메뉴 건너뛰기




Volumn 15, Issue 1, 1997, Pages 29-34

Display of heterologous proteins on the surface of microorganisms: From the screening of combinatorial libraries to live recombinant vaccines

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; HYBRID PROTEIN; LIPOPROTEIN; MEMBRANE PROTEIN; OLIGOSACCHARIDE; OUTER MEMBRANE PROTEIN; POLYPEPTIDE; PULLULANASE; RECOMBINANT VACCINE;

EID: 0031012062     PISSN: 10870156     EISSN: 15461696     Source Type: Journal    
DOI: 10.1038/nbt0197-29     Document Type: Review
Times cited : (455)

References (90)
  • 1
    • 0028843867 scopus 로고
    • A generic method for expression and use of “tagged” soluble versions of cell surface receptors
    • Whitehorn, E.A., Tate, E., Yanofsky, S.D., Kochersperger, L, Davis, A., Mortensen, R.B., et al. 1995. A generic method for expression and use of “tagged” soluble versions of cell surface receptors. Bio/Technology 13:1215-19.
    • (1995) Bio/Technology , vol.13 , pp. 1215-1219
    • Whitehorn, E.A.1    Tate, E.2    Yanofsky, S.D.3    Kochersperger, L.4    Davis, A.5    Mortensen, R.B.6
  • 3
    • 0027507184 scopus 로고
    • Bacterial surface presentation of proteins and peptides: An alternative to phage technology?
    • Little, M., Fuchs, P., Breitling, F., and Dübel, S. 1993. Bacterial surface presentation of proteins and peptides: an alternative to phage technology? Trends Biotechnol. 11:3-5.
    • (1993) Trends Biotechnol , vol.11 , pp. 3-5
    • Little, M.1    Fuchs, P.2    Breitling, F.3    Dübel, S.4
  • 4
    • 0026086582 scopus 로고
    • Expression of foreign polypeptides at the Escherichia coli cell surface
    • Hofnung, M. 1991. Expression of foreign polypeptides at the Escherichia coli cell surface. Methods Cell Biol. 34:77-105.
    • (1991) Methods Cell Biol , vol.34 , pp. 77-105
    • Hofnung, M.1
  • 5
    • 0023822867 scopus 로고
    • Versatility of a vector for expressing foreign polypeptides at the surface of Gram-negative bacteria
    • Charbit, A., Molla, A., Saurín, W., and Hofnung, M. 1988. Versatility of a vector for expressing foreign polypeptides at the surface of Gram-negative bacteria. Gene 70:181-189.
    • (1988) Gene , vol.70 , pp. 181-189
    • Charbit, A.1    Molla, A.2    Saurín, W.3    Hofnung, M.4
  • 6
    • 0025309315 scopus 로고
    • Outer-membrane PhoE protein of Escherichia coli K-12 as an exposure vector: Possibilities and limitations
    • Agterberg, M., Adriaanse, H., van Bruggen, A., Karperien, M., and Tommassen, J. 1990. Outer-membrane PhoE protein of Escherichia coli K-12 as an exposure vector: possibilities and limitations. Gene 88:37-45.
    • (1990) Gene , vol.88 , pp. 37-45
    • Agterberg, M.1    Adriaanse, H.2    Van Bruggen, A.3    Karperien, M.4    Tommassen, J.5
  • 7
    • 0026631468 scopus 로고
    • Construction of stable LamB-Shiga toxin B subunit hybrids: Analysis of expression in Salmonella typhimurium aroA strains and stimulation of B subunit-specific mucosal and serum antibody responses
    • Su, G.-R, Brahmbhatt, H.N., Wehland, J., Ronde, M., and Timmis, K.N. 1992. Construction of stable LamB-Shiga toxin B subunit hybrids: analysis of expression in Salmonella typhimurium aroA strains and stimulation of B subunit-specific mucosal and serum antibody responses. Infect. Immun. 60:3345-3359.
    • (1992) Infect. Immun. , vol.60 , pp. 3345-3359
    • Su, G.-R.1    Brahmbhatt, H.N.2    Wehland, J.3    Ronde, M.4    Timmis, K.N.5
  • 8
    • 0029053958 scopus 로고
    • Pseudomonas aeruginosa outer membrane protein OprF as an expression vector for foreign epitopes: The effects of positioning and length on the antigenicity of the epitope
    • Wong, R.S.Y., Wirtz, RA, and Hancock, R.E.W. 1995. Pseudomonas aeruginosa outer membrane protein OprF as an expression vector for foreign epitopes: the effects of positioning and length on the antigenicity of the epitope. Gene 158:55-60.
    • (1995) Gene , vol.158 , pp. 55-60
    • Wong, R.S.Y.1    Wirtz, R.A.2    Hancock, R.E.W.3
  • 9
    • 0029971104 scopus 로고    scopus 로고
    • Topology of the membrane protein LamB by epitope tagging and a comparison with the X-ray model
    • Newton, S.M., Klebba, P.E., Michel, V., Hofnung, M., and Charbit, A. 1996. Topology of the membrane protein LamB by epitope tagging and a comparison with the X-ray model. J. Bacteriol. 178:3447-3456.
