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Volumn 55, Issue 1, 2007, Pages 75-83

Overexpression of the recombinant Enterobacter cloacae P99 AmpC β-lactamase and its mutants based on a φ{symbol}105 prophage system in Bacillus subtilis

Author keywords

AmpC lactamase; Bacillus subtilis; Extracellular expression; Intracellular expression; Thermo induction

Indexed keywords

AMPC BETA LACTAMASES; AMPC BETA-LACTAMASES; BACTERIAL PROTEIN; BETA LACTAMASE; HISTIDINE; RECOMBINANT PROTEIN; UNCLASSIFIED DRUG;

EID: 34547897638     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2007.06.001     Document Type: Article
Times cited : (4)

References (39)
  • 1
    • 0033862706 scopus 로고    scopus 로고
    • β-Lactamases: which ones are clinically important?
    • Rice L.B., and Bonomo R.A. β-Lactamases: which ones are clinically important?. Drug Resist. Updat. 3 (2000) 178-189
    • (2000) Drug Resist. Updat. , vol.3 , pp. 178-189
    • Rice, L.B.1    Bonomo, R.A.2
  • 2
    • 14844362964 scopus 로고    scopus 로고
    • Bacterial resistance to β-lactam antibiotics: compelling opportunism, compelling opportunity
    • Fisher J.F., Meroueh S.O., and Mobashery S. Bacterial resistance to β-lactam antibiotics: compelling opportunism, compelling opportunity. Chem. Rev. 105 (2005) 395-424
    • (2005) Chem. Rev. , vol.105 , pp. 395-424
    • Fisher, J.F.1    Meroueh, S.O.2    Mobashery, S.3
  • 4
    • 0033963352 scopus 로고    scopus 로고
    • β-Lactamase epidemiology and the utility of established and novel β-lactamase inhibitors
    • Payne D.J., Du W., and Bateson J.H. β-Lactamase epidemiology and the utility of established and novel β-lactamase inhibitors. Expert. Opin. Investig. Drugs 9 (2000) 247-261
    • (2000) Expert. Opin. Investig. Drugs , vol.9 , pp. 247-261
    • Payne, D.J.1    Du, W.2    Bateson, J.H.3
  • 5
    • 0027518228 scopus 로고
    • An efficient expression and secretion system based on Bacillus subtilis phage φ{symbol}105 and its use for the production of B. cereus β-lactamase I
    • Thornewell S.J., East A.K., and Errington J. An efficient expression and secretion system based on Bacillus subtilis phage φ{symbol}105 and its use for the production of B. cereus β-lactamase I. Gene 133 (1993) 47-53
    • (1993) Gene , vol.133 , pp. 47-53
    • Thornewell, S.J.1    East, A.K.2    Errington, J.3
  • 6
    • 0028893338 scopus 로고
    • Characterization of an insertion in the phage φ{symbol}105 genome that blocks host Bacillus subtilis lysis and provides strong expression of heterologous genes
    • Leung Y.C., and Errington J. Characterization of an insertion in the phage φ{symbol}105 genome that blocks host Bacillus subtilis lysis and provides strong expression of heterologous genes. Gene 154 (1995) 1-6
    • (1995) Gene , vol.154 , pp. 1-6
    • Leung, Y.C.1    Errington, J.2
  • 7
    • 0141792426 scopus 로고    scopus 로고
    • Interaction of a putative transcriptional regulatory protein and the thermo-inducible cts-52 mutant repressor in the Bacillus subtilis phage φ{symbol}105 genome
    • Chan A.Y., and Lim B.L. Interaction of a putative transcriptional regulatory protein and the thermo-inducible cts-52 mutant repressor in the Bacillus subtilis phage φ{symbol}105 genome. J. Mol. Biol. 333 (2003) 21-31
    • (2003) J. Mol. Biol. , vol.333 , pp. 21-31
    • Chan, A.Y.1    Lim, B.L.2
  • 8
    • 0028181043 scopus 로고
    • Site-directed mutagenesis of β-lactamase I: role of Glu-166
    • Leung Y.C., Robinson C.V., Aplin R.T., and Waley S.G. Site-directed mutagenesis of β-lactamase I: role of Glu-166. Biochem. J. 299 (1994) 671-678
    • (1994) Biochem. J. , vol.299 , pp. 671-678
    • Leung, Y.C.1    Robinson, C.V.2    Aplin, R.T.3    Waley, S.G.4
  • 9
    • 0032102861 scopus 로고    scopus 로고
    • A heat-inducible Bacillus subtilis bacteriophage φ{symbol}105 expression system for the production of the protective antigen of Bacillus anthracis
