메뉴 건너뛰기




Volumn 111, Issue 6, 2011, Pages 1406-1415

Cloning, expression and purification of extracellular serine protease Esp, a biofilm-degrading enzyme, from Staphylococcus epidermidis

Author keywords

Biofilm(s); Biotechnology; Proteinase; Rapid methods; Staphylococci

Indexed keywords

AFFINITY CHROMATOGRAPHY; AMINO ACIDS; BIOFILMS; BIOTECHNOLOGY; ENZYME ACTIVITY; ESCHERICHIA COLI; GENES; RECOMBINANT PROTEINS;

EID: 81255153660     PISSN: 13645072     EISSN: 13652672     Source Type: Journal    
DOI: 10.1111/j.1365-2672.2011.05167.x     Document Type: Article
Times cited : (15)

References (20)
  • 1
    • 0034254189 scopus 로고    scopus 로고
    • Macromolecular crowding perturbs protein refolding kinetics: implications for folding inside the cell
    • van den Berg, B., Wain, R., Dobson, C.M. and Ellis, R.J. (2000) Macromolecular crowding perturbs protein refolding kinetics: implications for folding inside the cell. EMBO J 19, 3870-3875.
    • (2000) EMBO J , vol.19 , pp. 3870-3875
    • van den Berg, B.1    Wain, R.2    Dobson, C.M.3    Ellis, R.J.4
  • 2
    • 79954759457 scopus 로고    scopus 로고
    • Protein body-inducing fusions for high-level production and purification of recombinant proteins in plants
    • Conley, A.J., Joensuu, J.J., Richman, A. and Menassa, R. (2011) Protein body-inducing fusions for high-level production and purification of recombinant proteins in plants. Plant Biotechnol J 9, 419-433.
    • (2011) Plant Biotechnol J , vol.9 , pp. 419-433
    • Conley, A.J.1    Joensuu, J.J.2    Richman, A.3    Menassa, R.4
  • 3
    • 79955788202 scopus 로고    scopus 로고
    • Manufacturing recombinant proteins in kg-ton quantities using animal cells in bioreactors
    • De Jesus, M. and Wurm, F.M. (2011) Manufacturing recombinant proteins in kg-ton quantities using animal cells in bioreactors. Eur J Pharm Biopharm 78, 184-188.
    • (2011) Eur J Pharm Biopharm , vol.78 , pp. 184-188
    • De Jesus, M.1    Wurm, F.M.2
  • 4
    • 0018082649 scopus 로고
    • Role of a metalloprotease in activation of the precursor of staphylococcal protease
    • Drapeau, G.R. (1978) Role of a metalloprotease in activation of the precursor of staphylococcal protease. J Bacteriol 136, 607-613.
    • (1978) J Bacteriol , vol.136 , pp. 607-613
    • Drapeau, G.R.1
  • 5
    • 0035202193 scopus 로고    scopus 로고
    • Molecular cloning and biochemical characterization of proteases from Staphylococcus epidermidis
    • Dubin, G., Chmiel, D., Mak, P., Rakwalska, M., Rzychon, M. and Dubin, A. (2001) Molecular cloning and biochemical characterization of proteases from Staphylococcus epidermidis. Biol Chem 382, 1575-1582.
    • (2001) Biol Chem , vol.382 , pp. 1575-1582
    • Dubin, G.1    Chmiel, D.2    Mak, P.3    Rakwalska, M.4    Rzychon, M.5    Dubin, A.6
  • 6
    • 25844514728 scopus 로고    scopus 로고
    • Preparative expression of secreted proteins in bacteria: status report and future prospects
    • Georgiou, G. and Segatori, L. (2005) Preparative expression of secreted proteins in bacteria: status report and future prospects. Curr Opin Biotechnol 16, 538-545.
    • (2005) Curr Opin Biotechnol , vol.16 , pp. 538-545
    • Georgiou, G.1    Segatori, L.2
  • 7
    • 77952723375 scopus 로고    scopus 로고
    • Staphylococcus epidermidis Esp inhibits Staphylococcus aureus biofilm formation and nasal colonization
