메뉴 건너뛰기




Volumn 90, Issue 6, 2011, Pages 1973-1979

Identification and characterization of a putative endolysin encoded by episomal phage phiSM101 of Clostridium perfringens

Author keywords

Bacteriophage; Clostridium perfringens; Endolysin; N acetylmuramidase; N acetylmuramoyl L alanine amidase

Indexed keywords

AMIDASE; ANION EXCHANGE CHROMATOGRAPHY; CATALYTIC DOMAINS; CLOSTRIDIUM PERFRINGENS; ENDOLYSIN; ENTEROTOXIGENIC; HOMOLOGOUS GENES; IMMOBILIZED METAL AFFINITY CHROMATOGRAPHY; LYTIC ENZYMES; N-ACETYLMURAMIDASE; N-TERMINALS; PURIFIED ENZYME; TURBIDITY REDUCTION;

EID: 79958215234     PISSN: 01757598     EISSN: 14320614     Source Type: Journal    
DOI: 10.1007/s00253-011-3253-z     Document Type: Article
Times cited : (39)

References (36)
  • 1
    • 0036895178 scopus 로고    scopus 로고
    • Trends in indigenous foodborne disease and deaths, England and Wales: 1992 to 2000
    • Adak GK, Long SM, O'Brien SJ (2002) Trends in indigenous foodborne disease and deaths, England and Wales: 1992 to 2000. Gut 51:832-841
    • (2002) Gut , vol.51 , pp. 832-841
    • Adak, G.K.1    Long, S.M.2    O'Brien, S.J.3
  • 2
    • 33646247394 scopus 로고    scopus 로고
    • Clostridium perfringens phospholipase C-induced platelet/leukocyte interactions impede neutrophil diapedesis
    • Bryant AE, