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Volumn 50, Issue 1, 2003, Pages 12-27

Display and release of the Plasmodium falciparum circumsporozoite protein using the autotransporter MisL of Salmonella enterica

Author keywords

Autodisplay; Circumsporozoite protein; Live vector vaccines; MisL; Plasmodium falciparum; Salmonella enterica

Indexed keywords

CARRIER PROTEIN; HYBRID PROTEIN;

EID: 0038121598     PISSN: 0147619X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0147-619X(03)00047-7     Document Type: Article
Times cited : (34)

References (39)
  • 1
    • 0034064649 scopus 로고    scopus 로고
    • The sig A gene which is borne on the she pathogenicity island of Shigella flexneri 2a encodes an exported cytopathic protease involved in intestinal fluid accumulation
    • Al Hasani K., Henderson I.R., Sakellaris H., Rajakumar K., Grant T., Nataro J.P., Robins-Browne R., Adler B. The sig A gene which is borne on the she pathogenicity island of Shigella flexneri 2a encodes an exported cytopathic protease involved in intestinal fluid accumulation. Infect. Immun. 68:2000;2457-2463.
    • (2000) Infect. Immun. , vol.68 , pp. 2457-2463
    • Al Hasani, K.1    Henderson, I.R.2    Sakellaris, H.3    Rajakumar, K.4    Grant, T.5    Nataro, J.P.6    Robins-Browne, R.7    Adler, B.8
  • 2
    • 0024517699 scopus 로고
    • Cloning and expression of an adhesin (AIDA-I) involved in diffuse adherence of enteropathogenic Escherichia coli
    • Benz I., Schmidt M.A. Cloning and expression of an adhesin (AIDA-I) involved in diffuse adherence of enteropathogenic Escherichia coli. Infect. Immun. 57:1989;1506-1511.
    • (1989) Infect. Immun. , vol.57 , pp. 1506-1511
    • Benz, I.1    Schmidt, M.A.2
  • 3
    • 0032996225 scopus 로고    scopus 로고
    • Biochemistry of type IV secretion
    • Burns D.L. Biochemistry of type IV secretion. Curr. Opin. Microbiol. 2:1999;25-29.
    • (1999) Curr. Opin. Microbiol. , vol.2 , pp. 25-29
    • Burns, D.L.1
  • 4
    • 0033932231 scopus 로고    scopus 로고
    • Relationship between the Tsh autotransporter and pathogenicity of avian Escherichia coli and localization and analysis of the Tsh genetic region
    • Dozois C.M., Dho-Moulin M., Bree A., Fairbrother J.M., Desautels C., Curtiss III R. Relationship between the Tsh autotransporter and pathogenicity of avian Escherichia coli and localization and analysis of the Tsh genetic region. Infect. Immun. 68:2000;4145-4154.
    • (2000) Infect. Immun. , vol.68 , pp. 4145-4154
    • Dozois, C.M.1    Dho-Moulin, M.2    Bree, A.3    Fairbrother, J.M.4    Desautels, C.5    Curtiss R. III6
  • 5
    • 0035914443 scopus 로고    scopus 로고
    • The Haemophilus influenzae Hap autotransporter is a chymotrypsin clan serine protease and undergoes autoproteolysis via an intermolecular mechanism
    • Fink D.L., Cope L.D., Hansen E.J., Geme III J.W. The Haemophilus influenzae Hap autotransporter is a chymotrypsin clan serine protease and undergoes autoproteolysis via an intermolecular mechanism. J. Biol. Chem. 276:2001;39492-39500.
    • (2001) J. Biol. Chem. , vol.276 , pp. 39492-39500
    • Fink, D.L.1    Cope, L.D.2    Hansen, E.J.3    Geme J.W. III4
  • 6
    • 0024596351 scopus 로고
    • Comparison of Escherichia coli K-12 outer membrane protease OmpT and Salmonella typhimurium E protein
    • Grodberg J., Dunn J.J. Comparison of Escherichia coli K-12 outer membrane protease OmpT and Salmonella typhimurium E protein. J. Bacteriol. 171:1989;2903-2905.