    • (1996) J. Bacteriol. , vol.178 , pp. 3447-3456
    • Newton, S.M.1    Klebba, P.E.2    Michel, V.3    Hofnung, M.4    Charbit, A.5
  • 10
    • 0026669435 scopus 로고
    • Engineered iron oxide-adhesion mutants of the Escherichia coli phage λ receptor
    • Brown, S. 1992. Engineered iron oxide-adhesion mutants of the Escherichia coli phage λ receptor. Proc. Natl. Acad. Sci. USA 89:8651-8655.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 8651-8655
    • Brown, S.1
  • 12
    • 0029817522 scopus 로고    scopus 로고
    • Enhanced metalloadsorption of bacterial cells displaying poly-His peptides
    • Sousa, C, Cebolla, A., and de Lorenzo, V. 1996. Enhanced metalloadsorption of bacterial cells displaying poly-His peptides. Nature Biotech. 14:1017-1020.
    • (1996) Nature Biotech , vol.14 , pp. 1017-1020
    • Sousa, C.1    Cebolla, A.2    De Lorenzo, V.3
  • 13
    • 0028947997 scopus 로고
    • Expression of thioredoxin random peptide libraries on the Escherichia coli cell surface as functional fusions to flagellin: A system designed for exploring protein-protein Interactions
    • Lu, Z., Murray, K.S., Van Cleave V, LaVallie, E.R., Stahl, M.L., and McCoy, J.M. 1995. Expression of thioredoxin random peptide libraries on the Escherichia coli cell surface as functional fusions to flagellin: A system designed for exploring protein-protein Interactions. Bio/Technology 13:366-372.
    • (1995) Bio/Technology , vol.13 , pp. 366-372
    • Lu, Z.1    Murray, K.S.2    Van Cleave, V.3    Lavallie, E.R.4    Stahl, M.L.5    McCoy, J.M.6
  • 14
    • 0029876415 scopus 로고    scopus 로고
    • Genetic selection of peptide aptamers that recognize cyclin-dependent kinase 2
    • Colas, P., Cohen, B., Jessen, T., Grishlna, I., McCoy, J., and Brent, R. 1996. Genetic selection of peptide aptamers that recognize cyclin-dependent kinase 2. Nature 380:548-550.
    • (1996) Nature , vol.380 , pp. 548-550
    • Colas, P.1    Cohen, B.2    Jessen, T.3    Grishlna, I.4    McCoy, J.5    Brent, R.6
  • 15
    • 0027378014 scopus 로고
    • Pap pili as a vector system for surface for surface exposition of an immunoglobulin G-binding domain of protein A of Staphylococcus aureus in Escherichia coli
    • Steidler, L, Remaut, E., and Fiers, W. 1993. Pap pili as a vector system for surface for surface exposition of an immunoglobulin G-binding domain of protein A of Staphylococcus aureus in Escherichia coli. J. Bacteriol. 175:7639-7643.
    • (1993) J. Bacteriol , vol.175 , pp. 7639-7643
    • Steidler, L.1    Remaut, E.2    Fiers, W.3
  • 16
    • 0028998480 scopus 로고
    • Expression and immunogenicity of an 18-residue epitope of HIV1 gp41 inserted in the flagellar protein of a Salmonella live vaccine
    • Newton, S.M.C., Joys, T.M., Anderson, S.A., Kennedy, R.C., Hovi, M.E., and Stocker, B.A.D. 1995. Expression and immunogenicity of an 18-residue epitope of HIV1 gp41 inserted in the flagellar protein of a Salmonella live vaccine. Res. Microbiol. 146:203-216.
    • (1995) Res. Microbiol , vol.146 , pp. 203-216
    • Newton, S.M.C.1    Joys, T.M.2    Erson, S.A.3    Kennedy, R.C.4    Hovi, M.E.5    Stocker, B.A.D.6
  • 17
    • 0028863961 scopus 로고
    • Chimeric FimH adhesin of type 1 fimbriae: A bacterial surface display system for heterologous sequences
    • Pallesen, L., Poulsen, L.K., Christiansen, G., and Klemm, P. 1995. Chimeric FimH adhesin of type 1 fimbriae: a bacterial surface display system for heterologous sequences. Microbiology 141:2839-2848.
    • (1995) Microbiology , vol.141 , pp. 2839-2848
    • Pallesen, L.1    Poulsen, L.K.2    Christiansen, G.3    Klemm, P.4
  • 19
    • 0027434697 scopus 로고
    • Membrane traffic wardens and protein secretion in Gram-negative bacteria
    • Salmong, G.P.C, and Reeves, P.J. 1993. Membrane traffic wardens and protein secretion in Gram-negative bacteria. Trends Biol. Sci. 18:7-12.
    • (1993) Trends Biol. Sci. , vol.18 , pp. 7-12
    • Salmong, G.1    Reeves, P.J.2
  • 20
    • 0024989426 scopus 로고
    • The TraT lipoprotein as a vehicle for the transport of foreign antigenic determinants to the cell surface of Escherichia coli K12: Structure-function relationship in the TraT protein
    • Taylor, I.M., Harrison, J.L, Timmis, K.N., and O’Connor, CD. 1990. The TraT lipoprotein as a vehicle for the transport of foreign antigenic determinants to the cell surface of Escherichia coli K12: structure-function relationship in the TraT protein. Mol. Microbiol. 4:1259-1268.
