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Volumn 85, Issue 2, 2004, Pages 214-221

Functional Display of Foreign Protein on Surface of Escherichia coli Using N-Terminal Domain of Ice Nucleation Protein

Author keywords

Cell surface display; Escherichia coli; Green fluorescent protein; Ice nucleation protein; N terminal domain; Organophosphorus hydrolase

Indexed keywords

BIOTECHNOLOGY; CELLS; ESCHERICHIA COLI; NUCLEATION; SURFACE CHEMISTRY;

EID: 0942297855     PISSN: 00063592     EISSN: None     Source Type: Journal    
DOI: 10.1002/bit.10892     Document Type: Article
Times cited : (118)

References (33)
  • 1
    • 0019892005 scopus 로고
    • Renaturation of Aequorea green fluorescent protein
    • Bokman SH, Ward WW. 1981. Renaturation of Aequorea green fluorescent protein. Biochem Biophys Res Commun 101:1372-1380.
    • (1981) Biochem Biophys Res Commun , vol.101 , pp. 1372-1380
    • Bokman, S.H.1    Ward, W.W.2
  • 2
    • 0025836538 scopus 로고
    • Limits of diffusion in the hydrolysis of substrates by the phophotriesterase from Pseudomonas diminuta
    • Caldwell SR, Newcomb JR, Schlecht KA, Raushel FM. 1991. Limits of diffusion in the hydrolysis of substrates by the phophotriesterase from Pseudomonas diminuta. Biochemistry 30:7438-7444.
    • (1991) Biochemistry , vol.30 , pp. 7438-7444
    • Caldwell, S.R.1    Newcomb, J.R.2    Schlecht, K.A.3    Raushel, F.M.4
  • 3
    • 0001154861 scopus 로고    scopus 로고
    • Observations of green fluorescent protein as a fusion partner in genetically engineered Escherichia coli: Monitoring protein expression and solubility
    • Cha HJ, Wu CF, Valdes JJ, Rao G, Bentley WE. 2000. Observations of green fluorescent protein as a fusion partner in genetically engineered Escherichia coli: monitoring protein expression and solubility. Biotechnol Bioeng 67:565-574.
    • (2000) Biotechnol Bioeng , vol.67 , pp. 565-574
    • Cha, H.J.1    Wu, C.F.2    Valdes, J.J.3    Rao, G.4    Bentley, W.E.5
  • 5
    • 0033848415 scopus 로고    scopus 로고
    • Ice crystallization by Pseudomonas syringae
    • Cochet N, Widehem O. 2000. Ice crystallization by Pseudomonas syringae. Appl Microbiol Biotechnol 54:153-161.
    • (2000) Appl Microbiol Biotechnol , vol.54 , pp. 153-161
    • Cochet, N.1    Widehem, O.2
  • 6
    • 0024340489 scopus 로고
    • Structure-activity relationship in the hydrolysis of substrates by the phosphotriesterase from Pseudomonas diminuta
    • Donarski WJ, Dumas DP, Heitmeyer DP, Lewis VE, Raushel FM. 1989. Structure-activity relationship in the hydrolysis of substrates by the phosphotriesterase from Pseudomonas diminuta. Biochemistry 28:4650-4655.
    • (1989) Biochemistry , vol.28 , pp. 4650-4655
    • Donarski, W.J.1    Dumas, D.P.2    Heitmeyer, D.P.3    Lewis, V.E.4    Raushel, F.M.5
  • 7
    • 0027425230 scopus 로고
    • Production and fluorescence-activated cell sorting of Escherichia coli expressing a functional antibody fragment on the external surface
    • Francisco JA, Campbell R, Iverson BL, 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
  • 8
    • 0031012062 scopus 로고    scopus 로고
    • Display of heterologous proteins on the surface of microorganisms: From the screening of combinatorial libraries to live recombinant vaccines
    • Georgiou G, Stathopoulos C, Daugherty PS, Nayak AR, Iverson BL, Curtiss R. 1997. Display of heterologous proteins on the surface of microorganisms: from the screening of combinatorial libraries to live recombinant vaccines. Nat Biotechnol 15:29-34.
    • (1997) Nat Biotechnol , vol.15 , pp. 29-34
