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Volumn 68, Issue 11, 2002, Pages 5311-5317

The murein hydrolase of the bacteriophage φ3626 dual lysis system is active against all tested Clostridium perfringens strains

Author keywords

[No Author keywords available]

Indexed keywords

AFFINITY CHROMATOGRAPHY; AMINO ACIDS; BACTERIA; BIOLOGICAL MEMBRANES; CELLS; DISEASES; ENZYMES; GENES; RNA;

EID: 0036840423     PISSN: 00992240     EISSN: None     Source Type: Journal    
DOI: 10.1128/AEM.68.11.5311-5317.2002     Document Type: Article
Times cited : (126)

References (43)
  • 1
    • 0029790464 scopus 로고    scopus 로고
    • Target cell specificity of a bacteriocin molecule: A C-terminal signal directs lysostaphin to the cell wall of Staphylococcus aureus
    • Baba, T., and O. Schneewind. 1996. Target cell specificity of a bacteriocin molecule: A C-terminal signal directs lysostaphin to the cell wall of Staphylococcus aureus. EMBO J. 15:4789-4797.
    • (1996) EMBO J. , vol.15 , pp. 4789-4797
    • Baba, T.1    Schneewind, O.2
  • 3
    • 0027319793 scopus 로고
    • In vitro susceptibility of Clostridium perfringens isolated from farm animals to growth-enhancing antibiotics
    • Devriese, L. A., G. Daube, J. Hommez, and F. Haesebrouck. 1993. In vitro susceptibility of Clostridium perfringens isolated from farm animals to growth-enhancing antibiotics. J. Appl. Bacteriol. 75:55-57.
    • (1993) J. Appl. Bacteriol. , vol.75 , pp. 55-57
    • Devriese, L.A.1    Daube, G.2    Hommez, J.3    Haesebrouck, F.4
  • 5
    • 0033931924 scopus 로고    scopus 로고
    • Gene cloning and expression and secretion of Listeria monocytogenes bacteriophage-lytic enzymes in Lactococcus lactis
    • Gaeng, S., S. Scherer, H. Neve, and M. J. Loessner. 2000. Gene cloning and expression and secretion of Listeria monocytogenes bacteriophage-lytic enzymes in Lactococcus lactis. Appl. Environ. Microbiol. 66:2951-2958.
    • (2000) Appl. Environ. Microbiol. , vol.66 , pp. 2951-2958
    • Gaeng, S.1    Scherer, S.2    Neve, H.3    Loessner, M.J.4
  • 6
    • 0025037846 scopus 로고
    • Modular organization of the lytic enzymes of Streptococcus pneumoniae and its bacteriophages
    • Garcia, P., J. L. Garcia, E. Garcia, J. M. Sanchez-Puelles, and R. Lopez. 1990. Modular organization of the lytic enzymes of Streptococcus pneumoniae and its bacteriophages. Gene 86:81-88.
    • (1990) Gene , vol.86 , pp. 81-88
    • Garcia, P.1    Garcia, J.L.2    Garcia, E.3    Sanchez-Puelles, J.M.4    Lopez, R.5
  • 7
    • 0022873043 scopus 로고
    • Characterization of a bacteriocinogenic plasmid from Clostridium perfringens and molecular genetic analysis of the bacteriocin-encoding gene
    • Garnier, T., and S. T. Cole. 1986. Characterization of a bacteriocinogenic plasmid from Clostridium perfringens and molecular genetic analysis of the bacteriocin-encoding gene. J. Bacteriol. 168:1189-1196.
    • (1986) J. Bacteriol. , vol.168 , pp. 1189-1196
    • Garnier, T.1    Cole, S.T.2
  • 8
    • 0023682818 scopus 로고
    • Complete nucleotide sequence and genetic organization of the bacteriocinogenic plasmid, pIP404, from Clostridium perfringens
    • Garnier, T., and S. T. Cole. 1988. Complete nucleotide sequence and genetic organization of the bacteriocinogenic plasmid, pIP404, from Clostridium perfringens. Plasmid 19:134-150.
