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Volumn 73, Issue 13, 2007, Pages 4142-4151

Characterization of the zinc-containing metalloprotease encoded by zpx and development of a species-specific detection method for Enterobacter sakazakii

Author keywords

[No Author keywords available]

Indexed keywords

ENVIRONMENTAL STRAINS; GEL FILTRATION CHROMATOGRAPHY; PATHOGENICITY; PROTEOLYTIC ENZYMES;

EID: 34447540369     PISSN: 00992240     EISSN: None     Source Type: Journal    
DOI: 10.1128/AEM.02729-06     Document Type: Article
Times cited : (91)

References (35)
  • 1
    • 0027515396 scopus 로고
    • Astacins, serralysins, snake venom and matrix metalloproteases exhibit identical zinc-binding environments (HEXXHXXGXXH and Met turn) and topologies and should be grouped into a common family, the metzincins
    • Bode, W., F. X. Gomis-Rüth, and W. Stöker. 1993. Astacins, serralysins, snake venom and matrix metalloproteases exhibit identical zinc-binding environments (HEXXHXXGXXH and Met turn) and topologies and should be grouped into a common family, the metzincins. FEBS Lett. 331:134-140.
    • (1993) FEBS Lett , vol.331 , pp. 134-140
    • Bode, W.1    Gomis-Rüth, F.X.2    Stöker, W.3
  • 2
    • 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. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248-254.
    • (1976) Anal. Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 5
    • 0345096420 scopus 로고    scopus 로고
    • Isolation and characterization of a zinc-containing metalloprotease expressed by Vibrio tubiashii
    • Delston, R. B., M. H. Kothary, K. A. Shangraw, and B. D. Tall. 2003. Isolation and characterization of a zinc-containing metalloprotease expressed by Vibrio tubiashii. Can. J. Microbiol. 49:525-529.
    • (2003) Can. J. Microbiol , vol.49 , pp. 525-529
    • Delston, R.B.1    Kothary, M.H.2    Shangraw, K.A.3    Tall, B.D.4
  • 7
    • 0019311549 scopus 로고    scopus 로고
    • Farmer, J. J., III, M. A. Asbury, F. W. Hickman, D. J. Brenner, and the Enterobacteriaceae Study Group. 1980. Enterobacter sakazakii: a new species of Enterobacteriaceae isolated from clinical specimens. Int. J. Sys. Bacteriol. 30:569-584.
    • Farmer, J. J., III, M. A. Asbury, F. W. Hickman, D. J. Brenner, and the Enterobacteriaceae Study Group. 1980. Enterobacter sakazakii: a new species of "Enterobacteriaceae" isolated from clinical specimens. Int. J. Sys. Bacteriol. 30:569-584.
  • 8
    • 0542360407 scopus 로고
    • Vibrio cholerae hemagglutinin/lectin/protease hydrolyzes fibronectin and ovomucin: F. M. Burnet revisited
    • Finkelstein, R. A., M. Boesman-Finkelstein, and P. Holt. 1983. Vibrio cholerae hemagglutinin/lectin/protease hydrolyzes fibronectin and ovomucin: F. M. Burnet revisited. Proc. Natl. Acad. Sci. USA 80:1092-1095.
    • (1983) Proc. Natl. Acad. Sci. USA , vol.80 , pp. 1092-1095
    • Finkelstein, R.A.1    Boesman-Finkelstein, M.2    Holt, P.3
  • 9
    • 0028292373 scopus 로고
    • A carboxy-terminal four amino acid motif is required for secretion of the metalloprotease PrtG through the Erwinia chrysanthemi protease secretion pathway
    • Ghigo, J. M., and C. Wandersman. 1994. A carboxy-terminal four amino acid motif is required for secretion of the metalloprotease PrtG through the Erwinia chrysanthemi protease secretion pathway. J. Biol. Chem. 269:8979-8985.
