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Volumn 332, Issue 1, 2012, Pages 76-83

Characterization of an endolysin, LysBPS13, from a Bacillus cereus bacteriophage

Author keywords

Bacillus cereus; Endolysin; N acetylmuramyl l alanine amidase

Indexed keywords

AMINO TERMINAL SEQUENCE; ARTICLE; BACILLUS CEREUS; BACTERIAL GENE; BACTERIAL GROWTH; BACTERIAL STRAIN; BACTERIOPHAGE; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; ENDOLYSIN GENE; ENZYME ACTIVITY; IONIC STRENGTH; NONHUMAN; NUCLEOTIDE SEQUENCE; OPEN READING FRAME; PH; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN MOTIF; TEMPERATURE; THERMOSTABILITY;

EID: 84862259899     PISSN: 03781097     EISSN: 15746968     Source Type: Journal    
DOI: 10.1111/j.1574-6968.2012.02578.x     Document Type: Article
Times cited : (46)

References (39)
  • 1
    • 0038403691 scopus 로고    scopus 로고
    • The CHAP domain: a large family of amidases including GSP amidase and peptidoglycan hydrolases
    • Bateman A & Rawlings ND (2003) The CHAP domain: a large family of amidases including GSP amidase and peptidoglycan hydrolases. Trends Biochem Sci 28: 234-237.
    • (2003) Trends Biochem Sci , vol.28 , pp. 234-237
    • Bateman, A.1    Rawlings, N.D.2
  • 2
    • 33645227952 scopus 로고    scopus 로고
    • Bacteriophage endolysins as a novel class of antibacterial agents
    • Borysowski J, Weber-Dabrowska B & Gorski A (2006) Bacteriophage endolysins as a novel class of antibacterial agents. Exp Biol Med 231: 366-377.
    • (2006) Exp Biol Med , vol.231 , pp. 366-377
    • Borysowski, J.1    Weber-Dabrowska, B.2    Gorski, A.3
  • 3
    • 77950658604 scopus 로고    scopus 로고
    • Bacillus cereus, a volatile human pathogen
    • Bottone EJ (2010) Bacillus cereus, a volatile human pathogen. Clin Microbiol Rev 23: 382-398.
    • (2010) Clin Microbiol Rev , vol.23 , pp. 382-398
    • Bottone, E.J.1
  • 4
    • 79958281245 scopus 로고    scopus 로고
    • A second endolysin gene is fully embedded in-frame with the lysA gene of mycobacteriophage Ms6
    • Catalao MJ, Milho C, Gil F et al. (2011) A second endolysin gene is fully embedded in-frame with the lysA gene of mycobacteriophage Ms6. PLoS ONE 6: e20515.
    • (2011) PLoS ONE , vol.6
    • Catalao, M.J.1    Milho, C.2    Gil, F.3
  • 5
    • 79959722500 scopus 로고    scopus 로고
    • Regulation of toxin production by Bacillus cereus and its food safety implications
    • Ceuppens S, Rajkovic A, Heyndrickx M et al. (2011) Regulation of toxin production by Bacillus cereus and its food safety implications. Crit Rev Microbiol 37: 188-213.
    • (2011) Crit Rev Microbiol , vol.37 , pp. 188-213
    • Ceuppens, S.1    Rajkovic, A.2    Heyndrickx, M.3
  • 6
    • 0028223308 scopus 로고
    • The structure of bacteriophage T7 lysozyme, a zinc amidase and an inhibitor of T7 RNA polymerase
    • Cheng X, Zhang X, Pflugrath JW & Studier FW (1994) The structure of bacteriophage T7 lysozyme, a zinc amidase and an inhibitor of T7 RNA polymerase. P Natl Acad Sci USA 91: 4034-4038.
    • (1994) P Natl Acad Sci USA , vol.91 , pp. 4034-4038
    • Cheng, X.1    Zhang, X.2    Pflugrath, J.W.3    Studier, F.W.4
  • 7
    • 0348048803 scopus 로고    scopus 로고
    • Peptidoglycan recognition proteins (PGRPs)
    • Dziarski R (2004) Peptidoglycan recognition proteins (PGRPs). Mol Immunol 40: 877-886.
    • (2004) Mol Immunol , vol.40 , pp. 877-886
    • Dziarski, R.1
  • 8
    • 33845586621 scopus 로고    scopus 로고
    • The peptidoglycan recognition proteins (PGRPs)
    • Dziarski R & Gupta D (2006) The peptidoglycan recognition proteins (PGRPs). Genome Biol 7: 232.
    • (2006) Genome Biol , vol.7 , pp. 232
    • Dziarski, R.1    Gupta, D.2
  • 9
    • 72949120004 scopus 로고    scopus 로고
    • Influence of glycerol on the structure and thermal stability of lysozyme: a dynamic light scattering and circular dichroism study
