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Volumn 2, Issue 5, 2014, Pages

Spore surface display

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; HYBRID PROTEIN; MEMBRANE PROTEIN; PROTEIN BINDING;

EID: 84927787905     PISSN: None     EISSN: 21650497     Source Type: Journal    
DOI: 10.1128/microbiolspec.TBS-0011-2012     Document Type: Article
Times cited : (50)

References (109)
  • 4
    • 41549136380 scopus 로고    scopus 로고
    • Versatile microbial surfacedisplay for environmental remediation and biofuels production
    • Wu CH, Mulchandani A, Chen W. 2008. Versatile microbial surfacedisplay for environmental remediation and biofuels production. Trends Microbiol 16:181-188.
    • (2008) Trends Microbiol , vol.16 , pp. 181-188
    • Wu, C.H.1    Mulchandani, A.2    Chen, W.3
  • 5
    • 0031957257 scopus 로고    scopus 로고
    • Metalloadsorption by Escherichia coli cells displaying yeast and mammalian metallothioneins anchored to the outer membrane protein LamB
    • Sousa C, Kotrba P, Ruml T, Cebolla A, De Lorenzo V. 1998. Metalloadsorption by Escherichia coli cells displaying yeast and mammalian metallothioneins anchored to the outer membrane protein LamB. J Bacteriol 180:2280-2284.
    • (1998) J Bacteriol , vol.180 , pp. 2280-2284
    • Sousa, C.1    Kotrba, P.2    Ruml, T.3    Cebolla, A.4    De Lorenzo, V.5
  • 6
    • 0029817522 scopus 로고    scopus 로고
    • Enhanced metalloadsorption of bacterial cells displaying poly-His peptides
    • Sousa C, Cebolla A, de Lorenzo V. 1996. Enhanced metalloadsorption of bacterial cells displaying poly-His peptides. Nat. Biotechnol. 14:1017-1020.
    • (1996) Nat. Biotechnol , vol.14 , pp. 1017-1020
    • Sousa, C.1    Cebolla, A.2    de Lorenzo, V.3
  • 7
    • 0034732652 scopus 로고    scopus 로고
    • Engineering outer-membrane proteins in Pseudomonas putida for enhanced heavy metal bioadsorption
    • Valls M, de Lorenzo V, Gonzalez-Duarte R, Atrian S. 2000. Engineering outer-membrane proteins in Pseudomonas putida for enhanced heavy metal bioadsorption. J Inorg Biochem 79:219-223.
    • (2000) J Inorg Biochem , vol.79 , pp. 219-223
    • Valls, M.1    de Lorenzo, V.2    Gonzalez-Duarte, R.3    Atrian, S.4
  • 8
    • 0034045457 scopus 로고    scopus 로고
    • Engineering a mouse metallothionein on the cell surface of Ralstonia eutropha CH34 for immobilization of heavy metals in soil
    • Valls M, Atrian S, de Lorenzo V, Fernandez LA. 2000. Engineering a mouse metallothionein on the cell surface of Ralstonia eutropha CH34 for immobilization of heavy metals in soil. Nat Biotechol 18:661-665.
    • (2000) Nat Biotechol , vol.18 , pp. 661-665
    • Valls, M.1    Atrian, S.2    de Lorenzo, V.3    Fernandez, L.A.4
  • 9
    • 0034610528 scopus 로고    scopus 로고
    • Enhanced bioaccumulation of heavy metals by bacterial cells displaying synthetic phytochelatins
    • Bae W, Chen W, Mulchandani A, Mehra R. 2000. Enhanced bioaccumulation of heavy metals by bacterial cells displaying synthetic phytochelatins. Biotechnol Bioeng 70:518-524.
    • (2000) Biotechnol Bioeng , vol.70 , pp. 518-524
    • Bae, W.1    Chen, W.2    Mulchandani, A.3    Mehra, R.4
  • 10
    • 0035512233 scopus 로고    scopus 로고
    • Genetic engineering of Escherichia coli for enhanced uptake and bioaccumulation of mercury
    • Bae W, Mehra R, Mulchandani A, Chen W. 2001. Genetic engineering of Escherichia coli for enhanced uptake and bioaccumulation of mercury. Appl Environ Microbiol 67:5335-5338.
    • (2001) Appl Environ Microbiol , vol.67 , pp. 5335-5338
    • Bae, W.1    Mehra, R.2    Mulchandani, A.3    Chen, W.4
  • 11
    • 0037081387 scopus 로고    scopus 로고
    • Cell surface display of synthetic phytochelatins using ice nucleation protein for enhanced heavy metal bioaccumulation
    • Bae W, Mulchandani A, Chen W. 2002. Cell surface display of synthetic phytochelatins using ice nucleation protein for enhanced heavy metal bioaccumulation. J Inorg Biochem 88:223-227.
    • (2002) J Inorg Biochem , vol.88 , pp. 223-227
    • Bae, W.1    Mulchandani, A.2    Chen, W.3
  • 12
    • 0030855956 scopus 로고    scopus 로고
    • Biodegradation of organophosphorus pesticides by surface-expressed organophosphorus hydrolase
    • Richins R, Kaneva I, Mulchandani A, Chen W. 1997. Biodegradation of organophosphorus pesticides by surface-expressed organophosphorus hydrolase. Nature Biotechnol 15:984-987.
