin B subunit and alkaline phosphatase as carriers for oral vaccines. Infect. Immun. 61:48-55. (Pubitemid 23015398)
    • (1993) Infection and Immunity , vol.61 , Issue.1 , pp. 48-55
    • Dertzbaugh, M.T.1    Elson, C.O.2
  • 7
    • 0028985871 scopus 로고
    • Dissociation of Escherichia coli heat-labile enterotoxin adjuvanticity from ADP-ribosyltransferase activity
    • Dickinson, B. L., and J. D. Clements. 1995. Dissociation of Escherichia coli heat-labile enterotoxin adjuvanticity from ADP-ribosyltransferase activity. Infect. Immun. 63:1617-1623.
    • (1995) Infect. Immun. , vol.63 , pp. 1617-1623
    • Dickinson, B.L.1    Clements, J.D.2
  • 8
    • 0034575138 scopus 로고    scopus 로고
    • Actinobacillus pleuropneumoniae surface polysaccharides: Their role in diagnosis and immunogenicity
    • Dubreuil, J. D., M. Jacques, K. R. Mittal, and M. Gottschalk. 2000. Actinobacillus pleuropneumoniae surface polysaccharides: their role in diagnosis and immunogenicity. Anim. Health Res. Rev. 1:73-93.
    • (2000) Anim. Health Res. Rev. , vol.1 , pp. 73-93
    • Dubreuil, J.D.1    Jacques, M.2    Mittal, K.R.3    Gottschalk, M.4
  • 9
    • 0026740089 scopus 로고
    • Assessment of the anti-viral effect of a short-term oral treatment of mice with live Saccharomyces cerevisiae cells
    • Fattal-German, M., and B. Bizzini. 1992. Assessment of the anti-viral effect of a short-term oral treatment of mice with live Saccharomyces cerevisiae cells. Dev. Biol. Stand. 77:115-120.
    • (1992) Dev. Biol. Stand. , vol.77 , pp. 115-120
    • Fattal-German, M.1    Bizzini, B.2
  • 10
    • 0029897005 scopus 로고    scopus 로고
    • Protein engineering studies of A-chain loop 47-56 of Escherichia coli heat-labile enterotoxin point to a prominent role of this loop for cytotoxicity
    • Feil, I. K., et al. 1996. Protein engineering studies of A-chain loop 47-56 of Escherichia coli heat-labile enterotoxin point to a prominent role of this loop for cytotoxicity. Mol. Microbiol. 20:823-832.
    • (1996) Mol. Microbiol. , vol.20 , pp. 823-832
    • Feil, I.K.1
  • 11
    • 23644433479 scopus 로고    scopus 로고
    • Vaccine and adjuvant activity of recombinant subunit B of E. coli enterotoxin produced in yeast
    • DOI 10.1016/j.vaccine.2005.03.050, PII S0264410X05004895
    • Fingerut, E., B. Gutter, R. Meir, D. Eliahoo, and J. Pitcovski. 2005. Vaccine and adjuvant activity of recombinant subunit B of E. coli enterotoxin produced in yeast. Vaccine 23:4685-4696. (Pubitemid 41132818)
    • (2005) Vaccine , vol.23 , Issue.38 , pp. 4685-4696
    • Fingerut, E.1    Gutter, B.2    Meir, R.3    Eliahoo, D.4    Pitcovski, J.5
  • 12
    • 0029124931 scopus 로고
    • Development of an efficient PCR method for toxin typing of Actinobacillus pleuropneumoniae strains
    • Frey, J., M. Beck, J. F. van den Bosch, R. P. Segers, and J. Nicolet. 1995. Development of an efficient PCR method for toxin typing of Actinobacillus pleuropneumoniae strains. Mol. Cell. Probes 9:277-282.
    • (1995) Mol. Cell. Probes , vol.9 , pp. 277-282
    • Frey, J.1    Beck, M.2    Van Den Bosch, J.F.3    Segers, R.P.4    Nicolet, J.5
  • 13
    • 0034659985 scopus 로고    scopus 로고
    • A genetically-defined riboflavin auxotroph of Actinobacillus pleuropneumoniae as a live attenuated vaccine
    • PII S0264410X00000761
    • Fuller, T. E., B. J. Thacker, C. O. Duran, and M. H. Mulks. 2000. A genetically-defined riboflavin auxotroph of Actinobacillus pleuropneumoniae as a live attenuated vaccine. Vaccine 18:2867-2877. (Pubitemid 30254474)
    • (2000) Vaccine , vol.18 , Issue.25 , pp. 2867-2877
    • Fuller, T.E.1    Thacker, B.J.2    Duran, C.O.3    Mulks, M.H.4
  • 14
    • 0024266139 scopus 로고
    • New yeast-Escherichia coli shuttle vectors constructed with in vitro mutagenized yeast genes lacking six-base pair restriction sites
    • DOI 10.1016/0378-1119(88)90185-0
    • Gietz, R. D., and A. Sugino. 1988. New yeast-Escherichia coli shuttle vectors constructed with in vitro mutagenized yeast genes lacking six-base pair restriction sites. Gene 30:527-534. (Pubitemid 19060666)
    • (1988) Gene , vol.74 , Issue.2 , pp. 527-534
    • Gietz, R.D.1    Sugino, A.2
  • 15
    • 0031457849 scopus 로고    scopus 로고
    • Actinobacillus pleuropneumoniae infections in pigs: The role of virulence factors in pathogenesis and protection
    • DOI 10.1016/S0378-1135(97)00162-4, PII S0378113597001624
    • Haesebrouck, F., K. Chiers, I. Van Overbeke, and R. Ducatelle. 1997. Actinobacillus pleuropneumoniae infections in pigs: the role of virulence factors in pathogenesis and protection. Vet. Microbiol. 58:239-249. (Pubitemid 28026787)
    • (1997) Veterinary Microbiology , vol.58 , Issue.2-4 , pp. 239-249
    • Haesebrouck, F.1    Chiers, K.2    Van Overbeke, I.3    Ducatelle, R.4
  • 17
    • 0001232852 scopus 로고
    • An introduction to polyacrylamide gel electrophoresis
    • B. D. Hames and D. Rickwood (ed.), IRL Press, Oxford, United Kingdom
    • Hames, B. D. 1981. An introduction to polyacrylamide gel electrophoresis, p. 26-42. In B. D. Hames and D. Rickwood (ed.), Gel electrophoresis of proteins, a practical approach. IRL Press, Oxford, United Kingdom.
    • (1981) Gel Electrophoresis of Proteins, A Practical Approach , pp. 26-42
    • Hames, B.D.1
  • 18
    • 0029055060 scopus 로고
    • Oral immunization with a recombinant bacterial antigen produced in transgenic plants
    • Haq, T. A., H. S. Mason, J. D. Clements, and C. J. Arntzen. 1995. Oral immunization with a recombinant bacterial antigen produced in transgenic plants. Science 268:714-716.
    • (1995) Science , vol.268 , pp. 714-716
    • Haq, T.A.1    Mason, H.S.2    Clements, J.D.3    Arntzen, C.J.4
  • 20
    • 0020529962 scopus 로고
    • Transformation of intact yeast cells treated with alkali cations
    • Ito, H., Y. Fukuda, K. Murata, and A. Kimura. 1983. Transformation of intact yeast cells treated with alkali cations. J. Bacteriol. 153:163-168. (Pubitemid 13119852)
    • (1983) Journal of Bacteriology , vol.153 , Issue.1 , pp. 163-168
    • Ito, H.1    Fukuda, Y.2    Murata, K.3    Kimura, A.4
  • 21
    • 0027400811 scopus 로고
    • Escherichia coli heat-labile toxin subunit B fusions with Streptococcus sobrinus antigens expressed by Salmonella typhimurium oral vaccine strains: Importance of the linker for antigenicity and biological activities of the hybrid proteins
    • Jagusztyn-Krynicka, E. K., J. E. Clark-Curtiss, and R. Curtiss. 1993. Escherichia coli heat-labile toxin subunit B fusions with Streptococcus sobrinus antigens expressed by Salmonella typhimurium oral vaccine strains: importance of the linker for antigenicity and biological activities of the hybrid proteins. Infect. Immun. 61:1004-1015. (Pubitemid 23059661)
    • (1993) Infection and Immunity , vol.61 , Issue.3 , pp. 1004-1015
    • Jagusztyn-Krynicka, E.K.1    Clark-Curtiss, J.E.2    Curtiss III, R.3
  • 22
    • 4344716080 scopus 로고    scopus 로고
    • Enhanced expression of B-subunit of Escherichia coli heat-labile enterotoxin in tobacco by optimization of coding sequence
    • Kang, T. J., et al. 2004. Enhanced expression of B-subunit of Escherichia coli heat-labile enterotoxin in tobacco by optimization of coding sequence. Appl. Biochem. Biotechnol. 117:175-187.