    • Esposito A, Comez L, Cinelli S et al. (2009) Influence of glycerol on the structure and thermal stability of lysozyme: a dynamic light scattering and circular dichroism study. J Phys Chem B 113: 16420-16424.
    • (2009) J Phys Chem B , vol.113 , pp. 16420-16424
    • Esposito, A.1    Comez, L.2    Cinelli, S.3
  • 10
    • 24944587206 scopus 로고    scopus 로고
    • Bacteriophage lytic enzymes: novel anti-infectives
    • Fischetti VA (2005) Bacteriophage lytic enzymes: novel anti-infectives. Trends Microbiol 13: 491-496.
    • (2005) Trends Microbiol , vol.13 , pp. 491-496
    • Fischetti, V.A.1
  • 11
    • 55049135817 scopus 로고    scopus 로고
    • Bacteriophage lysins as effective antibacterials
    • Fischetti VA (2008) Bacteriophage lysins as effective antibacterials. Curr Opin Microbiol 11: 393-400.
    • (2008) Curr Opin Microbiol , vol.11 , pp. 393-400
    • Fischetti, V.A.1
  • 12
    • 77955557492 scopus 로고    scopus 로고
    • Bacteriophage endolysins: a novel anti-infective to control Gram-positive pathogens
    • Fischetti VA (2010) Bacteriophage endolysins: a novel anti-infective to control Gram-positive pathogens. Int J Med Microbiol 300: 357-362.
    • (2010) Int J Med Microbiol , vol.300 , pp. 357-362
    • Fischetti, V.A.1
  • 13
    • 0037757622 scopus 로고    scopus 로고
    • A mammalian peptidoglycan recognition protein with N-acetylmuramoyl-L-alanine amidase activity
    • Gelius E, Persson C, Karlsson J & Steiner H (2003) A mammalian peptidoglycan recognition protein with N-acetylmuramoyl-L-alanine amidase activity. Biochem Biophys Res Commun 306: 988-994.
    • (2003) Biochem Biophys Res Commun , vol.306 , pp. 988-994
    • Gelius, E.1    Persson, C.2    Karlsson, J.3    Steiner, H.4
  • 14
    • 0031573776 scopus 로고    scopus 로고
    • Bacillus cereus and its food poisoning toxins
    • Granum PE & Lund T (1997) Bacillus cereus and its food poisoning toxins. FEMS Microbiol Lett 157: 223-228.
    • (1997) FEMS Microbiol Lett , vol.157 , pp. 223-228
    • Granum, P.E.1    Lund, T.2
  • 15
    • 0016239643 scopus 로고
    • A simple method for the quantitative determination of muramic acid
    • Hadzija O (1974) A simple method for the quantitative determination of muramic acid. Anal Biochem 60: 512-517.
    • (1974) Anal Biochem , vol.60 , pp. 512-517
    • Hadzija, O.1
  • 16
    • 34250892577 scopus 로고    scopus 로고
    • Bacteriophages: an appraisal of their role in the treatment of bacterial infections
    • Hanlon GW (2007) Bacteriophages: an appraisal of their role in the treatment of bacterial infections. Int J Antimicrob Agents 30: 118-128.
    • (2007) Int J Antimicrob Agents , vol.30 , pp. 118-128
    • Hanlon, G.W.1
  • 17
    • 0026507746 scopus 로고
    • Assay for N-acetylmuramyl-L-alanine amidase in serum by determination of muramic acid released from the peptidoglycan of Brevibacterium divaricatum
    • Hazenberg MP & de Visser H (1992) Assay for N-acetylmuramyl-L-alanine amidase in serum by determination of muramic acid released from the peptidoglycan of Brevibacterium divaricatum. Eur J Clin Chem Clin Biochem 30: 141-144.
    • (1992) Eur J Clin Chem Clin Biochem , vol.30 , pp. 141-144
    • Hazenberg, M.P.1    de Visser, H.2
  • 18
    • 35948990424 scopus 로고    scopus 로고
    • Taking aim on bacterial pathogens: from phage therapy to enzybiotics
    • Hermoso JA, Garcia JL & Garcia P (2007) Taking aim on bacterial pathogens: from phage therapy to enzybiotics. Curr Opin Microbiol 10: 461-472.
    • (2007) Curr Opin Microbiol , vol.10 , pp. 461-472
    • Hermoso, J.A.1    Garcia, J.L.2    Garcia, P.3
  • 19
    • 0042195829 scopus 로고    scopus 로고
    • Crystal structure of peptidoglycan recognition protein LB from Drosophila melanogaster
    • Kim MS, Byun M & Oh BH (2003) Crystal structure of peptidoglycan recognition protein LB from Drosophila melanogaster. Nat Immunol 4: 787-793.