    • (1988) Plasmid , vol.19 , pp. 134-150
    • Garnier, T.1    Cole, S.T.2
  • 9
    • 0026892602 scopus 로고
    • Barley inclusion and avoparcin supplementation in broiler diets. 2. Clinical, pathological, and bacteriological findings in a mild form of necrotic enteritis
    • Kaldhusdal, M., and M. Hofshagen. 1992. Barley inclusion and avoparcin supplementation in broiler diets. 2. Clinical, pathological, and bacteriological findings in a mild form of necrotic enteritis. Poult. Sci. 71:1145-1153.
    • (1992) Poult. Sci. , vol.71 , pp. 1145-1153
    • Kaldhusdal, M.1    Hofshagen, M.2
  • 10
    • 0025824740 scopus 로고
    • Molecular cloning and sequencing of a major Bacillus subtilis autolysin gene
    • Kuroda, A., and J. Sekiguchi. 1991. Molecular cloning and sequencing of a major Bacillus subtilis autolysin gene. J. Bacteriol. 173:7304-7312.
    • (1991) J. Bacteriol. , vol.173 , pp. 7304-7312
    • Kuroda, A.1    Sekiguchi, J.2
  • 11
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte, J., and R. F. Doolittle. 1982. A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 157:105-132.
    • (1982) J. Mol. Biol. , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 12
    • 0035824437 scopus 로고    scopus 로고
    • Rapid killing of Streptococcus pneumoniae with a bacteriophage cell wall hydrolase
    • Loeffler, J. M., D. Nelson, and V. A. Fischetti. 2001. Rapid killing of Streptococcus pneumoniae with a bacteriophage cell wall hydrolase. Science 294:2170-2172.
    • (2001) Science , vol.294 , pp. 2170-2172
    • Loeffler, J.M.1    Nelson, D.2    Fischetti, V.A.3
  • 13
    • 0032809133 scopus 로고    scopus 로고
    • Evidence for a holin-like protein gene fully embedded out of frame in the endolysin gene of Staphylococcus aureus bacteriophage 187
    • Loessner, M. J., S. Gaeng, and S. Scherer. 1999. Evidence for a holin-like protein gene fully embedded out of frame in the endolysin gene of Staphylococcus aureus bacteriophage 187. J. Bacteriol. 181:4452-4460.
    • (1999) J. Bacteriol. , vol.181 , pp. 4452-4460
    • Loessner, M.J.1    Gaeng, S.2    Scherer, S.3
  • 14
    • 0032525314 scopus 로고    scopus 로고
    • The two-component lysis system of Staphylococcus aureus bacteriophage Twort: A large TTG-start holin and an associated amidase endolysin
    • Loessner, M. J., S. Gaeng, G. Wendlinger, S. K. Maier, and S. Scherer. 1998. The two-component lysis system of Staphylococcus aureus bacteriophage Twort: A large TTG-start holin and an associated amidase endolysin. FEMS Microbiol. Lett. 162:265-274.
    • (1998) FEMS Microbiol. Lett. , vol.162 , pp. 265-274
    • Loessner, M.J.1    Gaeng, S.2    Wendlinger, G.3    Maier, S.K.4    Scherer, S.5
  • 15
    • 0036231904 scopus 로고    scopus 로고
    • C-terminal domains of Listeria monocytogenes bacteriophage murein hydrolases determine specific recognition and high affinity binding to bacterial cell wall carbohydrates
    • Loessner, M. J., K. Kramer, F. Ebel, and S. Scherer. 2002. C-terminal domains of Listeria monocytogenes bacteriophage murein hydrolases determine specific recognition and high affinity binding to bacterial cell wall carbohydrates. Mol. Microbiol. 44:335-349.
    • (2002) Mol. Microbiol. , vol.44 , pp. 335-349
    • Loessner, M.J.1    Kramer, K.2    Ebel, F.3    Scherer, S.4
  • 16
    • 0030894847 scopus 로고    scopus 로고
    • Three Bacillus cereus bacteriophage endolysins are unrelated but reveal high homology to cell wall hydrolases from different bacilli
    • Loessner, M. J., S. K. Maier, H. Daubek-Puza, G. Wendlinger, and S. Scherer. 1997. Three Bacillus cereus bacteriophage endolysins are unrelated but reveal high homology to cell wall hydrolases from different bacilli. J. Bacteriol. 179:2845-2851.