    • (1990) Mol. Microbiol. , vol.4 , pp. 1259-1268
    • Taylor, I.M.1    Harrison, J.L.2    Timmis, K.N.3    O’Connor, C.D.4
  • 21
    • 0027207223 scopus 로고
    • Lipid-tagged antibodies: Bacterial expression and characterization of a lipoprotein-single-chain antibody fusion protein
    • Laukkanen, M.-L, Teeri, T.T., and Keinanen, K. 1993. Lipid-tagged antibodies: bacterial expression and characterization of a lipoprotein-single-chain antibody fusion protein. Protein Engineer. 6:449-454.
    • (1993) Protein Engineer , vol.6 , pp. 449-454
    • Laukkanen, M.-L.1    Teeri, T.T.2    Keinanen, K.3
  • 22
    • 14744287360 scopus 로고
    • Targeting recombinant antibodies to the surface of Escherichia coli: Fusion to a peptido-glycan-associated lipoprotein
    • Fuchs, P., Breitling, F., Dübel, S., Seehaus, T., and Little, M. 1991. Targeting recombinant antibodies to the surface of Escherichia coli: fusion to a peptido-glycan-associated lipoprotein. Bio/Technology 9:1369-1372.
    • (1991) Bio/Technology , vol.9 , pp. 1369-1372
    • Fuchs, P.1    Breitling, F.2    Dübel, S.3    Seehaus, T.4    Little, M.5
  • 23
    • 13344280367 scopus 로고    scopus 로고
    • Development of new cloning vectors for the production of immunogenic outer membrane fusion proteins in Escherichia coli
    • Cornellis, P., Sierra, J.C., Lim Jr., A., Malur, A., Tungpradabkul, S., Tazka, H., et al. 1996. Development of new cloning vectors for the production of immunogenic outer membrane fusion proteins in Escherichia coli. Bio/Technology 14:203-208.
    • (1996) Bio/Technology , vol.14 , pp. 203-208
    • Cornellis, P.1    Sierra, J.C.2    Lim, A.3    Malur, A.4    Tungpradabkul, S.5    Tazka, H.6
  • 24
    • 0026594374 scopus 로고
    • Transport and anchoring of β-lactamase to the external surface of Escherichia coli
    • Francisco, J.A., Earhart, CF., and Georgiou, G. 1992. Transport and anchoring of β-lactamase to the external surface of Escherichia coli. Proc. Natl. Acad. Sci. USA 89:2713-2717.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 2713-2717
    • Francisco, J.A.1    Earhart, C.F.2    Georgiou, G.3
  • 25
    • 0029916414 scopus 로고    scopus 로고
    • Characterization of Escherichia coli expressing an Lpp’OmpA(46-159)-PhoA fusion protein localized In the outer membrane
    • Stathopoulos, C, Georgiou, G., and Earhart, C.F. 1996. Characterization of Escherichia coli expressing an Lpp’OmpA(46-159)-PhoA fusion protein localized In the outer membrane. Appl. Microbiol. Biotechnol. 45:112-119.
    • (1996) Appl. Microbiol. Biotechnol. , vol.45 , pp. 112-119
    • Stathopoulos, C.1    Georgiou, G.2    Earhart, C.F.3
  • 26
    • 0027751445 scopus 로고
    • The secretion pathway of IgA protease-type proteins in Gram-negative bacteria
    • Klauser, T., Pohlner, J., and Meyer, T.F. 1993. The secretion pathway of IgA protease-type proteins in Gram-negative bacteria. Bioessays 15:799-805.
    • (1993) Bioessays , vol.15 , pp. 799-805
    • Klauser, T.1    Pohlner, J.2    Meyer, T.F.3
  • 27
    • 0028824728 scopus 로고
    • Common structural features of lgA1 protease-like outer membrane protein
    • Jose, J., Jaehnig, F., and Meyer, T.F. 1995. Common structural features of lgA1 protease-like outer membrane protein. Mol. Microbiol. 18:378-380.
    • (1995) Mol. Microbiol. , vol.18 , pp. 378-380
    • Jose, J.1    Jaehnig, F.2    Meyer, T.F.3
  • 30
    • 0027987985 scopus 로고
    • A Haemophilus influenzae IgA protease-like protein promotes intimate interaction with human epithelial cells
    • St. Gerne, J.W. III, de la Morena, M.L, and Falkow, S. 1994. A Haemophilus influenzae IgA protease-like protein promotes intimate interaction with human epithelial cells. Mol. Microbiol. 14:217-233.
    • (1994) Mol. Microbiol. , vol.14 , pp. 217-233
    • St. Gerne, J.W.1    De La Morena, M.L.2    Falkow, S.3
  • 31
    • 0025353145 scopus 로고
    • Extracellular transport of cholera toxin B subunit using Neisseria IgA protease B-domain: Conformation-dependent outer membrane translocation
    • Klauser, T, Pohlner, J., and Meyer, T.F. 1990. Extracellular transport of cholera toxin B subunit using Neisseria IgA protease B-domain: conformation-dependent outer membrane translocation. EMBO J. 9:1991-1999.