    • Baillie L.W., Moore P., and McBride B.W. A heat-inducible Bacillus subtilis bacteriophage φ{symbol}105 expression system for the production of the protective antigen of Bacillus anthracis. FEMS Microbiol. Lett. 163 (1998) 43-47
    • (1998) FEMS Microbiol. Lett. , vol.163 , pp. 43-47
    • Baillie, L.W.1    Moore, P.2    McBride, B.W.3
  • 10
    • 0036315591 scopus 로고    scopus 로고
    • Molecular cloning and the biochemical characterization of two novel phytases from B. subtilis 168 and B. licheniformis
    • Tye A.J., Siu F.K., Leung T.Y., and Lim B.L. Molecular cloning and the biochemical characterization of two novel phytases from B. subtilis 168 and B. licheniformis. Appl. Microbiol. Biotechnol. 59 (2002) 190-197
    • (2002) Appl. Microbiol. Biotechnol. , vol.59 , pp. 190-197
    • Tye, A.J.1    Siu, F.K.2    Leung, T.Y.3    Lim, B.L.4
  • 11
    • 1542345030 scopus 로고    scopus 로고
    • An efficient heat-inducible Bacillus subtilis bacteriophage φ{symbol}105 expression and secretion system for the production of the Streptomyces clavuligerus β-lactamase inhibitory protein (BLIP)
    • Liu H.B., Chui K.S., Chan C.L., Tsang C.W., and Leung Y.C. An efficient heat-inducible Bacillus subtilis bacteriophage φ{symbol}105 expression and secretion system for the production of the Streptomyces clavuligerus β-lactamase inhibitory protein (BLIP). J. Biotechnol. 108 (2004) 207-217
    • (2004) J. Biotechnol. , vol.108 , pp. 207-217
    • Liu, H.B.1    Chui, K.S.2    Chan, C.L.3    Tsang, C.W.4    Leung, Y.C.5
  • 13
    • 0347567025 scopus 로고    scopus 로고
    • Co-expression of a prophage system and a plasmid system in Bacillus subtilis
    • Ho K.M., and Lim B.L. Co-expression of a prophage system and a plasmid system in Bacillus subtilis. Protein Expr. Purif. 32 (2003) 293-301
    • (2003) Protein Expr. Purif. , vol.32 , pp. 293-301
    • Ho, K.M.1    Lim, B.L.2
  • 14
    • 0024287069 scopus 로고
    • Sequence and comparative analysis of three Enterobacter cloacae amp C β-lactamase genes and their products
    • Galleni M., Lindberg F., Normark S., Cole S., Honore N., Joris B., and Frère J.M. Sequence and comparative analysis of three Enterobacter cloacae amp C β-lactamase genes and their products. Biochem. J. 250 (1988) 753-760
    • (1988) Biochem. J. , vol.250 , pp. 753-760
    • Galleni, M.1    Lindberg, F.2    Normark, S.3    Cole, S.4    Honore, N.5    Joris, B.6    Frère, J.M.7
  • 15
    • 0024520745 scopus 로고
    • Site-directed mutagenesis by overlap extension using the polymerase chain reaction
    • Ho S.N., Hunt H.D., Horton R.M., Pullen J.K., and Pease L.R. Site-directed mutagenesis by overlap extension using the polymerase chain reaction. Gene 77 (1989) 51-59
    • (1989) Gene , vol.77 , pp. 51-59
    • Ho, S.N.1    Hunt, H.D.2    Horton, R.M.3    Pullen, J.K.4    Pease, L.R.5
  • 16
    • 0021994611 scopus 로고
    • Thermoinducible transcription system for Bacillus subtilis that utilizes control elements from template phage phi-105
    • Osburne M.S., Craig R.J., and Rothstein D.M. Thermoinducible transcription system for Bacillus subtilis that utilizes control elements from template phage phi-105. J. Bacteriol. 163 (1985) 1101-1108
    • (1985) J. Bacteriol. , vol.163 , pp. 1101-1108
    • Osburne, M.S.1    Craig, R.J.2    Rothstein, D.M.3
  • 17
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72 (1976) 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 18
    • 0016162098 scopus 로고
    • A spectrophotometric assay of β-lactamase action on penicillins
    • Waley S.G. A spectrophotometric assay of β-lactamase action on penicillins. Biochem. J. 139 (1974) 789-790
    • (1974) Biochem. J. , vol.139 , pp. 789-790
    • Waley, S.G.1
  • 19
    • 0016418342 scopus 로고
    • β-Lactamase (Enterobacter species)
    • Ross G.W. β-Lactamase (Enterobacter species). Methods Enzymol. 43 (1975) 678-687
    • (1975) Methods Enzymol. , vol.43 , pp. 678-687
    • Ross, G.W.1