    • Georgiou, G.1    Stathopoulos, C.2    Daugherty, P.S.3    Nayak, A.R.4    Iverson, B.L.5    Curtiss, R.6
  • 9
    • 0030711517 scopus 로고    scopus 로고
    • Organophosphorus hydrolase is a remarkably stable enzyme that unfolds through a homodimeric intermediate
    • Grimsley JK, Scholtz JM, Pace CN, Wild JR. 1997. Organophosphorus hydrolase is a remarkably stable enzyme that unfolds through a homodimeric intermediate. Biochemistry 36:14366-14374.
    • (1997) Biochemistry , vol.36 , pp. 14366-14374
    • Grimsley, J.K.1    Scholtz, J.M.2    Pace, C.N.3    Wild, J.R.4
  • 10
    • 0026719273 scopus 로고
    • Expression of recombinant proteins on the surface of the coagulase-negative bacteria Staphylococcus xylosus
    • Hansson M, Stahl S, Nguyen TN, Bachi T, Robert A, Binz H, Sjolander A, Uhlen M. 1992. Expression of recombinant proteins on the surface of the coagulase-negative bacteria 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    Sjolander, A.7    Uhlen, M.8
  • 11
    • 0031863713 scopus 로고    scopus 로고
    • Surface display of Zymomonas mobilis levansucrase by using the ice-nucleation protein of Pseudomonas syringae
    • Jung HC, Lebeault CM, Pan JG. 1998a. Surface display of Zymomonas mobilis levansucrase by using the ice-nucleation protein of Pseudomonas syringae. Nat Biotechnol 16:576-580.
    • (1998) Nat Biotechnol , vol.16 , pp. 576-580
    • Jung, H.C.1    Lebeault, C.M.2    Pan, J.G.3
  • 12
    • 0032055018 scopus 로고    scopus 로고
    • Expression of carboxymethyl cellulase on the surface of Escherichia coli using Pseudomonas syringae ice nucleation protein
    • Jung HC, Park JH, Park SH, Lebeault CM, Pan JG. 1998b. Expression of carboxymethyl cellulase on the surface of Escherichia coli using Pseudomonas syringae ice nucleation protein. Enzyme Microb Technol 22:348-354.
    • (1998) Enzyme Microb Technol , vol.22 , pp. 348-354
    • Jung, H.C.1    Park, J.H.2    Park, S.H.3    Lebeault, C.M.4    Pan, J.G.5
  • 13
    • 0036038422 scopus 로고    scopus 로고
    • Comparison of green fluorescent protein expression in two industrial Escherichia coli strains, BL21 and W3110, under co-expression of bacterial hemoglobin
    • Kang DG, Kim YK, Cha HJ. 2002a. Comparison of green fluorescent protein expression in two industrial Escherichia coli strains, BL21 and W3110, under co-expression of bacterial hemoglobin. Appl Microbiol Biotechnol 59:523-528.
    • (2002) Appl Microbiol Biotechnol , vol.59 , pp. 523-528
    • Kang, D.G.1    Kim, Y.K.2    Cha, H.J.3
  • 14
    • 0036276694 scopus 로고    scopus 로고
    • Enhanced detoxification of organophosphates using recombinant Escherichia coli with co-expression of organophosphorus hydrolase and bacterial hemoglobin
    • Kang DG, Kim JYH, Cha HJ. 2002b. Enhanced detoxification of organophosphates using recombinant Escherichia coli with co-expression of organophosphorus hydrolase and bacterial hemoglobin. Biotechnol Lett 24:879-883.
    • (2002) Biotechnol Lett , vol.24 , pp. 879-883
    • Kang, D.G.1    Kim, J.Y.H.2    Cha, H.J.3
  • 15
    • 0025122755 scopus 로고
    • The normally periplasmic 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 MG, Pugsley AP. 1990. The normally periplasmic 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
  • 16
    • 0025952051 scopus 로고
    • Formation of bacterial membrane ice-nucleating lipoglycoprotein complexes
    • Kozloff LM, Turner MA, Arellano F. 1991. Formation of bacterial membrane ice-nucleating lipoglycoprotein complexes. J Bacteriol 173:6528-6536.
    • (1991) J Bacteriol , vol.173 , pp. 6528-6536