    • (2004) Appl. Biochem. Biotechnol. , vol.117 , pp. 175-187
    • Kang, T.J.1
  • 23
    • 32644478787 scopus 로고    scopus 로고
    • Expression of synthetic neutralizing epitope of porcine epidemic diarrhea virus fused with synthetic B subunit of Escherichia coli heat-labile enterotoxin in tobacco plants
    • Kang, T. J., S. C. Han, M. S. Yang, and Y. S. Jang. 2006. Expression of synthetic neutralizing epitope of porcine epidemic diarrhea virus fused with synthetic B subunit of Escherichia coli heat-labile enterotoxin in tobacco plants. Protein Expr. Purif. 46:16-22.
    • (2006) Protein Expr. Purif. , vol.46 , pp. 16-22
    • Kang, T.J.1    Han, S.C.2    Yang, M.S.3    Jang, Y.S.4
  • 25
    • 0037391352 scopus 로고    scopus 로고
    • Expression of heteropolymeric ferritin improves iron storage in Saccharomyces cerevisiae
    • Kim, H. J., et al. 2003. Expression of heteropolymeric ferritin improves iron storage in Saccharomyces cerevisiae. Appl. Environ. Microbiol. 69:1999-2005.
    • (2003) Appl. Environ. Microbiol. , vol.69 , pp. 1999-2005
    • Kim, H.J.1
  • 26
    • 77955198011 scopus 로고    scopus 로고
    • Surface-displayed expression of a neutralizing epitope of ApxIIA exotoxin in Saccharomyces cerevisiae and oral administration of it for protective immune responses against challenge by Actinobacillus pleuropneumoniae
    • Kim, J. M., et al. 2010. Surface-displayed expression of a neutralizing epitope of ApxIIA exotoxin in Saccharomyces cerevisiae and oral administration of it for protective immune responses against challenge by Actinobacillus pleuropneumoniae. Biosci. Biotechnol. Biochem. 74:1362-1367.
    • (2010) Biosci. Biotechnol. Biochem. , vol.74 , pp. 1362-1367
    • Kim, J.M.1
  • 27
    • 78650662147 scopus 로고    scopus 로고
    • The M cell-targeting ligand promotes antigen delivery and induces antigen-specific immune responses in mucosal vaccination
    • Kim, S. H., K. W. Seo, J. Kim, K. Y. Lee, and Y. S. Jang. 2010. The M cell-targeting ligand promotes antigen delivery and induces antigen-specific immune responses in mucosal vaccination. J. Immunol. 185:5787-5795.
    • (2010) J. Immunol. , vol.185 , pp. 5787-5795
    • Kim, S.H.1    Seo, K.W.2    Kim, J.3    Lee, K.Y.4    Jang, Y.S.5
  • 28
    • 33751419198 scopus 로고    scopus 로고
    • Synthesis and assembly of Escherichia coli heat-labile enterotoxin B subunit in transgenic lettuce (Lactuca sativa)
    • Kim, T. G., et al. 2007. Synthesis and assembly of Escherichia coli heat-labile enterotoxin B subunit in transgenic lettuce (Lactuca sativa). Protein Expr. Purif. 51:22-27.
    • (2007) Protein Expr. Purif. , vol.51 , pp. 22-27
    • Kim, T.G.1
  • 29
    • 77957753828 scopus 로고    scopus 로고
    • Cholera toxin B subunit-domain III of dengue virus envelope glycoprotein E fusion protein production in transgenic plants
    • Kim, T. G., M. Y. Kim, and M. S. Yang. 2010. Cholera toxin B subunit-domain III of dengue virus envelope glycoprotein E fusion protein production in transgenic plants. Protein Expr. Purif. 74:236-241.