    • Iwase, T., Uehara, Y., Shinji, H., Tajima, A., Seo, H., Takada, K., Agata, T. and Mizunoe, Y. (2010) Staphylococcus epidermidis Esp inhibits Staphylococcus aureus biofilm formation and nasal colonization. Nature 465, 346-349.
    • (2010) Nature , vol.465 , pp. 346-349
    • Iwase, T.1    Uehara, Y.2    Shinji, H.3    Tajima, A.4    Seo, H.5    Takada, K.6    Agata, T.7    Mizunoe, Y.8
  • 8
    • 77049115760 scopus 로고    scopus 로고
    • Extracellular production of riboflavin-binding protein, a potential bitter inhibitor, by Brevibacillus choshinensis
    • Maehashi, K., Matano, M., Saito, M. and Udaka, S. (2010) Extracellular production of riboflavin-binding protein, a potential bitter inhibitor, by Brevibacillus choshinensis. Protein Expr Purif 71, 85-90.
    • (2010) Protein Expr Purif , vol.71 , pp. 85-90
    • Maehashi, K.1    Matano, M.2    Saito, M.3    Udaka, S.4
  • 9
    • 0033524956 scopus 로고    scopus 로고
    • The prosequence of thermolysin acts as an intramolecular chaperone when expressed in trans with the mature sequence in Escherichia coli
    • Marie-Claire, C., Ruffet, E., Beaumont, A. and Roques, B.P. (1999) The prosequence of thermolysin acts as an intramolecular chaperone when expressed in trans with the mature sequence in Escherichia coli. J Mol Biol 285, 1911-1915.
    • (1999) J Mol Biol , vol.285 , pp. 1911-1915
    • Marie-Claire, C.1    Ruffet, E.2    Beaumont, A.3    Roques, B.P.4
  • 10
    • 0034871603 scopus 로고    scopus 로고
    • Isolation and characterization of a highly specific serine endopeptidase from an oral strain of Staphylococcus epidermidis
    • Moon, J.L., Banbula, A., Oleksy, A., Mayo, J.A. and Travis, J. (2001) Isolation and characterization of a highly specific serine endopeptidase from an oral strain of Staphylococcus epidermidis. Biol Chem 382, 1095-1099.
    • (2001) Biol Chem , vol.382 , pp. 1095-1099
    • Moon, J.L.1    Banbula, A.2    Oleksy, A.3    Mayo, J.A.4    Travis, J.5
  • 11
    • 38149018614 scopus 로고    scopus 로고
    • Characterization of the glutamyl endopeptidase from Staphylococcus aureus expressed in Escherichia coli
    • Nemoto, T.K., Ohara-Nemoto, Y., Ono, T., Kobayakawa, T., Shimoyama, Y., Kimura, S. and Takagi, T. (2008) Characterization of the glutamyl endopeptidase from Staphylococcus aureus expressed in Escherichia coli. FEBS J 275, 573-587.
    • (2008) FEBS J , vol.275 , pp. 573-587
    • Nemoto, T.K.1    Ohara-Nemoto, Y.2    Ono, T.3    Kobayakawa, T.4    Shimoyama, Y.5    Kimura, S.6    Takagi, T.7
  • 12
    • 0036377884 scopus 로고    scopus 로고
    • Characterization and molecular cloning of a glutamyl endopeptidase from Staphylococcus epidermidis
    • Ohara-Nemoto, Y., Ikeda, Y., Kobayashi, M., Sasaki, M., Tajika, S. and Kimura, S. (2002) Characterization and molecular cloning of a glutamyl endopeptidase from Staphylococcus epidermidis. Microb Pathog 33, 33-41.
    • (2002) Microb Pathog , vol.33 , pp. 33-41
    • Ohara-Nemoto, Y.1    Ikeda, Y.2    Kobayashi, M.3    Sasaki, M.4    Tajika, S.5    Kimura, S.6
  • 13
    • 54049137972 scopus 로고    scopus 로고
    • Homologous and heterologous expression and maturation processing of extracellular glutamyl endopeptidase of Staphylococcus epidermidis
    • Ohara-Nemoto, Y., Ono, T., Shimoyama, Y., Kimura, S. and Nemoto, T.K. (2008) Homologous and heterologous expression and maturation processing of extracellular glutamyl endopeptidase of Staphylococcus epidermidis. Biol Chem 389, 1209-1217.
    • (2008) Biol Chem , vol.389 , pp. 1209-1217
    • Ohara-Nemoto, Y.1    Ono, T.2    Shimoyama, Y.3    Kimura, S.4    Nemoto, T.K.5