    • (1997) Nature Biotechnol , vol.15 , pp. 984-987
    • Richins, R.1    Kaneva, I.2    Mulchandani, A.3    Chen, W.4
  • 13
    • 0029924013 scopus 로고    scopus 로고
    • Surface display of a functional single-chain Fv antibody on staphylococci
    • Gunneriusson E, Samuelson P, Uhlen M, Nygren PA, Stahl S. 1996. Surface display of a functional single-chain Fv antibody on staphylococci. J Bacteriol 178:1341-1346.
    • (1996) J Bacteriol , vol.178 , pp. 1341-1346
    • Gunneriusson, E.1    Samuelson, P.2    Uhlen, M.3    Nygren, P.A.4    Stahl, S.5
  • 14
    • 21644484287 scopus 로고    scopus 로고
    • Expression of a functional single-chain Fv antibody on the surface of Streptococcus gordonii
    • Giomarelli B, Maggi T, Younson J, Kelly C, Pozzi G. 2004 Expression of a functional single-chain Fv antibody on the surface of Streptococcus gordonii. Mol Biotechnol 28:105-112.
    • (2004) Mol Biotechnol , vol.28 , pp. 105-112
    • Giomarelli, B.1    Maggi, T.2    Younson, J.3    Kelly, C.4    Pozzi, G.5
  • 15
    • 0035249432 scopus 로고    scopus 로고
    • Biotechnological applications of phage and cell display
    • Benhar I. 2001. Biotechnological applications of phage and cell display. Biotechnol Adv 19:1-33.
    • (2001) Biotechnol Adv , vol.19 , pp. 1-33
    • Benhar, I.1
  • 16
    • 0028138396 scopus 로고
    • Structural mimicry and enhanced immunogenicity of peptide epitopes displayed on filamentous bacteriophage. The V3 loop of HIV-1 gp120
    • di Marzo Veronese F, Willis AE, Boyer-Thompson C, Appella E, Perham RN. 1994. Structural mimicry and enhanced immunogenicity of peptide epitopes displayed on filamentous bacteriophage. The V3 loop of HIV-1 gp120. J. Mol Biol 243:167-172.
    • (1994) J. Mol Biol , vol.243 , pp. 167-172
    • di Marzo Veronese, F.1    Willis, A.E.2    Boyer-Thompson, C.3    Appella, E.4    Perham, R.N.5
  • 17
    • 0030833999 scopus 로고    scopus 로고
    • Display of a PorA peptide from Neisseria meningitidis on the bacteriophage T4 capsid surface
    • Jiang J, Abu-Shilbayeh L, Rao VB. 1997. Display of a PorA peptide from Neisseria meningitidis on the bacteriophage T4 capsid surface. Infect Immun 65:4770-4777.
    • (1997) Infect Immun , vol.65 , pp. 4770-4777
    • Jiang, J.1    Abu-Shilbayeh, L.2    Rao, V.B.3
  • 18
    • 0026411004 scopus 로고
    • Selection of antibody ligands from a large library of oligopeptides expressed on a multivalent exposition vector
    • Felici F, Castagnoli L, Musacchio A, Jappelli R, Cesareni G. 1991. Selection of antibody ligands from a large library of oligopeptides expressed on a multivalent exposition vector. J Mol Biol 222:301-310.
    • (1991) J Mol Biol , vol.222 , pp. 301-310
    • Felici, F.1    Castagnoli, L.2    Musacchio, A.3    Jappelli, R.4    Cesareni, G.5
  • 20
    • 0028216366 scopus 로고
    • A general strategy to identify mimotopes of pathological antigens using only random peptide libraries and human sera
    • Folgori A, Tafi R, Meola A, Felici F, Galfre G, Cortese R, Monaci P, Nicosia A. 1994. A general strategy to identify mimotopes of pathological antigens using only random peptide libraries and human sera. EMBO J 13:2236-2243.
    • (1994) EMBO J , vol.13 , pp. 2236-2243
    • Folgori, A.1    Tafi, R.2    Meola, A.3    Felici, F.4    Galfre, G.5    Cortese, R.6    Monaci, P.7    Nicosia, A.8
  • 21
    • 0027241244 scopus 로고
    • Cell-surface display of heterologous epitopes on Staphylococcus xylosus as a potential delivery system for oral vaccination
    • Nguyen TN, Hansson M, Stahl S, Bachi T, Robert A, Domzig W, Binz H, Uhlen M. 1993. Cell-surface display of heterologous epitopes on Staphylococcus xylosus as a potential delivery system for oral vaccination. Gene 128:89-94.
    • (1993) Gene , vol.128 , pp. 89-94
    • Nguyen, T.N.1    Hansson, M.2    Stahl, S.3    Bachi, T.4    Robert, A.5    Domzig, W.6    Binz, H.7    Uhlen, M.8
  • 23
    • 0040883218 scopus 로고
    • Expression of immunogenic epitopes of hepatitis B surface antigen with hybrid flagellin proteins by a vaccine strain of Salmonella
    • Wu JY, Newton S, Judd A, Stocker B, Robinson WS. 1989. Expression of immunogenic epitopes of hepatitis B surface antigen with hybrid flagellin proteins by a vaccine strain of Salmonella. Proc Natl Acad Sci USA 86:4726-4730.