    • (1990) EMBO J , vol.9 , pp. 1991-1999
    • Klauser, T.1    Pohlner, J.2    Meyer, T.F.3
  • 32
    • 0025122755 scopus 로고
    • The normally perlplasmic enzyme β-lactamase is specifically and efficiently translocated through the Escherichia coli outer membrane when it is fused to the cell-surface enzyme pullulanase
    • Kornacker, M.G. and Pugsley, A.P. 1990. The normally perlplasmic enzyme β-lactamase is specifically and efficiently translocated through the Escherichia coli outer membrane when it is fused to the cell-surface enzyme pullulanase. Mol. Microbiol. 4:1101-1109.
    • (1990) Mol. Microbiol. , vol.4 , pp. 1101-1109
    • Kornacker, M.G.1    Pugsley, A.P.2
  • 33
    • 0008804841 scopus 로고    scopus 로고
    • Gram-positive commensal bacteria deliver antigens to elicit mucosal and systemic immunity
    • Fischetti, V.A. 1996. Gram-positive commensal bacteria deliver antigens to elicit mucosal and systemic immunity. ASM News 62:405-410.
    • (1996) ASM News , vol.62 , pp. 405-410
    • Fischetti, V.A.1
  • 34
    • 0026719273 scopus 로고
    • Expression of recombinant proteins on the surface of the coagulase-negative bacterium Staphylococcus xylosus
    • Hansson, M., Stahl, S., Nguyen, T.N., Bachi, T., Robert, A., Binz, H., et al. 1992. Expression of recombinant proteins on the surface of the coagulase-negative bacterium Staphylococcus xylosus. J. Bacteriol. 174:4239-4245.
    • (1992) J. Bacteriol , vol.174 , pp. 4239-4245
    • Hansson, M.1    Stahl, S.2    Nguyen, T.N.3    Bachi, T.4    Robert, A.5    Binz, H.6
  • 35
    • 0028953525 scopus 로고
    • Cell surface display of recombinant proteins on Staphylococcus carnosus
    • Samuelson, P., Hansson, M., Ahlborg, N., Andreoni, C, Gotz, F., Bachi, T., et al. 1995. Cell surface display of recombinant proteins on Staphylococcus carnosus. J. Bacteriol. 177:1470-1476.
    • (1995) J. Bacteriol , vol.177 , pp. 1470-1476
    • Samuelson, P.1    Hansson, M.2    Ahlborg, N.3    Reoni, C.4    Gotz, F.5    Bachi, T.6
  • 37
    • 0027155236 scopus 로고
    • Targeting of a heterologous protein to the cell wall of Saccharomyces cerevisiae
    • Schreuder, M.P., Brekelmans, S., van der Ende, H., and Klis, RM. 1993. Targeting of a heterologous protein to the cell wall of Saccharomyces cerevisiae. Yeast 9:399-409.
    • (1993) Yeast , vol.9 , pp. 399-409
    • Schreuder, M.P.1    Brekelmans, S.2    Van Der Ende, H.3    Klis, R.M.4
  • 38
    • 0029878805 scopus 로고    scopus 로고
    • Yeast expressing hepatitis B virus surface antigen determinants on its surface: Implications for a possible oral vaccine
    • Schreuder, M.R, Deen, C, Boersma, W.J.A., Pouwels, PH., and Klis, F.M. 1996. Yeast expressing hepatitis B virus surface antigen determinants on its surface: implications for a possible oral vaccine. Vaccine 14:383-388.
    • (1996) Vaccine , vol.14 , pp. 383-388
    • Schreuder, M.R.1    Deen, C.2    Boersma, W.J.A.3    Pouwels, P.H.4    Klis, F.M.5
  • 41
    • 0029983637 scopus 로고    scopus 로고
    • Display of β-lactamase on the Escherichia coli surface: Outer membrane phenotypes conferred by Lpp’-OmpA’-B-lactamase fusions
    • Georgiou, G., Stephens, D.L., Stathopoulos, C, Poetschle H.L., Mendenhall, J., and Earhart, C.F. 1996. Display of β-lactamase on the Escherichia coli surface: outer membrane phenotypes conferred by Lpp’-OmpA’-B-lactamase fusions. Protein Engineer. 9:239-247.
    • (1996) Protein Engineer , vol.9 , pp. 239-247
    • Georgiou, G.1    Stephens, D.L.2    Stathopoulos, C.3    Poetschle, H.L.4    Mendenhall, J.5    Earhart, C.F.6
  • 42
    • 0027109458 scopus 로고
    • Artificial antigens. Synthetic carbohydrate haptens immobilized on crystalline bacterial surface layer glycoproteins
    • Messner, P., Mazid, MA, Unger, F.M., and Sleytr, U.B. 1992. Artificial antigens. Synthetic carbohydrate haptens immobilized on crystalline bacterial surface layer glycoproteins. Carbohydr. Res. 233:175-184.
    • (1992) Carbohydr. Res. , vol.233 , pp. 175-184
    • Messner, P.1    Mazid, M.A.2    Unger, F.M.3    Sleytr, U.B.4
  • 43
    • 0029664728 scopus 로고    scopus 로고
    • Toward selective elicitation of TH1-controlled vaccination responses: Vaccine applications of bacterial surface layer proteins
    • Jahn-Schmid, B., Messner, P., Unger, F.M., Sleytr, U.B., Scheiner, O., Kraft, D. 1996. Toward selective elicitation of TH1-controlled vaccination responses: vaccine applications of bacterial surface layer proteins. J. Biotechnol. 44:225-231.