    • (1994) J. Biol. Chem , vol.269 , pp. 8979-8985
    • Ghigo, J.M.1    Wandersman, C.2
  • 10
    • 0025117758 scopus 로고
    • Cellular location of a Treponema denticola chymotrypsin-like protease and importance of the protease in migration through the basement membrane
    • Grenier, D., V. J. Uitto, and B. C. McBride. 1990. Cellular location of a Treponema denticola chymotrypsin-like protease and importance of the protease in migration through the basement membrane. Infect. Immun. 58:347-351.
    • (1990) Infect. Immun , vol.58 , pp. 347-351
    • Grenier, D.1    Uitto, V.J.2    McBride, B.C.3
  • 11
    • 0029991619 scopus 로고    scopus 로고
    • Bacterial collagenases and collagen-degrading enzymes and their potential role in human disease
    • Harrington, D. J. 1996. Bacterial collagenases and collagen-degrading enzymes and their potential role in human disease. Infect. Immun. 64:1885-1891.
    • (1996) Infect. Immun , vol.64 , pp. 1885-1891
    • Harrington, D.J.1
  • 12
    • 0027140429 scopus 로고
    • Bacterial extracellular zinc-containing metalloproteases
    • Hase, C. C., and R. A. Finkelstein. 1993. Bacterial extracellular zinc-containing metalloproteases. Microbiol. Rev. 57:823-837.
    • (1993) Microbiol. Rev , vol.57 , pp. 823-837
    • Hase, C.C.1    Finkelstein, R.A.2
  • 13
    • 0021346267 scopus 로고
    • Cellular location of heat-labile enterotoxin in Escherichia coli
    • Hirst, T. R., L. L. Randall, and S. J. S. Hardy. 1984. Cellular location of heat-labile enterotoxin in Escherichia coli. J. Bacteriol. 157:637-642.
    • (1984) J. Bacteriol , vol.157 , pp. 637-642
    • Hirst, T.R.1    Randall, L.L.2    Hardy, S.J.S.3
  • 14
    • 2042482746 scopus 로고    scopus 로고
    • The growth profile, thermotolerance and biofilm formation of Enterobacter sakazakii grown in infant formula milk
    • Iversen, C., M. Lane, and S. J. Forsythe. 2004. The growth profile, thermotolerance and biofilm formation of Enterobacter sakazakii grown in infant formula milk. Lett. Applied. Microbiol. 38:378-382.
    • (2004) Lett. Applied. Microbiol , vol.38 , pp. 378-382
    • Iversen, C.1    Lane, M.2    Forsythe, S.J.3
  • 15
    • 33750622848 scopus 로고    scopus 로고
    • The biochemical differentiation of Enterobacter sakazakii genotypes
    • Iversen, C., M. Waddington, J. J. Farmer III, and S. J. Forsythe. 2006. The biochemical differentiation of Enterobacter sakazakii genotypes. BMC Microbiol. 6:94-101.
    • (2006) BMC Microbiol , vol.6 , pp. 94-101
    • Iversen, C.1    Waddington, M.2    Farmer III, J.J.3    Forsythe, S.J.4
  • 16
    • 0024559146 scopus 로고
    • A unique signature identifies a family of zinc-dependent metallopeptidases
    • Jongeneel, C. V., J. Bouvier, and A. Bairoch. 1989. A unique signature identifies a family of zinc-dependent metallopeptidases. FEBS Lett. 242:211-214.
    • (1989) FEBS Lett , vol.242 , pp. 211-214
    • Jongeneel, C.V.1    Bouvier, J.2    Bairoch, A.3
  • 17
    • 0346024007 scopus 로고    scopus 로고
    • Occurrence of Enterobacter sakazakii in food production environments and households
    • Kandhai, M. C., M. W. Rey, L. G. Gorris, O. Guillaume-Gentil, and M. van Schothors. 2004. Occurrence of Enterobacter sakazakii in food production environments and households. Lancet 363:39-40.