    • (2010) Protein Expr. Purif. , vol.74 , pp. 236-241
    • Kim, T.G.1    Kim, M.Y.2    Yang, M.S.3
  • 30
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 31
    • 0033198608 scopus 로고    scopus 로고
    • The interaction between RTX toxins and target cells
    • DOI 10.1016/S0966-842X(99)01530-9, PII S0966842X99015309
    • Lally, E. T., R. B. Hill, I. R. Kieba, and J. Korostoff. 1999. The interaction between RTX toxins and target cells. Trends Microbiol. 7:356-361. (Pubitemid 29421660)
    • (1999) Trends in Microbiology , vol.7 , Issue.9 , pp. 356-361
    • Lally, E.T.1    Hill, R.B.2    Kieba, I.R.3    Korostoff, J.4
  • 32
    • 0347993175 scopus 로고    scopus 로고
    • Induction of human IgM and IgG anti-GM1 antibodies in transgenic mice in response to lipopolysaccharides from Campylobacter jejuni
    • DOI 10.1016/j.jneuroim.2003.10.045
    • Lee, G., et al. 2004. Induction of human IgM and IgG anti-GM1 antibodies in transgenic mice in response to lipopolysaccharides from Campylobacter jejuni. J. Neuroimmunol. 146:63-75. (Pubitemid 38032957)
    • (2004) Journal of Neuroimmunology , vol.146 , Issue.1-2 , pp. 63-75
    • Lee, G.1    Jeong, Y.2    Wirguin, I.3    Hays, A.P.4    Willison, H.J.5    Latov, N.6
  • 33
    • 33750942121 scopus 로고    scopus 로고
    • Induction of protective immune responses against the challenge of Actinobacillus pleuropneumoniae by the oral administration of transgenic tobacco plant expressing ApxIIA toxin from the bacteria
    • Lee, K. Y., et al. 2006. Induction of protective immune responses against the challenge of Actinobacillus pleuropneumoniae by the oral administration of transgenic tobacco plant expressing ApxIIA toxin from the bacteria. FEMS Immunol. Med. Microbiol. 48:381-389.
    • (2006) FEMS Immunol. Med. Microbiol. , vol.48 , pp. 381-389
    • Lee, K.Y.1
  • 34
    • 0024222629 scopus 로고
    • Protection of mice against the lethal effect of an intraperitoneal infection with Haemophilus (Actinobacillus) pleuropneumoniae after vaccination with capsular proteins
    • Lenser, D. K., T. L. McDonald, and N. G. Miller. 1988. Protection of mice against the lethal effect of an intraperitoneal infection with Haemophilus (Actinobacillus) pleuropneumoniae after vaccination with capsular proteins. Vet. Microbiol. 18:335-348.
    • (1988) Vet. Microbiol. , vol.18 , pp. 335-348
    • Lenser, D.K.1    McDonald, T.L.2    Miller, N.G.3
  • 35
    • 67649429825 scopus 로고    scopus 로고
    • Expression of functional pentameric heat-labile enterotoxin B subunit of Escherichia coli in Saccharomyces cerevisiae
    • Lim, J. G., et al. 2009. Expression of functional pentameric heat-labile enterotoxin B subunit of Escherichia coli in Saccharomyces cerevisiae. J. Microbiol. Biotechnol. 19:502-510.
    • (2009) J. Microbiol. Biotechnol. , vol.19 , pp. 502-510
    • Lim, J.G.1
  • 36
    • 0035690062 scopus 로고    scopus 로고
    • Enhanced and targeted expression of fungal phytase in Saccharomyces cerevisiae
    • Lim, Y. Y., et al. 2001. Enhanced and targeted expression of fungal phytase in Saccharomyces cerevisiae. J. Microbiol. Biotechnol. 11:915-921.
    • (2001) J. Microbiol. Biotechnol. , vol.11 , pp. 915-921
    • Lim, Y.Y.1
  • 37
    • 0026699224 scopus 로고
    • The adjuvant effect of Vibrio cholerae and Escherichia coli heat-labile enterotoxins is linked to their ADPribosyltransferase activity
    • Lycke, N., T. Tsuji, and J. Holmgren. 1992. The adjuvant effect of Vibrio cholerae and Escherichia coli heat-labile enterotoxins is linked to their ADPribosyltransferase activity. Eur. J. Immunol. 22:2277-2281.