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 4726-4730
    • Wu, J.Y.1    Newton, S.2    Judd, A.3    Stocker, B.4    Robinson, W.S.5
  • 24
    • 0024558027 scopus 로고
    • Immune response to cholera toxin epitope inserted in Salmonella flagellin
    • Newton SM, Jacob CO, Stocker BA. 1989. Immune response 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.O.2    Stocker, B.A.3
  • 25
    • 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, Kupper HA, Amann 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    Kupper, H.A.4    Amann, E.5
  • 26
    • 0030561058 scopus 로고    scopus 로고
    • Gram-positive commensal bacteria for mucosal vaccine delivery
    • Fischetti VA, Medaglini D, Pozzi G. 1996. Gram-positive commensal bacteria for mucosal vaccine delivery. Curr Opin Biotechnol 7:659-666.
    • (1996) Curr Opin Biotechnol , vol.7 , pp. 659-666
    • Fischetti, V.A.1    Medaglini, D.2    Pozzi, G.3
  • 28
    • 37349047429 scopus 로고    scopus 로고
    • The autodisplay story, from discovery to biotechnical and biomedical applications
    • Jose J, Meyer TF. 2007. The autodisplay story, from discovery to biotechnical and biomedical applications. Microbiol Mol Biol Rev 71: 600-619.
    • (2007) Microbiol Mol Biol Rev , vol.71 , pp. 600-619
    • Jose, J.1    Meyer, T.F.2
  • 29
    • 0031034089 scopus 로고    scopus 로고
    • Autodisplay: one-component system for efficient surface display and release of soluble recombinant proteins in Escherichia coli
    • Maurer J, Jose J, Meyer TF. 1997. Autodisplay: one-component system for efficient surface display and release of soluble recombinant proteins in Escherichia coli. J Bacteriol 179:794-804.
    • (1997) J Bacteriol , vol.179 , pp. 794-804
    • Maurer, J.1    Jose, J.2    Meyer, T.F.3
  • 30
    • 34547640042 scopus 로고    scopus 로고
    • Structure, assembly and function of the spore surface layers
    • Henriques AO, Moran CP, Jr. 2007. Structure, assembly and function of the spore surface layers. Annu Rev Microbiol 61:555-588.
    • (2007) Annu Rev Microbiol , vol.61 , pp. 555-588
    • Henriques, A.O.1    Moran, C.P.2
  • 31
    • 30444457865 scopus 로고    scopus 로고
    • The Bacillus subtilis spore coat provides "eat resistance" during phagocytic predation by the protozoan Tetrahymena thermophila
    • Klobutcher LA, Ragkousi K, Setlow P. 2006. The Bacillus subtilis spore coat provides "eat resistance" during phagocytic predation by the protozoan Tetrahymena thermophila. Proc Natl Acad. Sci USA 103: 165-170.
    • (2006) Proc Natl Acad. Sci USA , vol.103 , pp. 165-170
    • Klobutcher, L.A.1    Ragkousi, K.2    Setlow, P.3
  • 37
    • 6444242391 scopus 로고    scopus 로고
    • GerE-independent expression of cotH leads to CotC accumulation in the mother cell compartment during Bacillus subtilis sporulation
    • Baccigalupi L, Castaldo G, Cangiano G, Isticato R, Marasco R, De Felice M, Ricca E. 2004. GerE-independent expression of cotH leads to CotC accumulation in the mother cell compartment during Bacillus subtilis sporulation. Microbiol UK 150:3441-3449.
    • (2004) Microbiol UK , vol.150 , pp. 3441-3449
    • Baccigalupi, L.1    Castaldo, G.2    Cangiano, G.3    Isticato, R.4    Marasco, R.5    De Felice, M.6    Ricca, E.7
  • 38
    • 0017351406 scopus 로고
    • Structure of tetanus toxin. I. Breakdown of the toxin molecule and discrimination between polypeptide fragments
    • Helting TB, Zwisler O. 1977. Structure of tetanus toxin. I. Breakdown of the toxin molecule and discrimination between polypeptide fragments. J Biol Chem 252:194-198.
    • (1977) J Biol Chem , vol.252 , pp. 194-198
    • Helting, T.B.1    Zwisler, O.2
  • 40
    • 0242575014 scopus 로고    scopus 로고
    • Localization of the vegetative cell wall hydrolases LytC, LytE, and LytF on the Bacillus subtilis cell wall surface and stability of these enzymes to cell wall-bound or extracellular proteases
    • Yamamoto H, Kurosawa S-I, Sekigushi J. 2003. Localization of the vegetative cell wall hydrolases LytC, LytE, and LytF on the Bacillus subtilis cell wall surface and stability of these enzymes to cell wall-bound or extracellular proteases. J Bacteriol 22:6666-6677.
    • (2003) J Bacteriol , vol.22 , pp. 6666-6677
    • Yamamoto, H.1    Kurosawa, S.-I.2    Sekigushi, J.3
  • 42
    • 4944234023 scopus 로고    scopus 로고
    • Oral priming of mice by recombinant spores of Bacillus subtilis
    • Ciabattini A, Parigi R, Isticato R, Oggioni MR, Pozzi G. 2004. Oral priming of mice by recombinant spores of Bacillus subtilis. Vaccine 22: 4139-4143.