    • (1989) J. Bacteriol. , vol.171 , pp. 2903-2905
    • Grodberg, J.1    Dunn, J.J.2
  • 7
    • 0033810425 scopus 로고    scopus 로고
    • Identification of sat, an autotransporter toxin produced by uropathogenic Escherichia coli
    • Guyer D.M., Henderson I.R., Nataro J.P., Mobley H.L. Identification of sat, an autotransporter toxin produced by uropathogenic Escherichia coli. Mol. Microbiol. 38:2000;53-66.
    • (2000) Mol. Microbiol. , vol.38 , pp. 53-66
    • Guyer, D.M.1    Henderson, I.R.2    Nataro, J.P.3    Mobley, H.L.4
  • 8
    • 0026711187 scopus 로고
    • Processing by OmpT of fusion proteins carrying the HlyA transport signal during secretion by the Escherichia coli hemolysin transport system
    • Hanke C., Hess J., Schumacher G., Goebel W. Processing by OmpT of fusion proteins carrying the HlyA transport signal during secretion by the Escherichia coli hemolysin transport system. Mol. Gen. Genet. 233:1992;42-48.
    • (1992) Mol. Gen. Genet. , vol.233 , pp. 42-48
    • Hanke, C.1    Hess, J.2    Schumacher, G.3    Goebel, W.4
  • 9
    • 0032734808 scopus 로고    scopus 로고
    • Characterization of pic, a secreted protease of Shigella flexneri and enteroaggregative Escherichia coli
    • Henderson I.R., Czeczulin J., Eslava C., Noriega F., Nataro J.P. Characterization of pic, a secreted protease of Shigella flexneri and enteroaggregative Escherichia coli. Infect. Immun. 67:1999;5587-5596.
    • (1999) Infect. Immun. , vol.67 , pp. 5587-5596
    • Henderson, I.R.1    Czeczulin, J.2    Eslava, C.3    Noriega, F.4    Nataro, J.P.5
  • 10
    • 0035111746 scopus 로고    scopus 로고
    • Virulence functions of autotransporter proteins
    • Henderson I.R., Nataro J.P. Virulence functions of autotransporter proteins. Infect. Immun. 69:2001;1231-1243.
    • (2001) Infect. Immun. , vol.69 , pp. 1231-1243
    • Henderson, I.R.1    Nataro, J.P.2
  • 11
    • 0025605708 scopus 로고
    • Analysis of the haemolysin secretion system by PhoA-HlyA fusion proteins
    • Hess J., Gentschev I., Goebel W., Jarchau T. Analysis of the haemolysin secretion system by PhoA-HlyA fusion proteins. Mol. Gen. Genet. 224:1990;201-208.
    • (1990) Mol. Gen. Genet. , vol.224 , pp. 201-208
    • Hess, J.1    Gentschev, I.2    Goebel, W.3    Jarchau, T.4
  • 12
    • 0030007941 scopus 로고    scopus 로고
    • Superior efficacy of secreted over somatic antigen display in recombinant Salmonella vaccine induced protection against listeriosis
    • Hess J., Gentschev I., Miko D., Welzel M., Ladel C., Goebel W., Kaufmann S.H. Superior efficacy of secreted over somatic antigen display in recombinant Salmonella vaccine induced protection against listeriosis. Proc. Natl. Acad. Sci. USA. 93:1996;1458-1463.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 1458-1463
    • Hess, J.1    Gentschev, I.2    Miko, D.3    Welzel, M.4    Ladel, C.5    Goebel, W.6    Kaufmann, S.H.7
  • 13
    • 0028824728 scopus 로고
    • Common structural features of IgA1 protease-like outer membrane protein autotransporters
    • Jose J., Jahnig F., Meyer T.F. Common structural features of IgA1 protease-like outer membrane protein autotransporters. Mol. Microbiol. 18:1995;378-380.