    • (1992) Eur. J. Immunol. , vol.22 , pp. 2277-2281
    • Lycke, N.1    Tsuji, T.2    Holmgren, J.3
  • 38
    • 0029911276 scopus 로고    scopus 로고
    • Channel-forming activity and channel size of the RTX toxins ApxI, ApxII, and ApxIII of Actinobacillus pleuropneumoniae
    • Maier, E., N. Reinhard, R. Benz, and J. Frey. 1996. Channel-forming activity and channel size of the RTX toxins ApxI, ApxII, and ApxIII of Actinobacillus pleuropneumoniae. Infect. Immun. 64:4415-4423. (Pubitemid 26357038)
    • (1996) Infection and Immunity , vol.64 , Issue.11 , pp. 4415-4423
    • Maier, E.1    Reinhard, N.2    Benz, R.3    Frey, J.4
  • 40
    • 0033612782 scopus 로고    scopus 로고
    • Serotype and apx genotype profiles of Actinobacillus pleuropneumoniae field isolates in Korea
    • Min, K., and C. Chae. 1999. Serotype and apx genotype profiles of Actinobacillus pleuropneumoniae field isolates in Korea. Vet. Rec. 145:251-254. (Pubitemid 129544103)
    • (1999) Veterinary Record , vol.145 , Issue.9 , pp. 251-254
    • Min, K.1    Chae, C.2
  • 41
    • 30344486939 scopus 로고    scopus 로고
    • Expression of fungal phytase on the cell surface of Saccharomyces cerevisiae
    • Mo, A. Y., Y. S. Kim, S. M. Park, M. S. Yang, and D. H. Kim. 2005. Expression of fungal phytase on the cell surface of Saccharomyces cerevisiae. Biotechnol. Bioprocess Eng. 10:576-581.
    • (2005) Biotechnol. Bioprocess Eng. , vol.10 , pp. 576-581
    • Mo, A.Y.1    Kim, Y.S.2    Park, S.M.3    Yang, M.S.4    Kim, D.H.5
  • 42
    • 0034725935 scopus 로고    scopus 로고
    • Expression of glucose oxidase by using recombinant yeast
    • Park, E. H., et al. 2000. Expression of glucose oxidase by using recombinant yeast. J. Biotechnol. 81:35-44.
    • (2000) J. Biotechnol. , vol.81 , pp. 35-44
    • Park, E.H.1
  • 43
    • 24344500774 scopus 로고    scopus 로고
    • Expression of the Apx toxins of Actinobacillus pleuropneumoniae in Saccharomyces cerevisiae and its induction of immune response in mice
    • Park, S. M., et al. 2005. Expression of the Apx toxins of Actinobacillus pleuropneumoniae in Saccharomyces cerevisiae and its induction of immune response in mice. Biotechnol. Bioprocess Eng. 10:362-366.
    • (2005) Biotechnol. Bioprocess Eng. , vol.10 , pp. 362-366
    • Park, S.M.1
  • 44
    • 21644461297 scopus 로고    scopus 로고
    • Expression of a functional human tumor necrosis factor (hTNF)-α in yeast Saccharomyces cerevisiae
    • Park, S. M., et al. 2004. Expression of a functional human tumor necrosis factor (hTNF)-α in yeast Saccharomyces cerevisiae. Biotech. Bioprocess Eng. 9:292-296.