    • Kozloff, L.M.1    Turner, M.A.2    Arellano, F.3
  • 17
    • 0028933772 scopus 로고
    • Characterization of P-S bond hydrolysis in organophosphorothioate pesticides by organophosphorus hydrolase
    • Lai K, Stolowich NJ, Wild JR. 1995. Characterization of P-S bond hydrolysis in organophosphorothioate pesticides by organophosphorus hydrolase. Arch Biochem Biophys 318:59-64.
    • (1995) Arch Biochem Biophys , vol.318 , pp. 59-64
    • Lai, K.1    Stolowich, N.J.2    Wild, J.R.3
  • 18
    • 0034051330 scopus 로고    scopus 로고
    • Surface-displayed viral antigens on Salmonella carrier vaccine
    • Lee JS, Shin KS, Pan JG, Kim CJ. 2000. Surface-displayed viral antigens on Salmonella carrier vaccine. Nat Biotechnol 18:645-648.
    • (2000) Nat Biotechnol , vol.18 , pp. 645-648
    • Lee, J.S.1    Shin, K.S.2    Pan, J.G.3    Kim, C.J.4
  • 19
    • 0026293775 scopus 로고
    • Principles and biotechnological applications of bacterial ice nucleation
    • Mararitis A, Bassi AS. 1991. Principles and biotechnological applications of bacterial ice nucleation. Crit Rev Biotechnol 11:277-295.
    • (1991) Crit Rev Biotechnol , vol.11 , pp. 277-295
    • Mararitis, A.1    Bassi, A.S.2
  • 20
    • 0347064880 scopus 로고    scopus 로고
    • Selection of cadmium specific hexapeptide and their expression as OmpA fusion proteins in Escherichia coli
    • Mejàre M, Ljung S, Bulow L. 1998. Selection of cadmium specific hexapeptide and their expression as OmpA fusion proteins in Escherichia coli. Protein Eng 11:489-494.
    • (1998) Protein Eng , vol.11 , pp. 489-494
    • Mejàre, M.1    Ljung, S.2    Bulow, L.3
  • 21
    • 0030614718 scopus 로고    scopus 로고
    • The kil gene of the ColE1 plasmid of Escherichia coli controlled by a growth-phase-dependent promoter mediates the secretion of a heterologous periplasmic protein during the stationary phase
    • Miksch G, Fiedler E, Dobrowolski P, Friehs K. 1997. The kil gene of the ColE1 plasmid of Escherichia coli controlled by a growth-phase-dependent promoter mediates the secretion of a heterologous periplasmic protein during the stationary phase. Arch Microbiol 167:143-150.
    • (1997) Arch Microbiol , vol.167 , pp. 143-150
    • Miksch, G.1    Fiedler, E.2    Dobrowolski, P.3    Friehs, K.4
  • 22
    • 0024332036 scopus 로고
    • Parathion hydrolase specified by the Flavobacterium opd gene: Relationship between the gene and protein
    • Mulbry WW, Karns JS. 1989. Parathion hydrolase specified by the Flavobacterium opd gene: relationship between the gene and protein. J Bacteriol 171:6740-6746.
    • (1989) J Bacteriol , vol.171 , pp. 6740-6746
    • Mulbry, W.W.1    Karns, J.S.2
  • 23
    • 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 SMC, Joys TM, Anderson SA, Kennedy RC, Hovi ME, Stocker BAD. 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    Anderson, S.A.3    Kennedy, R.C.4    Hovi, M.E.5    Stocker, B.A.D.6
  • 24
    • 0032133251 scopus 로고    scopus 로고
    • Phospholipid analysis and fractional reconstitution of the ice nucleation protein activity purified from Escherichia coli overexpressing the inaZ gene of Pseudomonas syringae
    • Palaiomylitou MA, Kalimanis A, Koukkou AI, Drainas C, Anastassopoulos E, Panopoulos NJ, Ekateriniadou LV, Kyriakidis DA. 1998. Phospholipid analysis and fractional reconstitution of the ice nucleation protein activity purified from Escherichia coli overexpressing the inaZ gene of Pseudomonas syringae. Cryobiology 37:67-76.
    • (1998) Cryobiology , vol.37 , pp. 67-76