    • (2004) Vaccine , vol.22 , pp. 4139-4143
    • Ciabattini, A.1    Parigi, R.2    Isticato, R.3    Oggioni, M.R.4    Pozzi, G.5
  • 43
    • 33845299870 scopus 로고    scopus 로고
    • Germination-independent induction of cellular immune response by Bacillus subtilis spores displaying the C fragment of the tetanus toxin
    • Mauriello EMF, Cangiano G, Maurano F, Saggese V, De Felice M, Rossi M, Ricca E. 2007. Germination-independent induction of cellular immune response by Bacillus subtilis spores displaying the C fragment of the tetanus toxin. Vaccine 25:788-793.
    • (2007) Vaccine , vol.25 , pp. 788-793
    • Mauriello, E.M.F.1    Cangiano, G.2    Maurano, F.3    Saggese, V.4    De Felice, M.5    Rossi, M.6    Ricca, E.7
  • 45
    • 55849098531 scopus 로고    scopus 로고
    • Recombinant Bacillus subtilis expressing the Clostridium perfringens alpha toxoid is a candidate orally delivered vaccine against necrotic enteritis
    • Hoang TH, Hong HA, Clark GC, Titball RW, Cutting SM. 2008. Recombinant Bacillus subtilis expressing the Clostridium perfringens alpha toxoid is a candidate orally delivered vaccine against necrotic enteritis. Infect Immun 76:5257-5265.
    • (2008) Infect Immun , vol.76 , pp. 5257-5265
    • Hoang, T.H.1    Hong, H.A.2    Clark, G.C.3    Titball, R.W.4    Cutting, S.M.5
  • 48
    • 81255137015 scopus 로고    scopus 로고
    • Surface-displayed VP28 on Bacillus subtilis spores induces protection against white spot syndrome virus in crayfish by oral administration
    • Ning D, Leng X, Li Q, Xu W. 2011. Surface-displayed VP28 on Bacillus subtilis spores induces protection against white spot syndrome virus in crayfish by oral administration. J Appl Microbiol 111:1327-1336.
    • (2011) J Appl Microbiol , vol.111 , pp. 1327-1336
    • Ning, D.1    Leng, X.2    Li, Q.3    Xu, W.4
  • 50
    • 0023645130 scopus 로고
    • Genes encoding spore coat polypeptides from Bacillus subtilis
    • Donovan W, Zheng L, Sandman K, Losick R. 1987. Genes encoding spore coat polypeptides from Bacillus subtilis. J Mol Biol 196:1-10.
    • (1987) J Mol Biol , vol.196 , pp. 1-10
    • Donovan, W.1    Zheng, L.2    Sandman, K.3    Losick, R.4
  • 51
    • 0024058980 scopus 로고
    • Gene encoding a morphogenic protein required in the assembly of the outer coat of the Bacillus subtilis endospore
    • Zheng L, Donovan WP, Fitz-James PC, Losick R. 1988. Gene encoding a morphogenic protein required in the assembly of the outer coat of the Bacillus subtilis endospore. Genes Dev 2:1047-1054.
    • (1988) Genes Dev , vol.2 , pp. 1047-1054
    • Zheng, L.1    Donovan, W.P.2    Fitz-James, P.C.3    Losick, R.4
  • 53
    • 75749150148 scopus 로고    scopus 로고
    • CotE binds to CotC and CotU and mediates their interaction during spore coat formation in Bacillus subtilis
    • Isticato R, Pelosi A, De Felice M, Ricca E. 2010. CotE binds to CotC and CotU and mediates their interaction during spore coat formation in Bacillus subtilis. J Bacteriol 192:949-954.
    • (2010) J Bacteriol , vol.192 , pp. 949-954
    • Isticato, R.1    Pelosi, A.2    De Felice, M.3    Ricca, E.4
  • 54
    • 34247552787 scopus 로고    scopus 로고
    • Amino terminal fusion of heterologous proteins to CotC increases display efficiencies in the Bacillus subtilis spore system
    • Isticato R, Scotto Di Mase D, Mauriello EMF, De Felice M, Ricca E. 2007. Amino terminal fusion of heterologous proteins to CotC increases display efficiencies in the Bacillus subtilis spore system. BioTechniques 42:151-156.
    • (2007) BioTechniques , vol.42 , pp. 151-156
    • Isticato, R.1    Scotto Di Mase, D.2    Mauriello, E.M.F.3    De Felice, M.4    Ricca, E.5
  • 55
    • 84864631558 scopus 로고    scopus 로고
    • Surface display of human serum albumin on Bacillus subtilis spores for oral administration
    • Mao L, Jiang S, Li G, He Y, Chen L, Yao Q, Chen K. 2012. Surface display of human serum albumin on Bacillus subtilis spores for oral administration. Curr Microbiol 64:545-551.
    • (2012) Curr Microbiol , vol.64 , pp. 545-551
    • Mao, L.1    Jiang, S.2    Li, G.3    He, Y.4    Chen, L.5    Yao, Q.6    Chen, K.7
  • 57
    • 40849099909 scopus 로고    scopus 로고
    • Oral administration of a Bacillus subtilis spore-based vaccine expressing Clonorchis sinensis tegumental protein 22.3 kDa confers protection against Clonorchis sinensis
    • Zhou Z, Xia H, Hu X, Huang Y, Li Y, Li L, Ma C, Chen X, Hu F, Xu J, Lu F, Wu Z, Yu X. 2008. Oral administration of a Bacillus subtilis spore-based vaccine expressing Clonorchis sinensis tegumental protein 22.3 kDa confers protection against Clonorchis sinensis. Vaccine 26: 1817-1825.