    • (2004) Lancet , vol.363 , pp. 39-40
    • Kandhai, M.C.1    Rey, M.W.2    Gorris, L.G.3    Guillaume-Gentil, O.4    van Schothors, M.5
  • 18
    • 0022405648 scopus 로고
    • Production and partial characterization of an elastolytic protease of Vibrio vulnificus
    • Kothary, M. H., and A. S. Kreger. 1985. Production and partial characterization of an elastolytic protease of Vibrio vulnificus. Infect. Immun. 50:534-540.
    • (1985) Infect. Immun , vol.50 , pp. 534-540
    • Kothary, M.H.1    Kreger, A.S.2
  • 19
    • 0029025587 scopus 로고
    • Purification and characterization of a Chinese hamster ovary cell elongation factor of Vibrio hollisae
    • Kothary, M. H., E. F. Claverie, M. D. Miliotis, J. M. Madden, and S. H. Richardson. 1995. Purification and characterization of a Chinese hamster ovary cell elongation factor of Vibrio hollisae. Infect. Immun. 63:2418-2423.
    • (1995) Infect. Immun , vol.63 , pp. 2418-2423
    • Kothary, M.H.1    Claverie, E.F.2    Miliotis, M.D.3    Madden, J.M.4    Richardson, S.H.5
  • 20
    • 0017817596 scopus 로고
    • Purification of Pseudomonas aeruginosa proteases and microscopic characterization of pseudomonal protease-induced rabbit corneal damage
    • Kreger, A. S., and L. D. Gray. 1978. Purification of Pseudomonas aeruginosa proteases and microscopic characterization of pseudomonal protease-induced rabbit corneal damage. Infect. Immun. 19:630-648.
    • (1978) Infect. Immun , vol.19 , pp. 630-648
    • Kreger, A.S.1    Gray, L.D.2
  • 21
    • 0026053153 scopus 로고
    • Erwinia carotovora subsp. carotovora extracellular protease: Characterization and nucleotide sequence of the gene
    • Kyostio, S. R. M., C. L. Cramer, and G. H. Lacy. 1991. Erwinia carotovora subsp. carotovora extracellular protease: characterization and nucleotide sequence of the gene. J. Bacteriol. 173:6537-6546.
    • (1991) J. Bacteriol , vol.173 , pp. 6537-6546
    • Kyostio, S.R.M.1    Cramer, C.L.2    Lacy, G.H.3
  • 22
    • 0020054002 scopus 로고
    • Detection of toxins produced by Vibrio fluvialis
    • Lockwood, D. E., A. S. Kreger, and S. H. Richardson. 1982. Detection of toxins produced by Vibrio fluvialis. Infect. Immun. 35:702-708.
    • (1982) Infect. Immun , vol.35 , pp. 702-708
    • Lockwood, D.E.1    Kreger, A.S.2    Richardson, S.H.3
  • 23
    • 0018396426 scopus 로고
    • Purification and characterization of a Serratia marcescens metalloprotease
    • Lyerly, D., and A. Kreger. 1979. Purification and characterization of a Serratia marcescens metalloprotease. Infect. Immun. 24:411-421.
    • (1979) Infect. Immun , vol.24 , pp. 411-421
    • Lyerly, D.1    Kreger, A.2
  • 24
    • 0033973889 scopus 로고    scopus 로고
    • Microbial metalloproteases and pathogenesis
    • Miyoshi, S., and S. Shinoda. 2000. Microbial metalloproteases and pathogenesis. Microbes Infect. 2:91-98.
    • (2000) Microbes Infect , vol.2 , pp. 91-98
    • Miyoshi, S.1    Shinoda, S.2
  • 25
  • 27
    • 27944480029 scopus 로고    scopus 로고
    • Molecular genetics of Erwinia amylovora involved in the development of fire blight
    • Oh, C.-S., and S. V. Beer. 2005. Molecular genetics of Erwinia amylovora involved in the development of fire blight. FEMS. Microbiol. Lett. 253:185-192.