    • (1995) Mol. Microbiol. , vol.18 , pp. 378-380
    • Jose, J.1    Jahnig, F.2    Meyer, T.F.3
  • 14
    • 0025353145 scopus 로고
    • Extracellular transport of cholera toxin B subunit using Neisseria IgA protease beta-domain: Conformation-dependent outer membrane translocation
    • Klauser T., Pohlner J., Meyer T.F. Extracellular transport of cholera toxin B subunit using Neisseria IgA protease beta-domain: conformation-dependent outer membrane translocation. EMBO J. 9:1990;1991-1999.
    • (1990) EMBO J. , vol.9 , pp. 1991-1999
    • Klauser, T.1    Pohlner, J.2    Meyer, T.F.3
  • 15
    • 0027751445 scopus 로고
    • The secretion pathway of IgA protease-type proteins in Gram-negative bacteria
    • Klauser T., Pohlner J., Meyer T.F. The secretion pathway of IgA protease-type proteins in Gram-negative bacteria. Bioessays. 15:1993;799-805.
    • (1993) Bioessays , vol.15 , pp. 799-805
    • Klauser, T.1    Pohlner, J.2    Meyer, T.F.3
  • 16
    • 0000983237 scopus 로고    scopus 로고
    • In vitro folding, purification and characterization of Escherichia coli outer membrane protease ompT
    • Kramer R.A., Zandwijken D., Egmond M.R., Dekker N. In vitro folding, purification and characterization of Escherichia coli outer membrane protease ompT. Eur. J. Biochem. 267:2000;885-893.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 885-893
    • Kramer, R.A.1    Zandwijken, D.2    Egmond, M.R.3    Dekker, N.4
  • 17
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:1970;680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 18
    • 0034051291 scopus 로고    scopus 로고
    • Autodisplay: Functional display of active beta-lactamase on the surface of Escherichia coli by the AIDA-I autotransporter
    • Lattemann C.T., Maurer J., Gerland E., Meyer T.F. Autodisplay: functional display of active beta-lactamase on the surface of Escherichia coli by the AIDA-I autotransporter. J. Bacteriol. 182:2000;3726-3733.
    • (2000) J. Bacteriol. , vol.182 , pp. 3726-3733
    • Lattemann, C.T.1    Maurer, J.2    Gerland, E.3    Meyer, T.F.4
  • 20
    • 0032783142 scopus 로고    scopus 로고
    • Identification of a glycoprotein produced by enterotoxigenic Escherichia coli
    • Lindenthal C., Elsinghorst E.A. Identification of a glycoprotein produced by enterotoxigenic Escherichia coli. Infect. Immun. 67:1999;4084-4091.
    • (1999) Infect. Immun. , vol.67 , pp. 4084-4091
    • Lindenthal, C.1    Elsinghorst, E.A.2
  • 21
    • 0032705124 scopus 로고    scopus 로고
    • The plasmid F OmpP protease, a homologue of OmpT, as a potential obstacle to E. coli-based protein production
    • Matsuo E., Sampei G., Mizobuchi K., Ito K. The plasmid F OmpP protease, a homologue of OmpT, as a potential obstacle to E. coli-based protein production. FEBS Lett. 461:1999;6-8.
    • (1999) FEBS Lett. , vol.461 , pp. 6-8
    • Matsuo, E.1    Sampei, G.2    Mizobuchi, K.3    Ito, K.4
  • 22
    • 0031034089 scopus 로고    scopus 로고
    • Autodisplay: One-component system for efficient surface display and release of soluble recombinant proteins from Escherichia coli
    • Maurer J., Jose J., Meyer T.F. Autodisplay: one-component system for efficient surface display and release of soluble recombinant proteins from Escherichia coli. J. Bacteriol. 179:1997;794-804.
    • (1997) J. Bacteriol. , vol.179 , pp. 794-804
    • Maurer, J.1    Jose, J.2    Meyer, T.F.3
  • 23
    • 0026717378 scopus 로고
    • A comparative genetic study of serologically distinct Haemophilus influenzae type 1 immunoglobulin A1 proteases
    • Poulsen K., Reinholdt J., Kilian M. A comparative genetic study of serologically distinct Haemophilus influenzae type 1 immunoglobulin A1 proteases. J. Bacteriol. 174:1992;2913-2921.