    • (2003) Nat Immunol , vol.4 , pp. 787-793
    • Kim, M.S.1    Byun, M.2    Oh, B.H.3
  • 20
    • 0017376602 scopus 로고
    • Purification and characterization of the lytic enzyme N-acetylmuramyl-L-alanine amidase of bacteriophage T7
    • Kleppe G, Jensen HB & Pryme IF (1977) Purification and characterization of the lytic enzyme N-acetylmuramyl-L-alanine amidase of bacteriophage T7. Eur J Biochem 76: 317-326.
    • (1977) Eur J Biochem , vol.76 , pp. 317-326
    • Kleppe, G.1    Jensen, H.B.2    Pryme, I.F.3
  • 21
    • 0025011966 scopus 로고
    • Cloning, sequencing and genetic mapping of a Bacillus subtilis cell wall hydrolase gene
    • Kuroda A & Sekiguchi J (1990) Cloning, sequencing and genetic mapping of a Bacillus subtilis cell wall hydrolase gene. J Gen Microbiol 136: 2209-2216.
    • (1990) J Gen Microbiol , vol.136 , pp. 2209-2216
    • Kuroda, A.1    Sekiguchi, J.2
  • 22
    • 11144252652 scopus 로고    scopus 로고
    • Identification and characterization of a highly thermostable bacteriophage lysozyme
    • Lavigne R, Briers Y, Hertveldt K et al. (2004) Identification and characterization of a highly thermostable bacteriophage lysozyme. Cell Mol Life Sci 61: 2753-2759.
    • (2004) Cell Mol Life Sci , vol.61 , pp. 2753-2759
    • Lavigne, R.1    Briers, Y.2    Hertveldt, K.3
  • 23
    • 0242286566 scopus 로고    scopus 로고
    • Phage lytic enzyme Cpl-1 as a novel antimicrobial for pneumococcal bacteremia
    • Loeffler JM, Djurkovic S & Fischetti VA (2003) Phage lytic enzyme Cpl-1 as a novel antimicrobial for pneumococcal bacteremia. Infect Immun 71: 6199-6204.
    • (2003) Infect Immun , vol.71 , pp. 6199-6204
    • Loeffler, J.M.1    Djurkovic, S.2    Fischetti, V.A.3
  • 24
    • 22544471225 scopus 로고    scopus 로고
    • Bacteriophage endolysins-current state of research and applications
    • Loessner MJ (2005) Bacteriophage endolysins-current state of research and applications. Curr Opin Microbiol 8: 480-487.
    • (2005) Curr Opin Microbiol , vol.8 , pp. 480-487
    • Loessner, M.J.1
  • 25
    • 0030894847 scopus 로고    scopus 로고
    • Three Bacillus cereus bacteriophage endolysins are unrelated but reveal high homology to cell wall hydrolases from different bacilli
    • Loessner MJ, Maier SK, Daubek-Puza H et al. (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
  • 26
    • 0024284222 scopus 로고
    • A new and fast method for preparing high quality lambda DNA suitable for sequencing
    • Manfioletti G & Schneider C (1988) A new and fast method for preparing high quality lambda DNA suitable for sequencing. Nucleic Acids Res 16: 2873-2884.
    • (1988) Nucleic Acids Res , vol.16 , pp. 2873-2884
    • Manfioletti, G.1    Schneider, C.2
  • 27
    • 78651285748 scopus 로고    scopus 로고
    • CDD: a Conserved Domain Database for the functional annotation of proteins
    • Marchler-Bauer A, Lu S, Anderson JB et al. (2011) CDD: a Conserved Domain Database for the functional annotation of proteins. Nucleic Acids Res 39: D225-D229.
    • (2011) Nucleic Acids Res , vol.39
    • Marchler-Bauer, A.1    Lu, S.2    Anderson, J.B.3
  • 28
    • 33746087272 scopus 로고    scopus 로고
    • PlyC: a multimeric bacteriophage lysin
    • Nelson D, Schuch R, Chahales P et al. (2006) PlyC: a multimeric bacteriophage lysin. P Natl Acad Sci USA 103: 10765-10770.
    • (2006) P Natl Acad Sci USA , vol.103 , pp. 10765-10770
    • Nelson, D.1    Schuch, R.2    Chahales, P.3
  • 29
    • 55549119928 scopus 로고    scopus 로고
    • Lytic activity of the recombinant staphylococcal bacteriophage PhiH5 endolysin active against Staphylococcus aureus in milk
    • Obeso JM, Martinez B, Rodriguez A & Garcia P (2008) Lytic activity of the recombinant staphylococcal bacteriophage PhiH5 endolysin active against Staphylococcus aureus in milk. Int J Food Microbiol 128: 212-218.