    • (2008) Vaccine , vol.26 , pp. 1817-1825
    • Zhou, Z.1    Xia, H.2    Hu, X.3    Huang, Y.4    Li, Y.5    Li, L.6    Ma, C.7    Chen, X.8    Hu, F.9    Xu, J.10    Lu, F.11    Wu, Z.12    Yu, X.13
  • 58
    • 79954417524 scopus 로고    scopus 로고
    • Display of Bombyx mori nucleopolyhedrovirus GP64 on the Bacillus subtilis spore coat
    • Li G, Tang Q, Chen H, Yao Q, Ning D, Chen K. 2011. Display of Bombyx mori nucleopolyhedrovirus GP64 on the Bacillus subtilis spore coat. Curr Microbiol 62:1368-1373.
    • (2011) Curr Microbiol , vol.62 , pp. 1368-1373
    • Li, G.1    Tang, Q.2    Chen, H.3    Yao, Q.4    Ning, D.5    Chen, K.6
  • 59
    • 79959680748 scopus 로고    scopus 로고
    • Display of Bombyx mori alcohol dehydrogenases on the Bacillus subtilis spore surface to enhance enzymatic activity under adverse conditions
    • Wang N, Chang C, Yao Q, Li G, Qin L, Chen L, Chen K. 2011. Display of Bombyx mori alcohol dehydrogenases on the Bacillus subtilis spore surface to enhance enzymatic activity under adverse conditions. PLoS ONE 6:e21454. doi:10.1371/journal.pone.0021454.
    • (2011) PLoS ONE , vol.6
    • Wang, N.1    Chang, C.2    Yao, Q.3    Li, G.4    Qin, L.5    Chen, L.6    Chen, K.7
  • 60
    • 0028851012 scopus 로고
    • An additional GerEcontrolled gene encoding an abundant spore coat protein from Bacillus subtilis
    • Sacco M, Ricca E, Losick R, Cutting S. 1995. An additional GerEcontrolled gene encoding an abundant spore coat protein from Bacillus subtilis. J Bacteriol 177:372-377.
    • (1995) J Bacteriol , vol.177 , pp. 372-377
    • Sacco, M.1    Ricca, E.2    Losick, R.3    Cutting, S.4
  • 62
    • 0031955996 scopus 로고    scopus 로고
    • Involvement of superoxide dismutase in spore coat assembly in Bacillus subtilis
    • Henriques AO, Melsen LR, Moran CP. 1998. Involvement of superoxide dismutase in spore coat assembly in Bacillus subtilis. J Bacteriol 180:2285-2291.
    • (1998) J Bacteriol , vol.180 , pp. 2285-2291
    • Henriques, A.O.1    Melsen, L.R.2    Moran, C.P.3
  • 64
    • 17444367302 scopus 로고    scopus 로고
    • Spore-displayed streptavidin: a live diagnostic tool in biotechnology
    • Kim J-H, Lee C-S, Kim B-G. 2005. Spore-displayed streptavidin: a live diagnostic tool in biotechnology. Biochem Biophys Res Commun 331:210-214.
    • (2005) Biochem Biophys Res Commun , vol.331 , pp. 210-214
    • Kim, J.-H.1    Lee, C.-S.2    Kim, B.-G.3
  • 66
    • 80053161551 scopus 로고    scopus 로고
    • Bacterial surface display of a co-factor containing enzyme ?-transaminase from Vibrio fluvialis using Bacillus subtilis spore display system
    • Hwang B-Y, Kim B-G, Kim J-H. 2011. Bacterial surface display of a co-factor containing enzyme ?-transaminase from Vibrio fluvialis using Bacillus subtilis spore display system. Biosci Biotechnol Biochem 75: 1862-1865.
    • (2011) Biosci Biotechnol Biochem , vol.75 , pp. 1862-1865
    • Hwang, B.-Y.1    Kim, B.-G.2    Kim, J.-H.3
  • 67
    • 79958190243 scopus 로고    scopus 로고
    • Production of N-acetyl-D-neuraminic acid by use of an efficient spore surface display system
    • Xu X, Gao C, Zhang X, Che B, Ma C, Qiu J, Tao F, Xu P. 2011. Production of N-acetyl-D-neuraminic acid by use of an efficient spore surface display system. Appl Environ Microbiol 77:3197-3201.
    • (2011) Appl Environ Microbiol , vol.77 , pp. 3197-3201
    • Xu, X.1    Gao, C.2    Zhang, X.3    Che, B.4    Ma, C.5    Qiu, J.6    Tao, F.7    Xu, P.8
  • 68
    • 34247495517 scopus 로고    scopus 로고
    • Transgalactosylation in a watersolvent biphasic reaction system with β-galactosidase displayed on the surfaces of Bacillus subtilis spores
    • Kwon SJ, Jung H-C, Pan J-G. 2007. Transgalactosylation in a watersolvent biphasic reaction system with β-galactosidase displayed on the surfaces of Bacillus subtilis spores. Appl Environ Microbiol 73:2251-2256.