    • (1997) J. Bacteriol. , vol.179 , pp. 2845-2851
    • Loessner, M.J.1    Maier, S.K.2    Daubek-Puza, H.3    Wendlinger, G.4    Scherer, S.5
  • 17
    • 0029783288 scopus 로고    scopus 로고
    • Modified Listeria bacteriophage lysin genes (ply) allow efficient overexpression and one-step purification of biochemically active fusion proteins
    • Loessner, M. J., A. Schneider, and S. Scherer. 1996. Modified Listeria bacteriophage lysin genes (ply) allow efficient overexpression and one-step purification of biochemically active fusion proteins. Appl. Environ. Microbiol. 62:3057-3060.
    • (1996) Appl. Environ. Microbiol. , vol.62 , pp. 3057-3060
    • Loessner, M.J.1    Schneider, A.2    Scherer, S.3
  • 18
    • 0028963469 scopus 로고
    • A new procedure for efficient recovery of DNA, RNA, and proteins from Listeria cells by rapid lysis with a recombinant bacteriophage endolysin
    • Loessner, M. J., A. Schneider, and S. Scherer. 1995. A new procedure for efficient recovery of DNA, RNA, and proteins from Listeria cells by rapid lysis with a recombinant bacteriophage endolysin. Appl. Environ. Microbiol. 61:1150-1152.
    • (1995) Appl. Environ. Microbiol. , vol.61 , pp. 1150-1152
    • Loessner, M.J.1    Schneider, A.2    Scherer, S.3
  • 19
    • 0029122651 scopus 로고
    • Heterogeneous endolysins in Listeria monocytogenes bacteriophages: A new class of enzymes and evidence for conserved holin genes within the siphoviral lysis cassettes
    • Loessner, M. J., G. Wendlinger, and S. Scherer. 1995. Heterogeneous endolysins in Listeria monocytogenes bacteriophages: A new class of enzymes and evidence for conserved holin genes within the siphoviral lysis cassettes. Mol. Microbiol. 16:1231-1241.
    • (1995) Mol. Microbiol. , vol.16 , pp. 1231-1241
    • Loessner, M.J.1    Wendlinger, G.2    Scherer, S.3
  • 20
    • 0035132749 scopus 로고    scopus 로고
    • Severely impaired production performance in broiler flocks with high incidence of Clostridium perfringens-associated hepatitis
    • Lovland, A., and M. Kaldhusdal. 2001. Severely impaired production performance in broiler flocks with high incidence of Clostridium perfringens-associated hepatitis. Avian Pathol. 30:73-81.
    • (2001) Avian Pathol. , vol.30 , pp. 73-81
    • Lovland, A.1    Kaldhusdal, M.2
  • 21
    • 0033604287 scopus 로고    scopus 로고
    • Similarly organized lysogeny modules in temperate Siphoviridae from low GC content gram-positive bacteria
    • Lucchini, S., F. Desiere, and H. Brüssow. 1999. Similarly organized lysogeny modules in temperate Siphoviridae from low GC content gram-positive bacteria. Virology 263:427-435.
    • (1999) Virology , vol.263 , pp. 427-435
    • Lucchini, S.1    Desiere, F.2    Brüssow, H.3
  • 22
    • 0028225456 scopus 로고
    • Identification and molecular analysis of a locus that regulates extracellular toxin production in Clostridium perfringens
    • Lyristis, M., A. E. Bryant, J. Sloan, M. M. Awad, I. T. Nisbet, D. L. Stevens, and J. I. Rood. 1994. Identification and molecular analysis of a locus that regulates extracellular toxin production in Clostridium perfringens. Mol. Microbiol. 12:761-777.
    • (1994) Mol. Microbiol. , vol.12 , pp. 761-777
    • Lyristis, M.1    Bryant, A.E.2    Sloan, J.3    Awad, M.M.4    Nisbet, I.T.5    Stevens, D.L.6    Rood, J.I.7
  • 23
    • 0001835253 scopus 로고    scopus 로고
    • Clostridium perfringens
    • M. P. Doyle, L. R. Beuchat, and T. J. Montville (ed.). ASM Press, Washington, D.C.
    • McClane, B. A. 2001. Clostridium perfringens, p. 351-372. In M. P. Doyle, L. R. Beuchat, and T. J. Montville (ed.), Food Microbiology: Fundamentals and Frontiers, 2nd Ed. ASM Press, Washington, D.C.