    • (2008) Int J Food Microbiol , vol.128 , pp. 212-218
    • Obeso, J.M.1    Martinez, B.2    Rodriguez, A.3    Garcia, P.4
  • 30
    • 0035997075 scopus 로고    scopus 로고
    • Effect of the environment on the protein dynamical transition: a neutron scattering study
    • Paciaroni A, Cinelli S & Onori G (2002) Effect of the environment on the protein dynamical transition: a neutron scattering study. Biophys J 83: 1157-1164.
    • (2002) Biophys J , vol.83 , pp. 1157-1164
    • Paciaroni, A.1    Cinelli, S.2    Onori, G.3
  • 31
    • 4344600526 scopus 로고    scopus 로고
    • The bifunctional peptidoglycan lysin of Streptococcus agalactiae bacteriophage B30
    • Pritchard DG, Dong S, Baker JR & Engler JA (2004) The bifunctional peptidoglycan lysin of Streptococcus agalactiae bacteriophage B30. Microbiology 150: 2079-2087.
    • (2004) Microbiology , vol.150 , pp. 2079-2087
    • Pritchard, D.G.1    Dong, S.2    Baker, J.R.3    Engler, J.A.4
  • 32
    • 84856294356 scopus 로고    scopus 로고
    • Listeria bacteriophage peptidoglycan hydrolases feature high thermoresistance and reveal increased activity after divalent metal cation substitution
    • Schmelcher M, Waldherr F & Loessner MJ (2012) Listeria bacteriophage peptidoglycan hydrolases feature high thermoresistance and reveal increased activity after divalent metal cation substitution. Appl Microbiol Biotechnol 93: 633-643.
    • (2012) Appl Microbiol Biotechnol , vol.93 , pp. 633-643
    • Schmelcher, M.1    Waldherr, F.2    Loessner, M.J.3
  • 33
    • 84858139801 scopus 로고    scopus 로고
    • Characterization of LysB4, an endolysin from the Bacillus cereus-infecting bacteriophage B4
    • Son B, Yun J, Lim JA et al. (2012) Characterization of LysB4, an endolysin from the Bacillus cereus-infecting bacteriophage B4. BMC Microbiol 12: 33.
    • (2012) BMC Microbiol , vol.12 , pp. 33
    • Son, B.1    Yun, J.2    Lim, J.A.3
  • 34
    • 47849109878 scopus 로고    scopus 로고
    • Microcalorimetric study of thermal unfolding of lysozyme in water/glycerol mixtures: an analysis by solvent exchange model
    • Spinozzi F, Ortore MG, Sinibaldi R et al. (2008) Microcalorimetric study of thermal unfolding of lysozyme in water/glycerol mixtures: an analysis by solvent exchange model. J Chem Phys 129: 035101.
    • (2008) J Chem Phys , vol.129 , pp. 035101
    • Spinozzi, F.1    Ortore, M.G.2    Sinibaldi, R.3
  • 36
    • 79551476231 scopus 로고    scopus 로고
    • Characterization of lytic enzyme open reading frame 9 (ORF9) derived from Enterococcus faecalis bacteriophage phiEF24C
    • Uchiyama J, Takemura I, Hayashi I et al. (2011) Characterization of lytic enzyme open reading frame 9 (ORF9) derived from Enterococcus faecalis bacteriophage phiEF24C. Appl Environ Microbiol 77: 580-585.
    • (2011) Appl Environ Microbiol , vol.77 , pp. 580-585
    • Uchiyama, J.1    Takemura, I.2    Hayashi, I.3
  • 37
    • 0028799370 scopus 로고
    • Genetic and biochemical characterization of the Lactobacillus delbrueckii subsp. lactis bacteriophage LL-H lysin
    • Vasala A, Valkkila M, Caldentey J & Alatossava T (1995) Genetic and biochemical characterization of the Lactobacillus delbrueckii subsp. lactis bacteriophage LL-H lysin. Appl Environ Microbiol 61: 4004-4011.
    • (1995) Appl Environ Microbiol , vol.61 , pp. 4004-4011
    • Vasala, A.1    Valkkila, M.2    Caldentey, J.3    Alatossava, T.4
  • 39
    • 40549088233 scopus 로고    scopus 로고
    • Characterization of a lysin from deep-sea thermophilic bacteriophage GVE2
    • Ye T & Zhang X (2008) Characterization of a lysin from deep-sea thermophilic bacteriophage GVE2. Appl Microbiol Biotechnol 78: 635-641.
    • (2008) Appl Microbiol Biotechnol , vol.78 , pp. 635-641
    • Ye, T.1    Zhang, X.2


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