  • 20
    • 0027401020 scopus 로고
    • Protein secretion in Bacillus species
    • Simonen M., and Palva I. Protein secretion in Bacillus species. Microbiol. Rev. 57 (1993) 109-137
    • (1993) Microbiol. Rev. , vol.57 , pp. 109-137
    • Simonen, M.1    Palva, I.2
  • 22
    • 0021095927 scopus 로고
    • Crystallographic data for β-lactamase from Enterobacter cloacae P99
    • Charlier P., Dideberg O., Frére J.M., Moews P.C., and Knox J.R. Crystallographic data for β-lactamase from Enterobacter cloacae P99. J. Mol. Biol. 171 (1983) 237-238
    • (1983) J. Mol. Biol. , vol.171 , pp. 237-238
    • Charlier, P.1    Dideberg, O.2    Frére, J.M.3    Moews, P.C.4    Knox, J.R.5
  • 23
    • 0024210583 scopus 로고
    • Large-scale purification of the chromosomal β-lactamase from Enterobacter cloacae P99
    • Goward C.R., Stevens G.B., Hammond P.M., and Scawen M.D. Large-scale purification of the chromosomal β-lactamase from Enterobacter cloacae P99. J. Chromatogr. 457 (1988) 317-324
    • (1988) J. Chromatogr. , vol.457 , pp. 317-324
    • Goward, C.R.1    Stevens, G.B.2    Hammond, P.M.3    Scawen, M.D.4
  • 24
    • 0023134051 scopus 로고
    • Common mechanism of amp C β-lactamase induction in Enterobactera: regulation of the cloned Enterobacter cloacae P99 β-lactamase gene
    • Lindberg F., and Normark S. Common mechanism of amp C β-lactamase induction in Enterobactera: regulation of the cloned Enterobacter cloacae P99 β-lactamase gene. J. Bacteriol. 169 (1987) 758-763
    • (1987) J. Bacteriol. , vol.169 , pp. 758-763
    • Lindberg, F.1    Normark, S.2
  • 25
    • 0030044332 scopus 로고    scopus 로고
    • Modifying the specificity and activity of the Enterobacter cloacae P99 β-lactamase by mutagenesis within an M13 phage vector
    • Siemers N.O., Yelton D.E., Bajorath J., and Senter P.D. Modifying the specificity and activity of the Enterobacter cloacae P99 β-lactamase by mutagenesis within an M13 phage vector. Biochemistry 35 (1996) 2104-2111
    • (1996) Biochemistry , vol.35 , pp. 2104-2111
    • Siemers, N.O.1    Yelton, D.E.2    Bajorath, J.3    Senter, P.D.4
  • 26
    • 0041842502 scopus 로고    scopus 로고
    • Identification of residues critical for catalysis in a class C β-lactamase by combinatorial scanning mutagenesis
    • Goldberg S.D., Iannuccilli W., Nguyen T., Ju J., and Cornish V.W. Identification of residues critical for catalysis in a class C β-lactamase by combinatorial scanning mutagenesis. Protein Sci. 12 (2003) 1633-1645
    • (2003) Protein Sci. , vol.12 , pp. 1633-1645
    • Goldberg, S.D.1    Iannuccilli, W.2    Nguyen, T.3    Ju, J.4    Cornish, V.W.5
  • 27
    • 0032555125 scopus 로고    scopus 로고
    • Effect of an amino acid insertion into the omega loop region of a class C β-lactamase on its substrate specificity
    • Nukaga M., Taniguchi K., Washio Y., and Sawai T. Effect of an amino acid insertion into the omega loop region of a class C β-lactamase on its substrate specificity. Biochemistry 37 (1998) 10461-10468
    • (1998) Biochemistry , vol.37 , pp. 10461-10468
    • Nukaga, M.1    Taniguchi, K.2    Washio, Y.3    Sawai, T.4
  • 28
    • 0035824615 scopus 로고    scopus 로고
    • Amino acid sequence determinants of extended spectrum cephalosporin hydrolysis by the class C P99 β-lactamase
    • Zhang Z., Yu Y., Musser J.M., and Palzkill T. Amino acid sequence determinants of extended spectrum cephalosporin hydrolysis by the class C P99 β-lactamase. J. Biol. Chem. 276 (2001) 46568-46574
    • (2001) J. Biol. Chem. , vol.276 , pp. 46568-46574
    • Zhang, Z.1    Yu, Y.2    Musser, J.M.3    Palzkill, T.4
  • 29
  • 30
    • 2342471916 scopus 로고    scopus 로고
    • Chromophoric spin-labeled β-lactam antibiotics for ENDOR structural characterization of reaction intermediates of class A and class C β-lactamases