    • (2001) Food Microbiology: Fundamentals and Frontiers, 2nd Ed. , pp. 351-372
    • McClane, B.A.1
  • 24
    • 0032969566 scopus 로고    scopus 로고
    • Surface proteins of gram-positive bacteria and mechanisms of their targeting to the cell wall envelope
    • Navarre, W. W., and O. Schneewind. 1999. Surface proteins of gram-positive bacteria and mechanisms of their targeting to the cell wall envelope. Microbiol. Mol. Biol. Rev. 63:174-229.
    • (1999) Microbiol. Mol. Biol. Rev. , vol.63 , pp. 174-229
    • Navarre, W.W.1    Schneewind, O.2
  • 25
    • 0035957329 scopus 로고    scopus 로고
    • Prevention and elimination of upper respiratory colonization of mice by group A streptococci by using a bacteriophage lytic enzyme
    • Nelson, D., L. Loomis, and V. A. Fischetti. 2001. Prevention and elimination of upper respiratory colonization of mice by group A streptococci by using a bacteriophage lytic enzyme. Proc. Natl. Acad. Sci. USA 98:4107-4112.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 4107-4112
    • Nelson, D.1    Loomis, L.2    Fischetti, V.A.3
  • 27
    • 0015462556 scopus 로고
    • Peptidoglycan types of bacterial cell walls and their taxonomic implications
    • Schleifer, K. H., and O. Kandler. 1972. Peptidoglycan types of bacterial cell walls and their taxonomic implications. Bacteriol. Rev. 36:407-477.
    • (1972) Bacteriol. Rev. , vol.36 , pp. 407-477
    • Schleifer, K.H.1    Kandler, O.2
  • 28
    • 0028203277 scopus 로고
    • The virR gene, a member of a class of two-component response regulators, regulates the production of perfringolysin O, collagenase, and hemagglutinin in Clostridium perfringens
    • Shimizu, T., W. Ba-Thein, M. Tamaki, and H. Hayashi. 1994. The virR gene, a member of a class of two-component response regulators, regulates the production of perfringolysin O, collagenase, and hemagglutinin in Clostridium perfringens. J. Bacteriol. 176:1616-1623.
    • (1994) J. Bacteriol. , vol.176 , pp. 1616-1623
    • Shimizu, T.1    Ba-Thein, W.2    Tamaki, M.3    Hayashi, H.4
  • 29
    • 0029915545 scopus 로고    scopus 로고
    • Clostridial enteric diseases of domestic animals
    • Songer, J. G. 1996. Clostridial enteric diseases of domestic animals. Clin. Microbiol. Rev. 9:216-234.
    • (1996) Clin. Microbiol. Rev. , vol.9 , pp. 216-234
    • Songer, J.G.1
  • 32
    • 0002449232 scopus 로고    scopus 로고
    • Phylogenetic relationships
    • J. I. Rood, B. A. McClane, J. G. Songer, and R. W. Titball (ed.). Academic Press, Inc., San Diego, Calif.
    • Stackebrandt, E., and F. A. Rainey. 1997. Phylogenetic relationships, p. 3-19. In J. I. Rood, B. A. McClane, J. G. Songer, and R. W. Titball (ed.), The Clostridia: Molecular Biology and Pathogenesis. Academic Press, Inc., San Diego, Calif.
    • (1997) The Clostridia: Molecular Biology and Pathogenesis , pp. 3-19
    • Stackebrandt, E.1    Rainey, F.A.2
  • 33
    • 0002575215 scopus 로고    scopus 로고
    • Necrotizing clostridial soft tissue infections
    • J. I. Rood, B. A. McClane, J. G. Songer, and R. W. Titball (ed.). Academic Press, Inc., San Diego, Calif.
    • Stevens, D. L. 1997. Necrotizing clostridial soft tissue infections, p. 141-151. In J. I. Rood, B. A. McClane, J. G. Songer, and R. W. Titball (ed.), The Clostridia: Molecular Biology and Pathogenesis. Academic Press, Inc., San Diego, Calif.
    • (1997) The Clostridia: Molecular Biology and Pathogenesis , pp. 141-151
    • Stevens, D.L.1
  • 34
    • 0034769921 scopus 로고    scopus 로고
    • Bacteriophage therapy
    • Summers, W. C. 2001. Bacteriophage therapy. Annu. Rev. Microbiol. 55:437-451.