    • (1996) J. Biotechnol. , vol.44 , pp. 225-231
    • Jahn-Schmid, B.1    Messner, P.2    Unger, F.M.3    Sleytr, U.B.4    Scheiner, O.5    Kraft, D.6
  • 45
    • 0025112794 scopus 로고
    • Searching for peptide ligands with an epitope library
    • Scott, J.K. and Smith, G.P. 1990. Searching for peptide ligands with an epitope library. Science 249:386-390.
    • (1990) Science , vol.249 , pp. 386-390
    • Scott, J.K.1    Smith, G.P.2
  • 47
    • 0027136111 scopus 로고
    • Affinity maturation of human growth hormone by monovalent phage display
    • Lowman, H.B. and Wells, J.A. 1993. Affinity maturation of human growth hormone by monovalent phage display. J. Mol. Biol. 234:564-578.
    • (1993) J. Mol. Biol. , vol.234 , pp. 564-578
    • Lowman, H.B.1    Wells, J.A.2
  • 48
    • 0029920670 scopus 로고    scopus 로고
    • Probing the basis of antibody reactivity with a panel of constrained peptide libraries displayed by filamentous phage
    • Bonnycastle, L.L.C., Mehroke, J.S., Rashed, M., Gong, X., and Scott, J.K. 1996. Probing the basis of antibody reactivity with a panel of constrained peptide libraries displayed by filamentous phage. J. Mol. Biol. 258:747-762.
    • (1996) J. Mol. Biol. , vol.258 , pp. 747-762
    • Bonnycastle, L.L.C.1    Mehroke, J.S.2    Rashed, M.3    Gong, X.4    Scott, J.K.5
  • 49
    • 0029953760 scopus 로고    scopus 로고
    • Iterative optimization of high affinity protease inhibitors using phage display. 1 plasmin
    • Markland, W., Ley, A.C., Lee, S.W., and Ladner, R.C. 1996. Iterative optimization of high affinity protease inhibitors using phage display. 1 plasmin. Biochem. 35:8045-8057.
    • (1996) Biochem , vol.35 , pp. 8045-8057
    • Markland, W.1    Ley, A.C.2    Lee, S.W.3    Ladner, R.C.4
  • 50
    • 0029927067 scopus 로고    scopus 로고
    • Phage display of proteases and macromoiecular inhibitors
    • Wang, C.I., Yang, Q., and Cralk, C.S. 1996. Phage display of proteases and macromoiecular inhibitors. Methods Enzymol. 267:28-51.
    • (1996) Methods Enzymol. , vol.267 , pp. 28-51
    • Wang, C.I.1    Yang, Q.2    Cralk, C.S.3
  • 51
    • 0027316004 scopus 로고
    • Substrate phage: Selection of protease substrates by monovalent phage display
    • Matthews, D.J. and Wells, J.A. 1993. Substrate phage: Selection of protease substrates by monovalent phage display. Science 260:113-117.
    • (1993) Science , vol.260 , pp. 113-117
    • Matthews, D.J.1    Wells, J.A.2
  • 52
    • 0027994717 scopus 로고
    • Toward a code for the interactions of zinc fingers with DNA: Selection of randomized zinc fingers displayed on phage
    • Choo, Y. and Klug, A. 1994. Toward a code for the interactions of zinc fingers with DNA: Selection of randomized zinc fingers displayed on phage. Proc. Natl. Acad. Sci. USA 91:11163-11167.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 11163-11167
    • Choo, Y.1    Klug, A.2
  • 53
    • 0028672525 scopus 로고
    • Human antibodies from combinatorial libraries
    • Burton, D.R. and Barbas III, C.F. 1994. Human antibodies from combinatorial libraries. Adv. Immunol. 57:191-281.
    • (1994) Adv. Immunol , vol.57 , pp. 191-281
    • Burton, D.R.1    Barbas, C.F.2
  • 55
    • 0029955258 scopus 로고    scopus 로고
    • Selection of linkers for a catalytic single chain antibody using phage display technology
    • Tang, Y., Jiang, N., Prakh, C, and Hilvert, D. 1996. Selection of linkers for a catalytic single chain antibody using phage display technology. J. Biol. Chem. 271:15682-15686.
    • (1996) J. Biol. Chem. , vol.271 , pp. 15682-15686
    • Tang, Y.1    Jiang, N.2    Prakh, C.3    Hilvert, D.4
  • 56
    • 0027425230 scopus 로고
    • Production and fluorescence-activated cell sorting of Escherichia coli expressing a functional antibody fragment on the external surface
    • Francisco, J.A., Campbell, R., Iverson, B.L., and Georgiou, G. 1993. Production and fluorescence-activated cell sorting of Escherichia coli expressing a functional antibody fragment on the external surface. Proc. Natl. Acad. Sci. USA 90:10444-10448.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 10444-10448
    • Francisco, J.A.1    Campbell, R.2    Iverson, B.L.3    Georgiou, G.4
  • 57
    • 0028962883 scopus 로고
    • Characterization of phage that binds plastic from phage-dlsplayed random peptide libraries
    • Adey, N.B., Mataragnon, A.H., Rider, J.E., Carter, J.M., and Kay, B.K. 1995. Characterization of phage that binds plastic from phage-dlsplayed random peptide libraries. Gene 156:27-31.