    • (2007) Appl Environ Microbiol , vol.73 , pp. 2251-2256
    • Kwon, S.J.1    Jung, H.-C.2    Pan, J.-G.3
  • 69
    • 77956598900 scopus 로고    scopus 로고
    • Display of recombinant proteins on Bacillus subtilis spores using a coat-associated enzyme as the carrier
    • Potot S, Serra CR, Henriques AO, Schyns G. 2010. Display of recombinant proteins on Bacillus subtilis spores using a coat-associated enzyme as the carrier. Appl Environ Microbiol 76:5926-5933.
    • (2010) Appl Environ Microbiol , vol.76 , pp. 5926-5933
    • Potot, S.1    Serra, C.R.2    Henriques, A.O.3    Schyns, G.4
  • 70
    • 0035941286 scopus 로고    scopus 로고
    • Oxalate decarboxylase requires manganese and dioxygen for activity: over-expression and characterization of Bacillus subtilis YvrK and YoaN
    • Tanner A, Bowater L, Fairhurst A, Bornemann S. 2001. Oxalate decarboxylase requires manganese and dioxygen for activity: over-expression and characterization of Bacillus subtilis YvrK and YoaN. J Biol Chem 276:43627-43634.
    • (2001) J Biol Chem , vol.276 , pp. 43627-43634
    • Tanner, A.1    Bowater, L.2    Fairhurst, A.3    Bornemann, S.4
  • 71
    • 1342304139 scopus 로고    scopus 로고
    • Assembly of an oxalate decaroxylase produced under the sigma k control into the Bacillus subtilis spore coat
    • Costa T, Steil L, Martins LO, Volker U, Henriques AO. 2004. Assembly of an oxalate decaroxylase produced under the sigma k control into the Bacillus subtilis spore coat. J Bacteriol 186:1462-1474.
    • (2004) J Bacteriol , vol.186 , pp. 1462-1474
    • Costa, T.1    Steil, L.2    Martins, L.O.3    Volker, U.4    Henriques, A.O.5
  • 72
    • 0035025713 scopus 로고    scopus 로고
    • SpoVID guides SafA to the spore coat in Bacillus subtilis
    • Ozin AJ, Samford CS, Henriques AO, Moran CP. 2001. SpoVID guides SafA to the spore coat in Bacillus subtilis. J Bacteriol 183:3041-3049.
    • (2001) J Bacteriol , vol.183 , pp. 3041-3049
    • Ozin, A.J.1    Samford, C.S.2    Henriques, A.O.3    Moran, C.P.4
  • 75
    • 84870256513 scopus 로고    scopus 로고
    • Global probabilistic annotation of metabolic networks enables enzyme discovery
    • Plata G, Fuhrer T, Hsiao T-L, Sauer U, Viktup D. 2012. Global probabilistic annotation of metabolic networks enables enzyme discovery. Nat Chem Biol 8:848-854.
    • (2012) Nat Chem Biol , vol.8 , pp. 848-854
    • Plata, G.1    Fuhrer, T.2    Hsiao, T.-L.3    Sauer, U.4    Viktup, D.5
  • 78
    • 0037166265 scopus 로고    scopus 로고
    • Molecular and biochemical characterization of a highly stable bacterial laccase that occurs as a structural component of the Bacillus subtilis endospore coat
    • Martins LO, Soares CM, Pereira MM, Teixeira M, Costa T, Jones GH, Henriques AO. 2002. Molecular and biochemical characterization of a highly stable bacterial laccase that occurs as a structural component of the Bacillus subtilis endospore coat. J Biol Chem 277:1849-1859.
    • (2002) J Biol Chem , vol.277 , pp. 1849-1859
    • Martins, L.O.1    Soares, C.M.2    Pereira, M.M.3    Teixeira, M.4    Costa, T.5    Jones, G.H.6    Henriques, A.O.7
  • 79
    • 77954994517 scopus 로고    scopus 로고
    • Directed evolution of CotA laccase for increased substrate specificity using Bacillus subtilis spores
    • Gupta N, Farinas ET. 2010. Directed evolution of CotA laccase for increased substrate specificity using Bacillus subtilis spores. Protein Eng Des Sel 23:679-682.
    • (2010) Protein Eng Des Sel , vol.23 , pp. 679-682
    • Gupta, N.1    Farinas, E.T.2
  • 80
    • 0029758940 scopus 로고    scopus 로고
    • Bacillus thuringiensis HD-73 spores have surface-localized Cry1Ac toxin: physiological and pathogenic consequences
    • Du C, Nickerson KW. 1996. Bacillus thuringiensis HD-73 spores have surface-localized Cry1Ac toxin: physiological and pathogenic consequences. Appl Environ Microbiol 62:3722-3726.
    • (1996) Appl Environ Microbiol , vol.62 , pp. 3722-3726
    • Du, C.1    Nickerson, K.W.2
  • 81
    • 20444396112 scopus 로고    scopus 로고
    • Surface display of recombinant proteins on Bacillus thuringiensis spores
    • Du C, Chan WC, McKeithan W, Nickerson KW. 2005. Surface display of recombinant proteins on Bacillus thuringiensis spores. Appl Environ Microbiol 71:3337-3341.