    • Palaiomylitou, M.A.1    Kalimanis, A.2    Koukkou, A.I.3    Drainas, C.4    Anastassopoulos, E.5    Panopoulos, N.J.6    Ekateriniadou, L.V.7    Kyriakidis, D.A.8
  • 25
    • 0030855956 scopus 로고    scopus 로고
    • Biodegradation of organophosphorus pesticides by surface-expressed organophosphorus hydrolase
    • Richins RD, Kaneva I, Mulchandani A, Chen W. 1997. Biodegradation of organophosphorus pesticides by surface-expressed organophosphorus hydrolase. Nat Biotechnol 15:984-987.
    • (1997) Nat Biotechnol , vol.15 , pp. 984-987
    • Richins, R.D.1    Kaneva, I.2    Mulchandani, A.3    Chen, W.4
  • 26
    • 0033532176 scopus 로고    scopus 로고
    • Co-translocation of a periplasmic enzyme complex by a hitchhiker mechanism through the bacterial Tat pathway
    • Rodrigue A, Chanal A, Beck K, Muller M, Wu L. 1999. Co-translocation of a periplasmic enzyme complex by a hitchhiker mechanism through the bacterial Tat pathway. J Biol Chem 274:13223-13228.
    • (1999) J Biol Chem , vol.274 , pp. 13223-13228
    • Rodrigue, A.1    Chanal, A.2    Beck, K.3    Muller, M.4    Wu, L.5
  • 27
    • 0030766938 scopus 로고    scopus 로고
    • Molecular organization of the ice nucleation protein InaV from Pseudomonas syringae
    • Schmid D, Pridmore D, Capitani G, Battistutta R, Neeser JR, Jann A. 1997. Molecular organization of the ice nucleation protein InaV from Pseudomonas syringae. FEBS Lett 414:590-594.
    • (1997) FEBS Lett , vol.414 , pp. 590-594
    • Schmid, D.1    Pridmore, D.2    Capitani, G.3    Battistutta, R.4    Neeser, J.R.5    Jann, A.6
  • 28
    • 0035793148 scopus 로고    scopus 로고
    • Display of green fluorescent protein on Escherichia coli cell surface
    • Shi H, Su WW. 2001. Display of green fluorescent protein on Escherichia coli cell surface. Enzyme Microb Technol 28:25-34.
    • (2001) Enzyme Microb Technol , vol.28 , pp. 25-34
    • Shi, H.1    Su, W.W.2
  • 29
    • 0035125229 scopus 로고    scopus 로고
    • Cell surface display of organophosphorus hydrolase using ice nucleation protein
    • Shimazu M, Mulchandani A, Chen W. 2001a. Cell surface display of organophosphorus hydrolase using ice nucleation protein. Biotechnol Prog 17:76-80.
    • (2001) Biotechnol Prog , vol.17 , pp. 76-80
    • Shimazu, M.1    Mulchandani, A.2    Chen, W.3
  • 30
    • 0035829836 scopus 로고    scopus 로고
    • Simultaneous degradation of organophosphorus pesticides and p-nitrophenol by a genetically engineered Moraxella sp. with surface-expressed organophosphorus hydrolase
    • Shimazu M, Mulchandani A, Chen W. 2001b. Simultaneous degradation of organophosphorus pesticides and p-nitrophenol by a genetically engineered Moraxella sp. with surface-expressed organophosphorus hydrolase. Biotechnol Bioeng 76:318-324.
    • (2001) Biotechnol Bioeng , vol.76 , pp. 318-324
    • Shimazu, M.1    Mulchandani, A.2    Chen, W.3
  • 31
    • 0343145679 scopus 로고    scopus 로고
    • Bacterial and archaeal s-layer proteins: Structure-function relationship and their biotechnological applications
    • Sleytr UB, Sara M. 1997. Bacterial and archaeal s-layer proteins: structure-function relationship and their biotechnological applications. Trends Biotechnol 15:20-26.
    • (1997) Trends Biotechnol , vol.15 , pp. 20-26
    • Sleytr, U.B.1    Sara, M.2
  • 32
    • 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
  • 33
    • 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-funcfion relationships in the TraT protein
    • Taylor IM, Harrison JL, Timmis KN, 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-funcfion relationships 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.