    • Mustafi D., Hofer J.E., Huang W., Palzkill T., and Makinen M.W. Chromophoric spin-labeled β-lactam antibiotics for ENDOR structural characterization of reaction intermediates of class A and class C β-lactamases. Spectrochim. Acta A Mol. Biomol. Spectrosc. 60 (2004) 1279-1289
    • (2004) Spectrochim. Acta A Mol. Biomol. Spectrosc. , vol.60 , pp. 1279-1289
    • Mustafi, D.1    Hofer, J.E.2    Huang, W.3    Palzkill, T.4    Makinen, M.W.5
  • 32
    • 0032884573 scopus 로고    scopus 로고
    • Recombinant protein expression in Escherichia coli
    • Baneyx F. Recombinant protein expression in Escherichia coli. Curr. Opin. Biotechnol. 10 (1999) 411-421
    • (1999) Curr. Opin. Biotechnol. , vol.10 , pp. 411-421
    • Baneyx, F.1
  • 33
    • 0035821418 scopus 로고    scopus 로고
    • Reaction of Lys-Tyr-Lys triad mimics with benzylpenicillin: insight into the role of Tyr150 in class C β-lactamase
    • Kato-Toma Y., and Ishiguro M. Reaction of Lys-Tyr-Lys triad mimics with benzylpenicillin: insight into the role of Tyr150 in class C β-lactamase. Bioorg. Med. Chem. Lett. 11 (2001) 1161-1164
    • (2001) Bioorg. Med. Chem. Lett. , vol.11 , pp. 1161-1164
    • Kato-Toma, Y.1    Ishiguro, M.2
  • 34
    • 0027978868 scopus 로고
    • The role of tyrosine 150 in catalysis of β-lactam hydrolysis by AmpC β-lactamase from Escherichia coli investigated by site-directed mutagenesis
    • Dubus A., Normark S., Kania M., and Page M.G.P. The role of tyrosine 150 in catalysis of β-lactam hydrolysis by AmpC β-lactamase from Escherichia coli investigated by site-directed mutagenesis. Biochemistry 33 (1994) 8577-8586
    • (1994) Biochemistry , vol.33 , pp. 8577-8586
    • Dubus, A.1    Normark, S.2    Kania, M.3    Page, M.G.P.4
  • 36
    • 0028216595 scopus 로고
    • Role of residue Lys315 in the mechanism of action of the Enterobacter cloacae 908R β-lactamase
    • Monnaie D., Dubus A., Cooke D., Marchand-Brynaert J., Normark S., and Frère J.M. Role of residue Lys315 in the mechanism of action of the Enterobacter cloacae 908R β-lactamase. Biochemistry 33 (1994) 5193-5201
    • (1994) Biochemistry , vol.33 , pp. 5193-5201
    • Monnaie, D.1    Dubus, A.2    Cooke, D.3    Marchand-Brynaert, J.4    Normark, S.5    Frère, J.M.6
  • 37
    • 0020440553 scopus 로고
    • Secretion of Escherichia coli β-lactamase from Bacillus subtilis by the aid of α-amylase signal sequence
    • Palva I., Sarvas M., Lehtovaara P., Sibakov M., and Kääriäinen L. Secretion of Escherichia coli β-lactamase from Bacillus subtilis by the aid of α-amylase signal sequence. Proc. Natl. Acad. Sci. USA 79 (1982) 5582-5586
    • (1982) Proc. Natl. Acad. Sci. USA , vol.79 , pp. 5582-5586
    • Palva, I.1    Sarvas, M.2    Lehtovaara, P.3    Sibakov, M.4    Kääriäinen, L.5
  • 38
    • 0021316249 scopus 로고
    • A Bacillus subtilis secretion vector system derived from the B. subtilis alpha-amylase promoter and signal sequence region, and secretion of Escherichia coli β-lactamase by the vector system
    • Ohmura K., Shiroza T., Nakamura K., Nakayama A., Yamane K., Yoda K., Yamasaki M., and Tamura G. A Bacillus subtilis secretion vector system derived from the B. subtilis alpha-amylase promoter and signal sequence region, and secretion of Escherichia coli β-lactamase by the vector system. J. Biochem. 95 (1984) 87-93
    • (1984) J. Biochem. , vol.95 , pp. 87-93
    • Ohmura, K.1    Shiroza, T.2    Nakamura, K.3    Nakayama, A.4    Yamane, K.5    Yoda, K.6    Yamasaki, M.7    Tamura, G.8
  • 39
    • 0021927129 scopus 로고
    • Transcription and translation of foreign genes in Bacillus subtilis by the aid of a secretion vector
    • Ulmanen I., Lundström K., Lehtovaara P., Sarvas M., Ruohonen M., and Palva I. Transcription and translation of foreign genes in Bacillus subtilis by the aid of a secretion vector. J. Bacteriol. 162 (1985) 176-182
    • (1985) J. Bacteriol. , vol.162 , pp. 176-182
    • Ulmanen, I.1    Lundström, K.2    Lehtovaara, P.3    Sarvas, M.4    Ruohonen, M.5    Palva, I.6


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