    • (2005) Appl Environ Microbiol , vol.71 , pp. 3337-3341
    • Du, C.1    Chan, W.C.2    McKeithan, W.3    Nickerson, K.W.4
  • 83
    • 52649144340 scopus 로고    scopus 로고
    • Targeting of the BclA and BclB proteins to the Bacillus anthracis spore surface
    • Thompson BM, Stewart GC. 2008. Targeting of the BclA and BclB proteins to the Bacillus anthracis spore surface. Mol Microbiol 70: 421-434.
    • (2008) Mol Microbiol , vol.70 , pp. 421-434
    • Thompson, B.M.1    Stewart, G.C.2
  • 84
    • 33847175919 scopus 로고    scopus 로고
    • Live bacterial vaccines-a review and identification of potential hazards
    • Detmer A, Glenting J. 2006. Live bacterial vaccines-a review and identification of potential hazards. Microb Cell Fact 5:23. doi:10.1186/1475-2859-5-23.
    • (2006) Microb Cell Fact , vol.5 , pp. 23
    • Detmer, A.1    Glenting, J.2
  • 85
    • 84954358368 scopus 로고    scopus 로고
    • Functional expression in Bacillus subtilis of mammalian NADPH-cytochrome P450 oxidoreductase and its spore-display
    • Yim S-K, Jung H-C, Yun C-H, PanJ-G. 2009. Functional expression in Bacillus subtilis of mammalian NADPH-cytochrome P450 oxidoreductase and its spore-display. Protein Expr Purif 63:5-11.
    • (2009) Protein Expr Purif , vol.63 , pp. 5-11
    • Yim, S.-K.1    Jung, H.-C.2    Yun, C.-H.3    Pan, J.-G.4
  • 86
    • 70449359790 scopus 로고    scopus 로고
    • Surface display of heterologous proteins in Bacillus thuringiensis using a peptidoglycan hydrolase anchor
    • Shao X, Jiang M, Yu Z, Cai H, Li L. 2009. Surface display of heterologous proteins in Bacillus thuringiensis using a peptidoglycan hydrolase anchor Microb Cell Fact 8:48. doi:10.1186/1475-2859-8-48.
    • (2009) Microb Cell Fact , vol.8 , pp. 48
    • Shao, X.1    Jiang, M.2    Yu, Z.3    Cai, H.4    Li, L.5
  • 87
    • 80051547339 scopus 로고    scopus 로고
    • In vivo and in vitro surface display of heterologous proteins on Bacillus thuringiensis vegetative cells and spores
    • Jiang M, Shao X, Ni H, Yu Z, Li L. 2011. In vivo and in vitro surface display of heterologous proteins on Bacillus thuringiensis vegetative cells and spores. Process Biochem. 46:1861-1866.
    • (2011) Process Biochem , vol.46 , pp. 1861-1866
    • Jiang, M.1    Shao, X.2    Ni, H.3    Yu, Z.4    Li, L.5
  • 89
    • 0027434814 scopus 로고
    • Biochemical properties of cloned glutathione S-transferases from Schistosoma mansoni and Schistosoma japonicum
    • Walker J, Crowley P, Moreman AD, Barrett J. 1993. Biochemical properties of cloned glutathione S-transferases from Schistosoma mansoni and Schistosoma japonicum. Mol Biochem Parasitol 61:255-264.
    • (1993) Mol Biochem Parasitol , vol.61 , pp. 255-264
    • Walker, J.1    Crowley, P.2    Moreman, A.D.3    Barrett, J.4
  • 90
    • 79957549505 scopus 로고    scopus 로고
    • Adsorption immobilization of Escherichia coli phytase on probiotic Bacillus polyfermenticus spores
    • Cho EA, Kim EJ, Pan JG. 2011. Adsorption immobilization of Escherichia coli phytase on probiotic Bacillus polyfermenticus spores. Enzyme Microb Technol 49:66-71.
    • (2011) Enzyme Microb Technol , vol.49 , pp. 66-71
    • Cho, E.A.1    Kim, E.J.2    Pan, J.G.3
  • 91
    • 84864502255 scopus 로고    scopus 로고
    • Adsorption of β-galactosidase of Alicyclobacillus acidocaldaricus on wild type and mutant spores of Bacillus subtilis
    • Sirec T, Strazzulli A, Isticato R, De Felice M, Moracci M, Ricca E. 2012. Adsorption of β-galactosidase of Alicyclobacillus acidocaldaricus on wild type and mutant spores of Bacillus subtilis. Microb Cell Fact 11:100. doi:10.1186/1475-2859-11-100.
    • (2012) Microb Cell Fact , vol.11 , pp. 100
    • Sirec, T.1    Strazzulli, A.2    Isticato, R.3    De Felice, M.4    Moracci, M.5    Ricca, E.6
  • 93
    • 39849099527 scopus 로고    scopus 로고
    • Physicochemical characterization of natural ionic microreservoirs: Bacillus subtilis dormant spores
    • Kazakov S, Bonvouloir E, Gazaryan I. 2008. Physicochemical characterization of natural ionic microreservoirs: Bacillus subtilis dormant spores. J Phys Chem 112:2233-2244.
    • (2008) J Phys Chem , vol.112 , pp. 2233-2244
    • Kazakov, S.1    Bonvouloir, E.2    Gazaryan, I.3
  • 94
  • 95
    • 84896707199 scopus 로고    scopus 로고
    • Surface charge and hydrodynamic coefficient measurements of Bacillus subtilis spore by optical tweezers
    • Pesce G, Rusciano G, Sasso A, Isticato R, Sirec T, Ricca E. 2014. Surface charge and hydrodynamic coefficient measurements of Bacillus subtilis spore by optical tweezers. Colloids Surf B Biointerfaces 116:568-575.