    • (2005) FEMS. Microbiol. Lett , vol.253 , pp. 185-192
    • Oh, C.-S.1    Beer, S.V.2
  • 28
    • 0345269152 scopus 로고    scopus 로고
    • Enterobacter sakazakii: Infectivity and enterotoxin production in vitro and in vivo
    • Pagotto, F. J., M. Nazarowec-White, S. Bidawid, and J. M. Farber. 2003. Enterobacter sakazakii: infectivity and enterotoxin production in vitro and in vivo. J. Food Prot. 66:370-375.
    • (2003) J. Food Prot , vol.66 , pp. 370-375
    • Pagotto, F.J.1    Nazarowec-White, M.2    Bidawid, S.3    Farber, J.M.4
  • 31
    • 0028068293 scopus 로고
    • Molecular cloning and sequencing of the cDNA and gene for a novel elastinolytic metalloprotease from Aspergillus fumigatus and its expression in Escherichia coli
    • Sirakova, T. D., A. Markaryan, and P. E. Kolattukudy. 1994. Molecular cloning and sequencing of the cDNA and gene for a novel elastinolytic metalloprotease from Aspergillus fumigatus and its expression in Escherichia coli. Infect. Immun. 62:4208-4218.
    • (1994) Infect. Immun , vol.62 , pp. 4208-4218
    • Sirakova, T.D.1    Markaryan, A.2    Kolattukudy, P.E.3
  • 32
    • 0022512195 scopus 로고
    • Two toxin-converting phages from Escherichia coli O157:H7 strain 933 encode antigenically distinct toxins with similar biologic activities
    • Strockbine, N. A., L. R. M. Marques, J. W. Newland, H. Williams-Smith, R. K. Holmes, and A. D. O'Brien. 1986. Two toxin-converting phages from Escherichia coli O157:H7 strain 933 encode antigenically distinct toxins with similar biologic activities. Infect. Immun. 53:135-140.
    • (1986) Infect. Immun , vol.53 , pp. 135-140
    • Strockbine, N.A.1    Marques, L.R.M.2    Newland, J.W.3    Williams-Smith, H.4    Holmes, R.K.5    O'Brien, A.D.6
  • 33
    • 0033854889 scopus 로고    scopus 로고
    • Analysis of gyrB- and toxR-targeted PCR methods for isolation of Vibrio hollisae from the environment and its identification
    • Vuddhakul, V., T. Nakai, C. Matsumoto, T. Oh, T. Nishino, C.-H. Chen, M. Nishibuchi, and J. Okuda. 2000. Analysis of gyrB- and toxR-targeted PCR methods for isolation of Vibrio hollisae from the environment and its identification. Appl. Environ. Microbiol. 66:3506-3514.
    • (2000) Appl. Environ. Microbiol , vol.66 , pp. 3506-3514
    • Vuddhakul, V.1    Nakai, T.2    Matsumoto, C.3    Oh, T.4    Nishino, T.5    Chen, C.-H.6    Nishibuchi, M.7    Okuda, J.8
  • 34
    • 0015437962 scopus 로고
    • Measurement of molecular weights by electrophoresis on SDS-acrylamide gel
    • Weber, K., J. R. Pringle, and M. Osborn. 1972. Measurement of molecular weights by electrophoresis on SDS-acrylamide gel. Methods Enzymol. 26:3-27.
    • (1972) Methods Enzymol , vol.26 , pp. 3-27
    • Weber, K.1    Pringle, J.R.2    Osborn, M.3
  • 35
    • 0033603510 scopus 로고    scopus 로고
    • Molecular characterization of a protease secreted by Erwinia amylovora
    • Zhang, Y., D. D. Bak, H. Held, and K. Geider. 1999. Molecular characterization of a protease secreted by Erwinia amylovora. J. Mol. Bacteriol. 289:1239-1251.
    • (1999) J. Mol. Bacteriol , vol.289 , pp. 1239-1251
    • Zhang, Y.1    Bak, D.D.2    Held, H.3    Geider, K.4


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