    • (1992) J. Bacteriol. , vol.174 , pp. 2913-2921
    • Poulsen, K.1    Reinholdt, J.2    Kilian, M.3
  • 24
    • 0036084379 scopus 로고    scopus 로고
    • Expression of the Plasmodium falciparum immunodominant epitope (NANP)(4) on the surface of Salmonella enterica using the autotransporter MisL
    • Ruiz-Perez F., Leon-Kempis R., Santiago-Machuca A., Ortega-Pierres G., Barry E., Levine M., Gonzalez-Bonilla C. Expression of the Plasmodium falciparum immunodominant epitope (NANP)(4) on the surface of Salmonella enterica using the autotransporter MisL. Infect. Immun. 70:2002;3611-3620.
    • (2002) Infect. Immun. , vol.70 , pp. 3611-3620
    • Ruiz-Perez, F.1    Leon-Kempis, R.2    Santiago-Machuca, A.3    Ortega-Pierres, G.4    Barry, E.5    Levine, M.6    Gonzalez-Bonilla, C.7
  • 25
    • 0027434697 scopus 로고
    • Membrane traffic wardens and protein secretion in Gram-negative bacteria
    • Salmond G.P., Reeves P.J. Membrane traffic wardens and protein secretion in Gram-negative bacteria. Trends Biochem. Sci. 18:1993;7-12.
    • (1993) Trends Biochem. Sci. , vol.18 , pp. 7-12
    • Salmond, G.P.1    Reeves, P.J.2
  • 26
    • 0003903345 scopus 로고    scopus 로고
    • Molecular Cloning: A Laboratory Manual
    • Cold Spring Harbor, New York, USA: Cold Spring Harbor Laboratory Press
    • Sambrook J., Russell D.W. Molecular Cloning: A Laboratory Manual. third ed. 2001;Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York, USA.
    • (2001) third ed.
    • Sambrook, J.1    Russell, D.W.2
  • 27
    • 0032882546 scopus 로고    scopus 로고
    • The C-terminal domain of the Bordetella pertussis autotransporter BrkA forms a pore in lipid bilayer membranes
    • Shannon J.L., Fernandez R.C. The C-terminal domain of the Bordetella pertussis autotransporter BrkA forms a pore in lipid bilayer membranes. J. Bacteriol. 181:1999;5838-5842.
    • (1999) J. Bacteriol. , vol.181 , pp. 5838-5842
    • Shannon, J.L.1    Fernandez, R.C.2
  • 28
    • 0034792632 scopus 로고    scopus 로고
    • The role of the TolC family in protein transport and multidrug efflux. From stereochemical certainty to mechanistic hypothesis
    • Sharff A., Fanutti C., Shi J., Calladine C., Luisi B. The role of the TolC family in protein transport and multidrug efflux. From stereochemical certainty to mechanistic hypothesis. Eur. J. Biochem. 268:2001;5011-5026.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 5011-5026
    • Sharff, A.1    Fanutti, C.2    Shi, J.3    Calladine, C.4    Luisi, B.5
  • 30
    • 0035793148 scopus 로고    scopus 로고
    • Display of green fluorescent protein on Escherichia coli cell surface
    • Shi H., Wen S.W. Display of green fluorescent protein on Escherichia coli cell surface. Enzyme Microb. Technol. 28:2001;25-34.
    • (2001) Enzyme Microb. Technol. , vol.28 , pp. 25-34
    • Shi, H.1    Wen, S.W.2
  • 31
    • 0024563389 scopus 로고
    • Nucleotide sequence of the plasminogen activator gene of Yersinia pestis: Relationship to omp T of Escherichia coli and gene E of Salmonella typhimurium
    • Sodeinde O.A., Goguen J.D. Nucleotide sequence of the plasminogen activator gene of Yersinia pestis: relationship to omp T of Escherichia coli and gene E of Salmonella typhimurium. Infect. Immun. 57:1989;1517-1523.