    • (2014) Colloids Surf B Biointerfaces , vol.116 , pp. 568-575
    • Pesce, G.1    Rusciano, G.2    Sasso, A.3    Isticato, R.4    Sirec, T.5    Ricca, E.6
  • 97
    • 79955557064 scopus 로고    scopus 로고
    • Bacterial spores as platforms for bioanalytical and biomedical applications
    • Knecht LD, Pasini P, Daunert S. 2011. Bacterial spores as platforms for bioanalytical and biomedical applications. Anal Bioanal Chem 400:977-989.
    • (2011) Anal Bioanal Chem , vol.400 , pp. 977-989
    • Knecht, L.D.1    Pasini, P.2    Daunert, S.3
  • 98
    • 79551719109 scopus 로고    scopus 로고
    • Bacillus probiotics
    • Cutting SM. 2011. Bacillus probiotics. Food Microbiol 28:214-220.
    • (2011) Food Microbiol , vol.28 , pp. 214-220
    • Cutting, S.M.1
  • 100
    • 84886393475 scopus 로고    scopus 로고
    • Non-recombinant display of the B subunit of the heat labile toxin of Escherichia coli on wild type and mutant spores of Bacillus subtilis
    • Isticato R, Sirec T, Treppiccione L, Maurano F, De Felice M, Rossi M, Ricca E. 2013. Non-recombinant display of the B subunit of the heat labile toxin of Escherichia coli on wild type and mutant spores of Bacillus subtilis. Microb Cell Fact 12:98. doi:10.1186/1475-2859-12-98.
    • (2013) Microb Cell Fact , vol.12 , pp. 98
    • Isticato, R.1    Sirec, T.2    Treppiccione, L.3    Maurano, F.4    De Felice, M.5    Rossi, M.6    Ricca, E.7
  • 101
    • 4344718438 scopus 로고    scopus 로고
    • Transglutaminase-mediated crosslinking of GerQ in the coats of Bacillus subtilis spores
    • Ragkousi K, Setlow P. 2004. Transglutaminase-mediated crosslinking of GerQ in the coats of Bacillus subtilis spores. J Bacteriol 186:5567-5575.
    • (2004) J Bacteriol , vol.186 , pp. 5567-5575
    • Ragkousi, K.1    Setlow, P.2
  • 103
    • 0030297463 scopus 로고    scopus 로고
    • e-(?-glutamyl)Lysine crosslinks of spore coat proteins and transglutaminase activity in Bacillus subtilis
    • Kobayashi K, Kumazawa Y, Miwa K, Yamanaka S. 1996. e-(?-glutamyl)Lysine crosslinks of spore coat proteins and transglutaminase activity in Bacillus subtilis. FEMS Microbiol Lett 144:157-160.
    • (1996) FEMS Microbiol Lett , vol.144 , pp. 157-160
    • Kobayashi, K.1    Kumazawa, Y.2    Miwa, K.3    Yamanaka, S.4
  • 105
    • 79961160010 scopus 로고    scopus 로고
    • Proteins involved in formation of the outermost layer of Bacillus subtilis spores
    • Imamura D, Kuwana R, Takamatsu H, Watabe K. 2011. Proteins involved in formation of the outermost layer of Bacillus subtilis spores. J Bacteriol 193:4075-4080.
    • (2011) J Bacteriol , vol.193 , pp. 4075-4080
    • Imamura, D.1    Kuwana, R.2    Takamatsu, H.3    Watabe, K.4
  • 106
    • 84874365109 scopus 로고    scopus 로고
    • New stable anchor protein and peptide linker suitable for successful spore surface display in B. subtilis
    • Hinc K, Iwanicki A, Obuchowski M. 2013. New stable anchor protein and peptide linker suitable for successful spore surface display in B. subtilis. Microb Cell Fact 12:22. doi:10.1186/1475-2859-12-22.
    • (2013) Microb Cell Fact , vol.12 , pp. 22
    • Hinc, K.1    Iwanicki, A.2    Obuchowski, M.3
  • 107
    • 84881581101 scopus 로고    scopus 로고
    • Expression and display of Clostridium difficile protein FliD on the surface of Bacillus subtilis spores
    • Negri A, Potocki W, Iwanicki A, Obuchowski M, Hinc K. 2013. Expression and display of Clostridium difficile protein FliD on the surface of Bacillus subtilis spores. J Med Microbiol 62:1379-1385.
    • (2013) J Med Microbiol , vol.62 , pp. 1379-1385
    • Negri, A.1    Potocki, W.2    Iwanicki, A.3    Obuchowski, M.4    Hinc, K.5
  • 109
    • 84893713642 scopus 로고    scopus 로고
    • Bacillus spores as building blocks for stimuli-responsive materials and nanogenerators
    • Chen X, Mahadevan L, Driks A, Sahin O. 2014. Bacillus spores as building blocks for stimuli-responsive materials and nanogenerators. Nat Nanotechnol 9:137-141.
    • (2014) Nat Nanotechnol , vol.9 , pp. 137-141
    • Chen, X.1    Mahadevan, L.2    Driks, A.3    Sahin, O.4


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