    • (2004) Biotech. Bioprocess Eng. , vol.9 , pp. 292-296
    • Park, S.M.1
  • 45
    • 0025234313 scopus 로고
    • Concentration of proteins and removal of solutes
    • DOI 10.1016/0076-6879(90)82009-Q
    • Pohl, T. 1990. Concentration of proteins and removal of solutes. Methods Enzymol. 182:68-83. (Pubitemid 20154380)
    • (1990) Methods in Enzymology , vol.182 , pp. 68-83
    • Pohl, T.1
  • 46
    • 0033057905 scopus 로고    scopus 로고
    • Vaccination and protection of pigs against pleuropneumonia with a vaccine strain of Actinobacillus pleuropneumoniae produced by site-specific mutagenesis of the ApxII operon
    • Prideaux, C. T., C. Lenghaus, J. Krywult, and A. L. Hodgson. 1999. Vaccination and protection of pigs against pleuropneumonia with a vaccine strain of Actinobacillus pleuropneumoniae produced by site-specific mutagenesis of the ApxII operon. Infect. Immun. 67:1962-1966. (Pubitemid 29144422)
    • (1999) Infection and Immunity , vol.67 , Issue.4 , pp. 1962-1966
    • Prideaux, C.T.1    Lenghaus, C.2    Krywult, J.3    Hodgson, A.L.M.4
  • 47
    • 0029040875 scopus 로고
    • Molecular investigation of the role of ApxI and ApxII in the virulence of Actinobacillus pleuropneumoniae serotype 5
    • Reimer, D., J. Frey, R. Jansen, H. P. Veit, and T. J. Inzana. 1995. Molecular investigation of the role of ApxI and ApxII in the virulence of Actinobacillus pleuropneumoniae serotype 5. Microb. Pathog. 18:197-209.
    • (1995) Microb. Pathog. , vol.18 , pp. 197-209
    • Reimer, D.1    Frey, J.2    Jansen, R.3    Veit, H.P.4    Inzana, T.J.5
  • 50
    • 43049105454 scopus 로고    scopus 로고
    • Expression of a bioactive fusion protein of Escherichia coli heat-labile toxin B subunit to a synapsin peptide
    • Scerbo, M. J., M. J. Bibolini, J. L. Barra, G. A. Roth, and C. G. Monferran. 2008. Expression of a bioactive fusion protein of Escherichia coli heat-labile toxin B subunit to a synapsin peptide. Protein Expr. Purif. 59:320-326.
    • (2008) Protein Expr. Purif. , vol.59 , pp. 320-326
    • Scerbo, M.J.1    Bibolini, M.J.2    Barra, J.L.3    Roth, G.A.4    Monferran, C.G.5
  • 52
    • 0025930765 scopus 로고
    • Targeting and assembly of an oligomeric bacterial enterotoxoid in the endoplasmic reticulum of Saccharomyces cerevisiae
    • Schonberger, O., T. R. Hirst, and O. Pines. 1991. Targeting and assembly of an oligomeric bacterial enterotoxoid in the endoplasmic reticulum of Saccharomyces cerevisiae. Mol. Microbiol. 5:2663-2667.
    • (1991) Mol. Microbiol. , vol.5 , pp. 2663-2667
    • Schonberger, O.1    Hirst, T.R.2    Pines, O.3
  • 54
    • 0036839670 scopus 로고    scopus 로고
    • The N-terminal domain of RTX toxin ApxI of Actinobacillus pleuropneumoniae elicits protective immunity in mice
    • DOI 10.1128/IAI.70.11.6464-6467.2002
    • Seah, J. N., J. Frey, and J. Kwang. 2002. The N-terminal domain of RTX toxin ApxI of Actinobacillus pleuropneumoniae elicits protective immunity in mice. Infect. Immun. 70:6464-6467. (Pubitemid 35192742)
    • (2002) Infection and Immunity , vol.70 , Issue.11 , pp. 6464-6467
    • Seah, J.N.1    Frey, J.2    Kwang, J.3
  • 55
    • 12844252535 scopus 로고    scopus 로고
    • Induction of antigen-specific immune responses by oral vaccination with Saccharomyces cerevisiae expressing Actinobacillus pleuropneumoniae ApxIIA
    • DOI 10.1016/j.femsim.2004.07.004, PII S0928824404001476
    • Shin, S. J., et al. 2005. Induction of antigen-specific immune responses by oral vaccination with Saccharomyces cerevisiae expressing Actinobacillus pleuropneumoniae ApxIIA. FEMS Immunol. Med. Microbiol. 43:155-164. (Pubitemid 40170284)
    • (2005) FEMS Immunology and Medical Microbiology , vol.43 , Issue.2 , pp. 155-164
    • Shin, S.J.1    Bae, J.L.2    Cho, Y.-W.3    Lee, D.Y.4    Kim, D.-H.5    Yang, M.-S.6    Jang, Y.-S.7    Yoo, H.S.8
  • 56
    • 37349038473 scopus 로고    scopus 로고
    • Enhancement of protective immune responses by oral vaccination with Saccharomyces cerevisiae expressing recombinant Actinobacillus pleuropneumoniae ApxIA or ApxIIA in mice
    • Shin, S. J., et al. 2007. Enhancement of protective immune responses by oral vaccination with Saccharomyces cerevisiae expressing recombinant Actinobacillus pleuropneumoniae ApxIA or ApxIIA in mice. J. Vet. Sci. 8:383-392.