    • (1989) Infect. Immun. , vol.57 , pp. 1517-1523
    • Sodeinde, O.A.1    Goguen, J.D.2
  • 32
    • 0033765760 scopus 로고    scopus 로고
    • The Haemophilus influenzae Hia adhesin is an autotransporter protein that remains uncleaved at the C terminus and fully cell associated
    • St III G.J., Cutter D. The Haemophilus influenzae Hia adhesin is an autotransporter protein that remains uncleaved at the C terminus and fully cell associated. J. Bacteriol. 182:2000;6005-6013.
    • (2000) J. Bacteriol. , vol.182 , pp. 6005-6013
    • St G.J. III1    Cutter, D.2
  • 33
    • 0033842544 scopus 로고    scopus 로고
    • Secretion of virulence determinants by the general secretory pathway in Gram-negative pathogens: An evolving story
    • Stathopoulos C., Hendrixson D.R., Thanassi D.G., Hultgren S.J., St III G.J., Curtiss III R. Secretion of virulence determinants by the general secretory pathway in Gram-negative pathogens: an evolving story. Microbes Infect. 2:2000;1061-1072.
    • (2000) Microbes Infect. , vol.2 , pp. 1061-1072
    • Stathopoulos, C.1    Hendrixson, D.R.2    Thanassi, D.G.3    Hultgren, S.J.4    St G.J. III5    Curtiss R. III6
  • 34
    • 0029621229 scopus 로고
    • Extracellular transport of VirG protein in Shigella
    • Suzuki T., Lett M.C., Sasakawa C. Extracellular transport of VirG protein in Shigella. J. Biol. Chem. 270:1995;30874-30880.
    • (1995) J. Biol. Chem. , vol.270 , pp. 30874-30880
    • Suzuki, T.1    Lett, M.C.2    Sasakawa, C.3
  • 35
    • 0033937939 scopus 로고    scopus 로고
    • Multiple pathways allow protein secretion across the bacterial outer membrane
    • Thanassi D.G., Hultgren S.J. Multiple pathways allow protein secretion across the bacterial outer membrane. Curr. Opin. Cell Biol. 12:2000;420-430.
    • (2000) Curr. Opin. Cell Biol. , vol.12 , pp. 420-430
    • Thanassi, D.G.1    Hultgren, S.J.2
  • 36
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin H., Staehelin T., Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. USA. 76:1979;4350-4354.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 37
    • 0032854025 scopus 로고    scopus 로고
    • Probing secretion and translocation of a beta-autotransporter using a reporter single-chain Fv as a cognate passenger domain
    • Veiga E., de L.V., Fernandez L.A. Probing secretion and translocation of a beta-autotransporter using a reporter single-chain Fv as a cognate passenger domain. Mol. Microbiol. 33:1999;1232-1243.
    • (1999) Mol. Microbiol. , vol.33 , pp. 1232-1243
    • Veiga, E.1    De, L.V.2    Fernandez, L.A.3
  • 38
    • 0036565670 scopus 로고    scopus 로고
    • Export of autotransported proteins proceeds through an oligomeric ring shaped by C-terminal domains
    • Veiga E., Sugawara E., Nikaido H., de L.V., Fernandez L.A. Export of autotransported proteins proceeds through an oligomeric ring shaped by C-terminal domains. EMBO J. 21:2002;2122-2131.
    • (2002) EMBO J. , vol.21 , pp. 2122-2131
    • Veiga, E.1    Sugawara, E.2    Nikaido, H.3    De, L.V.4    Fernandez, L.A.5
  • 39
    • 0035165665 scopus 로고    scopus 로고
    • Proof without prejudice revisited: Immunofluorescence histogram analysis using cumulative frequency subtraction plus ratio analysis of means
    • Watson J.V. Proof without prejudice revisited: immunofluorescence histogram analysis using cumulative frequency subtraction plus ratio analysis of means. Cytometry. 43:2001;55-68.
    • (2001) Cytometry , vol.43 , pp. 55-68
    • Watson, J.V.1


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