    • (2001) Annu. Rev. Microbiol. , vol.55 , pp. 437-451
    • Summers, W.C.1
  • 35
    • 0026716643 scopus 로고
    • Membrane protein structure prediction. Hydrophobicity analysis and the positive-inside rule
    • von Heijne, G. 1992. Membrane protein structure prediction. Hydrophobicity analysis and the positive-inside rule. J. Mol. Biol. 225:487-494.
    • (1992) J. Mol. Biol. , vol.225 , pp. 487-494
    • Von Heijne, G.1
  • 36
    • 0034654341 scopus 로고    scopus 로고
    • Functional analysis of heterologous holin proteins in a λΔS genetic background
    • Vukov, N., S. Scherer, E. Hibbert, and M. J. Loessner. 2000. Functional analysis of heterologous holin proteins in a λΔS genetic background. FEMS Microbiol. Lett. 184:179-186.
    • (2000) FEMS Microbiol. Lett. , vol.184 , pp. 179-186
    • Vukov, N.1    Scherer, S.2    Hibbert, E.3    Loessner, M.J.4
  • 37
    • 0033768655 scopus 로고    scopus 로고
    • Holins: The protein clocks of bacteriophage infections
    • Wang, I. N., D. L. Smith, and R. Young. 2000. Holins: The protein clocks of bacteriophage infections. Annu. Rev. Microbiol. 54:799-825.
    • (2000) Annu. Rev. Microbiol. , vol.54 , pp. 799-825
    • Wang, I.N.1    Smith, D.L.2    Young, R.3
  • 38
    • 0033042407 scopus 로고    scopus 로고
    • Use of antimicrobial growth promoters in food animals and Enterococcus faecium resistance to therapeutic antimicrobial drugs in Europe
    • Wegener, H. C., F. M. Aarestrup, L. B. Jensen, A. M. Hammerum, and F. Bager. 1999. Use of antimicrobial growth promoters in food animals and Enterococcus faecium resistance to therapeutic antimicrobial drugs in Europe. Emerg. Infect. Dis. 5:329-335.
    • (1999) Emerg. Infect. Dis. , vol.5 , pp. 329-335
    • Wegener, H.C.1    Aarestrup, F.M.2    Jensen, L.B.3    Hammerum, A.M.4    Bager, F.5
  • 39
    • 0032512458 scopus 로고    scopus 로고
    • Medical consequences of antibiotic use in agriculture
    • Witte, W. 1998. Medical consequences of antibiotic use in agriculture. Science 279:996-997.
    • (1998) Science , vol.279 , pp. 996-997
    • Witte, W.1
  • 40
    • 0026800935 scopus 로고
    • Bacteriophage lysis: Mechanism and regulation
    • Young, R. 1992. Bacteriophage lysis: Mechanism and regulation. Microbiol. Rev. 56:430-481.
    • (1992) Microbiol. Rev. , vol.56 , pp. 430-481
    • Young, R.1
  • 41
    • 0029097918 scopus 로고
    • Holins: Form and function in bacteriophage lysis
    • Young, R., and U. Bläsi. 1995. Holins: Form and function in bacteriophage lysis. FEMS Microbiol. Rev. 17:191-205.
    • (1995) FEMS Microbiol. Rev. , vol.17 , pp. 191-205
    • Young, R.1    Bläsi, U.2
  • 42
    • 0033854940 scopus 로고    scopus 로고
    • Simple and efficient method for heterologous expression of clostridial proteins
    • Zdanovsky, A. G., and M. V. Zdanovskaia. 2000. Simple and efficient method for heterologous expression of clostridial proteins. Appl. Environ. Microbiol. 66:3166-3173.
    • (2000) Appl. Environ. Microbiol. , vol.66 , pp. 3166-3173
    • Zdanovsky, A.G.1    Zdanovskaia, M.V.2
  • 43
    • 0036334441 scopus 로고    scopus 로고
    • Genomic analysis of Clostridium perfringens bacteriophage φ3626, which integrates into guaA and possibly affects sporulation
    • Zimmer, M., S. Scherer, and M. J. Loessner. 2002. Genomic analysis of Clostridium perfringens bacteriophage φ3626, which integrates into guaA and possibly affects sporulation. J. Bacteriol. 184:4359-4368.
    • (2002) J. Bacteriol. , vol.184 , pp. 4359-4368
    • Zimmer, M.1    Scherer, S.2    Loessner, M.J.3


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