    • (1995) Gene , vol.156 , pp. 27-31
    • Adey, N.B.1    Mataragnon, A.H.2    Rider, J.E.3    Carter, J.M.4    Kay, B.K.5
  • 58
    • 0028845856 scopus 로고
    • Contribution of antibody heavy chain CDR1 to digoxln binding analyzed by random mutagenesis of phage-displayed Fab 26-10
    • Short, M.K., Jeffrey, P.D., Kwong, R., and Margolles, M.N. 1995. Contribution of antibody heavy chain CDR1 to digoxln binding analyzed by random mutagenesis of phage-displayed Fab 26-10. J. Biol. Chem. 270:28541-28550.
    • (1995) J. Biol. Chem. , vol.270 , pp. 28541-28550
    • Short, M.K.1    Jeffrey, P.D.2    Kwong, R.3    Margolles, M.N.4
  • 59
    • 0028966985 scopus 로고
    • Engineered turns of a recombinant antibody improve its in vivo folding
    • Knappik, A. and Plilckthun, A. 1995. Engineered turns of a recombinant antibody improve its in vivo folding. Protein Eng. 8:81-89.
    • (1995) Protein Eng , vol.8 , pp. 81-89
    • Knappik, A.1    Plilckthun, A.2
  • 61
    • 0030048583 scopus 로고    scopus 로고
    • Construction and evolution of antibody-phage libraries by DNA shuffling
    • Crameri, A., Cwirla, S., and Stemmer, W.P.C. 1996. Construction and evolution of antibody-phage libraries by DNA shuffling. Nature Medic. 2:100-102.
    • (1996) Nature Medic , vol.2 , pp. 100-102
    • Crameri, A.1    Cwirla, S.2    Stemmer, W.P.C.3
  • 62
    • 0030199402 scopus 로고    scopus 로고
    • A quantitative immunoassay utilizing Escherichia coli cells possessing surface-exposed single chain Fv molecules
    • Chen, G., Cloud, J., Georgiou, G., and Iverson, B.L 1996. A quantitative immunoassay utilizing Escherichia coli cells possessing surface-exposed single chain Fv molecules. Biotechnol. Progr. 12:572-574.
    • (1996) Biotechnol. Progr. , vol.12 , pp. 572-574
    • Chen, G.1    Cloud, J.2    Georgiou, G.3    Iverson, B.L.4
  • 63
    • 0027473684 scopus 로고
    • Human anti-self antibodies with high specificity from phage display libraries
    • Griffiths, D. et al. 1993. Human anti-self antibodies with high specificity from phage display libraries. EMBO J. 12:725-734.
    • (1993) EMBO J , vol.12 , pp. 725-734
    • Griffiths, D.1
  • 64
    • 0029564921 scopus 로고    scopus 로고
    • CDR walking mutagenesis for the affinity maturation of a potent human anti-HIV antibody into the picomolar range
    • Yang, W.-R, Green, K., Pinz-Sweeney, S., Briones, A.T., Burton, D.R., and Barbas III, C.F. 1996. CDR walking mutagenesis for the affinity maturation of a potent human anti-HIV antibody into the picomolar range. J. Mol. Biol. 254:392–403.
    • (1996) J. Mol. Biol. , vol.254 , pp. 392-403
    • Yang, W.-R.1    Green, K.2    Pinz-Sweeney, S.3    Briones, A.T.4    Burton, D.R.5    Barbas, C.F.6
  • 65
    • 0029749705 scopus 로고
    • New methods for detection, analysis and isolation of rare cell populations
    • Leary, J.F., McLaughlin, S.R., and Kavanau, K. 1995. New methods for detection, analysis and isolation of rare cell populations. SPIE 2678:240-253.
    • (1995) SPIE , vol.2678 , pp. 240-253
    • Leary, J.F.1    McLaughlin, S.R.2    Kavanau, K.3
  • 66
    • 0025486622 scopus 로고
    • Antigen delivery systems for analysing host Immune responses and for vaccine development
    • Curtiss, R. III. 1990. Antigen delivery systems for analysing host Immune responses and for vaccine development. Trends Biotechnol. 8:237-240.
    • (1990) Trends Biotechnol , vol.8 , pp. 237-240
    • Curtiss, R.1
  • 67
    • 0002809316 scopus 로고
    • Salmonella as carriers of heterologous antigens
    • O’Hagan, D. T. (ed.). CRC Press, Inc
    • Roberts, M., Chatfield, S.N., Dougan, G. 1994. Salmonella as carriers of heterologous antigens, pp. 27-58 in Novel delivery systems for oral vaccines. O’Hagan, D. T. (ed.). CRC Press, Inc.
    • (1994) Novel Delivery Systems for Oral Vaccines , pp. 27-58
    • Roberts, M.1    Chatfield, S.N.2    Dougan, G.3
  • 68
    • 0002423687 scopus 로고
    • Attenuated Salmonella strains as live vectors for the expression of foreign antigens
    • Woodrow, G.C and Levine, M.M. (eds.). Marcel Dekker, Inc
    • Curtiss, R. III. 1990. Attenuated Salmonella strains as live vectors for the expression of foreign antigens, pp. 161-188 in New generation vaccines. Woodrow, G.C and Levine, M.M. (eds.). Marcel Dekker, Inc.