    • (2007) J. Vet. Sci. , vol.8 , pp. 383-392
    • Shin, S.J.1
  • 57
    • 0035289758 scopus 로고    scopus 로고
    • Enhanced iron uptake of Saccharomyces cerevisiae by heterologous expression of a tadpole ferritin gene
    • Shin, Y. M., et al. 2001. Enhanced iron uptake of Saccharomyces cerevisiae by heterologous expression of a tadpole ferritin gene. Appl. Environ. Microbiol. 67:1280-1283.
    • (2001) Appl. Environ. Microbiol. , vol.67 , pp. 1280-1283
    • Shin, Y.M.1
  • 59
    • 0026598947 scopus 로고
    • Lactose binding to heat-labile enterotoxin revealed by X-ray crystallography
    • Sixma, T. K., et al. 1992. Lactose binding to heat-labile enterotoxin revealed by X-ray crystallography. Nature 355:561-564.
    • (1992) Nature , vol.355 , pp. 561-564
    • Sixma, T.K.1
  • 60
    • 0029493562 scopus 로고
    • The mucosal adjuvant activities of ADP-ribosylating bacterial enterotoxins
    • Snider, D. P. 1995. The mucosal adjuvant activities of ADP-ribosylating bacterial enterotoxins. Crit. Rev. Immunol. 15:317-348. (Pubitemid 26259134)
    • (1995) Critical Reviews in Immunology , vol.15 , Issue.3-4 , pp. 317-348
    • Snider, D.P.1
  • 61
    • 0026458260 scopus 로고
    • Structure and function of cholera toxin and the related Escherichia coli heat-labile enterotoxin
    • Spangler, B. D. 1992. Structure and function of cholera toxin and the related Escherichia coli heat-labile enterotoxin. Microbiol. Rev. 56:622-647.
    • (1992) Microbiol. Rev. , vol.56 , pp. 622-647
    • Spangler, B.D.1
  • 63
    • 12444328812 scopus 로고    scopus 로고
    • Principles of mucosal immunity and development of mucosal vaccines using cholera toxin B subunit and its related adjuvants
    • Tochikubo, K., and Y. Yasuda. 2000. Principles of mucosal immunity and development of mucosal vaccines using cholera toxin B subunit and its related adjuvants. Rec. Res. Dev. Microbiol. 4:387-405.
    • (2000) Rec. Res. Dev. Microbiol. , vol.4 , pp. 387-405
    • Tochikubo, K.1    Yasuda, Y.2
  • 64
    • 0028826127 scopus 로고
    • Monomer of the B subunit of heat-labile enterotoxin from enterotoxigenic Escherichia coli has little ability to bind to GM1 ganglioside compared to its coligenoid
    • Tsuji, T., K. Watanabe, and A. Miyama. 1995. Monomer of the B subunit of heat-labile enterotoxin from enterotoxigenic Escherichia coli has little ability to bind to GM1 ganglioside compared to its coligenoid. Microbiol. Immunol. 39:817-819.
    • (1995) Microbiol. Immunol. , vol.39 , pp. 817-819
    • Tsuji, T.1    Watanabe, K.2    Miyama, A.3
  • 65
    • 0026751858 scopus 로고
    • Salvage carboplatin therapy for advanced ovarian cancer after first-line treatment with cisplatin
    • Williams, L. L., M. Fudge, L. S. Burnett, and H. W. Jones. 1992. Salvage carboplatin therapy for advanced ovarian cancer after first-line treatment with cisplatin. Am. J. Clin. Oncol. 15:331-336.
    • (1992) Am. J. Clin. Oncol. , vol.15 , pp. 331-336
    • Williams, L.L.1    Fudge, M.2    Burnett, L.S.3    Jones, H.W.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.