  • 14
    • 79952535978 scopus 로고    scopus 로고
    • Production of recombinant proteins and metabolites in yeasts: when are these systems better than bacterial production systems?
    • Porro, D., Gasser, B., Fossati, T., Maurer, M., Branduardi, P., Sauer, M. and Mattanovich, D. (2011) Production of recombinant proteins and metabolites in yeasts: when are these systems better than bacterial production systems? Appl Microbiol Biotechnol 89, 939-948.
    • (2011) Appl Microbiol Biotechnol , vol.89 , pp. 939-948
    • Porro, D.1    Gasser, B.2    Fossati, T.3    Maurer, M.4    Branduardi, P.5    Sauer, M.6    Mattanovich, D.7
  • 15
    • 0038333906 scopus 로고
    • Bacteriophage T7 DNA polymerase: cloning and high-level expression
    • Reutimann, H., Sjöberg, B.M. and Holmgren, A. (1985) Bacteriophage T7 DNA polymerase: cloning and high-level expression. Proc Natl Acad Sci USA 82, 6783-6787.
    • (1985) Proc Natl Acad Sci USA , vol.82 , pp. 6783-6787
    • Reutimann, H.1    Sjöberg, B.M.2    Holmgren, A.3
  • 16
    • 10644255526 scopus 로고    scopus 로고
    • Advanced genetic strategies for recombinant protein expression in Escherichia coli
    • Sørensen, H.P. and Mortensen, K.K. (2005) Advanced genetic strategies for recombinant protein expression in Escherichia coli. J Biotechnol 115, 113-128.
    • (2005) J Biotechnol , vol.115 , pp. 113-128
    • Sørensen, H.P.1    Mortensen, K.K.2
  • 17
    • 34250338178 scopus 로고    scopus 로고
    • A gram-negative characteristic segment in Escherichia coli DnaK is essential for the ATP-dependent cooperative function with the co-chaperones DnaJ and GrpE
    • Sugimoto, S., Higashi, C., Saruwatari, K., Nakayama, J. and Sonomoto, K. (2007) A gram-negative characteristic segment in Escherichia coli DnaK is essential for the ATP-dependent cooperative function with the co-chaperones DnaJ and GrpE. FEBS Lett 581, 2993-2999.
    • (2007) FEBS Lett , vol.581 , pp. 2993-2999
    • Sugimoto, S.1    Higashi, C.2    Saruwatari, K.3    Nakayama, J.4    Sonomoto, K.5
  • 18
    • 0027266020 scopus 로고
    • Characterization of an extracellular metalloprotease with elastase activity from Staphylococcus epidermidis
    • Teufel, P. and Götz, F. (1993) Characterization of an extracellular metalloprotease with elastase activity from Staphylococcus epidermidis. J Bacteriol 175, 4218-4224.
    • (1993) J Bacteriol , vol.175 , pp. 4218-4224
    • Teufel, P.1    Götz, F.2
  • 19
    • 77955962894 scopus 로고    scopus 로고
    • New baculovirus expression tools for recombinant protein complex production
    • Trowitzsch, S., Bieniossek, C., Nie, Y., Garzoni, F. and Berger, I. (2010) New baculovirus expression tools for recombinant protein complex production. J Struct Biol 172, 45-54.
    • (2010) J Struct Biol , vol.172 , pp. 45-54
    • Trowitzsch, S.1    Bieniossek, C.2    Nie, Y.3    Garzoni, F.4    Berger, I.5
  • 20
    • 0034810709 scopus 로고    scopus 로고
    • High-level production of recombinant chicken interferon-γ by Brevibacillus choshinensis
    • Yashiro, K., Lowenthal, J.W., O'Neil, T.E., Ebisu, S., Takagi, H. and Moore, R.J. (2001) High-level production of recombinant chicken interferon-γ by Brevibacillus choshinensis. Protein Expr Purif 23, 113-120.
    • (2001) Protein Expr Purif , vol.23 , pp. 113-120
    • Yashiro, K.1    Lowenthal, J.W.2    O'Neil, T.E.3    Ebisu, S.4    Takagi, H.5    Moore, R.J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.