    • (1990) New Generation Vaccines , pp. 161-188
    • Curtiss, R.1
  • 69
    • 0026636250 scopus 로고
    • Oral immunization using live attenuated Salmonella spp. As earners of foreign antigens
    • Cardenas, L. and Clements, J.D. 1992. Oral immunization using live attenuated Salmonella spp. as earners of foreign antigens. Clin. Microbiol. Rev. 5:328-342.
    • (1992) Clin. Microbiol. Rev. , vol.5 , pp. 328-342
    • Cardenas, L.1    Clements, J.D.2
  • 71
    • 0025597139 scopus 로고
    • Construction and evaluation of live attenuated vaccine strains of Shigella flexneri and Shigella dysenteriae 1 Res
    • Fortaine, A., Arondel, J., and Sansonetti, P.J. 1990. Construction and evaluation of live attenuated vaccine strains of Shigella flexneri and Shigella dysenteriae 1 Res. Microbiol. 141:907-912.
    • (1990) Microbiol , vol.141 , pp. 907-912
    • Fortaine, A.1    Arondel, J.2    Sansonetti, P.J.3
  • 72
    • 0002313665 scopus 로고    scopus 로고
    • Strategies for the use of live recombinant avlrulent bacterial vaccines for mucosal immunization
    • Kagnoff, M.F. and Kiyono, H. (eds.). Academic Press, Inc
    • Curtiss, R. III, Doggett, T., Nayak, A.R., and Srinivason, J. 1996. Strategies for the use of live recombinant avlrulent bacterial vaccines for mucosal immunization, pp. 499-511 in Essentials of mucosal immunology. Kagnoff, M.F. and Kiyono, H. (eds.). Academic Press, Inc.
    • (1996) Essentials of Mucosal Immunology , pp. 499-511
    • Curtiss, R.1    Doggett, T.2    Nayak, A.R.3    Srinivason, J.4
  • 73
    • 0019819989 scopus 로고
    • Construction of a potent bivalent vaccine strain: Introduction of Shigella sonnei form I antigen genes into the galE S. Typhi Ty21 a typhoid vaccine strain
    • Formal, S.B., Baron, L.S., Kopecko, D.J., Powell, C, and Life, CA. 1981. Construction of a potent bivalent vaccine strain: Introduction of Shigella sonnei form I antigen genes into the galE S. typhi Ty21 a typhoid vaccine strain. Infect. Immun. 34:746-750.
    • (1981) Infect. Immun. , vol.34 , pp. 746-750
    • Formal, S.B.1    Baron, L.S.2    Kopecko, D.J.3    Powell, C.4    Life, C.A.5
  • 74
    • 0025328103 scopus 로고
    • Specific immunoglobulin A-secreting cells in peripheral blood of humans following oral immunization with a bivalent Salmonella typhi-Shigella sonnei vaccine or infection by pathogenic S. Sonnei
    • van de Verg, L, Herrington, D.A., Murphy, J.R., Wasserman, S.S., Formal, S.B., and Levine, M.M. 1990. Specific immunoglobulin A-secreting cells in peripheral blood of humans following oral immunization with a bivalent Salmonella typhi-Shigella sonnei vaccine or infection by pathogenic S. sonnei. Infect. Immun. 58:2002-2004.
    • (1990) Infect. Immun , vol.58 , pp. 2002-2004
    • Van De Verg, L.1    Herrington, D.A.2    Murphy, J.R.3    Wasserman, S.S.4    Formal, S.B.5    Levine, M.M.6
  • 75
    • 84982574536 scopus 로고
    • Galactose eplmeraseless (GalE) mutant G30 of Salmonella typhimurium Is a good potential live oral vaccine carrier for fimbrial antigens
    • Stevenson, G. and Manning, P.A. 1985. Galactose eplmeraseless (galE) mutant G30 of Salmonella typhimurium Is a good potential live oral vaccine carrier for fimbrial antigens. FEMS Microbiol. Lett. 28:317-321.
    • (1985) FEMS Microbiol. Lett. , vol.28 , pp. 317-321
    • Stevenson, G.1    Manning, P.A.2
  • 77
    • 0024558027 scopus 로고
    • Immune responses to cholera toxin epitope inserted in Salmonella flagellin
    • Newton, S.M., Jacob, C, and Stocker, B.A.D. 1989. Immune responses to cholera toxin epitope inserted in Salmonella flagellin. Science 244:70-72.
    • (1989) Science , vol.244 , pp. 70-72
    • Newton, S.M.1    Jacob, C.2    Stocker, B.A.D.3
  • 78
    • 0025847989 scopus 로고
    • Surface expression of malarial antigens in Salmonella typhimurium: Induction of serum antibody response upon oral vaccination of mice
    • Schorr, J., Knapp, B., Hundt, E., Küpper, H.A., and Amman, E. 1991. Surface expression of malarial antigens in Salmonella typhimurium: induction of serum antibody response upon oral vaccination of mice. Vaccine 9:675-681.
    • (1991) Vaccine , vol.9 , pp. 675-681
    • Schorr, J.1    Knapp, B.2    Hundt, E.3    Küpper, H.A.4    Amman, E.5
  • 79
    • 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., and Kaufmann, S.H.E. 1996. Superior efficacy of secreted over somatic antigen display in recombinant Salmonella vaccine induced protection against listeriosis. Proc. Natl. Acad. Sci. USA 93:1458-1463.
    • (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.E.7
  • 81
    • 0028323422 scopus 로고
    • OmpA-FMDV VP1 fusion protein: Production, cell surface exposure and immune responses to the major antigenic domain of foot-and-mouth disease virus
    • Ruppert, A., Arnold, N., and Hobom, G. 1994. OmpA-FMDV VP1 fusion protein: production, cell surface exposure and immune responses to the major antigenic domain of foot-and-mouth disease virus. Vaccine 12:492-498.
    • (1994) Vaccine , vol.12 , pp. 492-498
    • Ruppert, A.1    Arnold, N.2    Hobom, G.3
  • 82
    • 0023201148 scopus 로고
    • Presentation of two epitopes of the preS2 region of hepatitis B virus on live recombinant bacteria
    • Charbit, A., Sobczak, E., Michel, M-L, Molla, A., Tiollais, P., and Hofnung, M. 1987. Presentation of two epitopes of the preS2 region of hepatitis B virus on live recombinant bacteria. J. Immunol. 139:1644-1658.
    • (1987) J. Immunol. , vol.139 , pp. 1644-1658
    • Charbit, A.1    Sobczak, E.2    Michel, M.-L.3    Molla, A.4    Tiollais, P.5    Hofnung, M.6
  • 83
    • 0024368708 scopus 로고
    • Antibody response to a foreign epitope expressed at the surface of recombinant bacteria: Importance of the route of immunization
    • Leclere, C, Charbit, A., Molla, A., and Hofnung, M. 1989. Antibody response to a foreign epitope expressed at the surface of recombinant bacteria: importance of the route of immunization. Vaccine 7:242-248.
    • (1989) Vaccine , vol.7 , pp. 242-248
    • Leclere, C.1    Charbit, A.2    Molla, A.3    Hofnung, M.4
  • 84
    • 0025044089 scopus 로고
    • Protection of guinea-pigs against foot-and-mouth disease virus by immunization with a PhoE-FMDV hybrid protein
    • Agterberg, M., Adrlaanse, H., Barteling, S., van Maanen, K., and Tommassen, J. 1990. Protection of guinea-pigs against foot-and-mouth disease virus by immunization with a PhoE-FMDV hybrid protein. Vaccine 8:438-440.
    • (1990) Vaccine , vol.8 , pp. 438-440
    • Agterberg, M.1    Adrlaanse, H.2    Barteling, S.3    Van Maanen, K.4    Tommassen, J.5
  • 85
    • 0029118119 scopus 로고
    • Mucosal and systemic immune responses to a recombinant protein expressed on the surface of the oral commensal bacterium Streptococcus gordonii alter oral colonization
    • Medaglini, D., Pozzi, G., King, T.P., and Fischetti, V.A. 1995. Mucosal and systemic immune responses to a recombinant protein expressed on the surface of the oral commensal bacterium Streptococcus gordonii alter oral colonization. Proc. Natl. Acad. Sci. USA 92:6868-6872.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 6868-6872
    • Medaglini, D.1    Pozzi, G.2    King, T.P.3    Fischetti, V.A.4
  • 86
    • 0026872822 scopus 로고
    • Induction of a humoral Immune response to a Shiga toxin B subunit epitope expressed as a chimeric LamB protein in a Shigella flexneri live vaccine strain
    • Ryd, M., Verma, N., and Lindberg, A.A. 1992. Induction of a humoral Immune response to a Shiga toxin B subunit epitope expressed as a chimeric LamB protein in a Shigella flexneri live vaccine strain. Microbiol. Pathogen. 12:399-407.
    • (1992) Microbiol. Pathogen. , vol.12 , pp. 399-407
    • Ryd, M.1    Verma, N.2    Lindberg, A.A.3
  • 88
    • 0018200168 scopus 로고
    • Use of Staphylococcal protein A as an immunological reagent
    • Goding, J.W. 1978. Use of Staphylococcal protein A as an immunological reagent. J. Immunol. Meth. 20:241-254.
    • (1978) J. Immunol. Meth. , vol.20 , pp. 241-254
    • Goding, J.W.1
  • 89
    • 31244437922 scopus 로고
    • Purification of goat immunoglobulin G1 (LgG1) and lgG2 antibodies by use of Streptococcus dysgalactiae cells with Fv receptors
    • Rantamaki, L.K. and Muller, H.-P. 1995. Purification of goat immunoglobulin G1 (lgG1) and lgG2 antibodies by use of Streptococcus dysgalactiae cells with Fv receptors. Veter. Immunol, immunopath. 45:115-126.
    • (1995) Veter. Immunol, Immunopath. , vol.45 , pp. 115-126
    • Rantamaki, L.K.1    Muller, H.-P.2
  • 90
    • 0030571577 scopus 로고    scopus 로고
    • Fixation and stabilization of E. Coli cells displaying genetically engineered cell surface proteins
    • Freeman, A., Abramov, S., and Georgiou, G. 1996. Fixation and stabilization of E. coli cells displaying genetically engineered cell surface proteins. Biotechnol. Bioeng. 52:625-630.
    • (1996) Biotechnol. Bioeng. , vol.52 , pp. 625-630
    • Freeman, A.1    Abramov, S.2    Georgiou, G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.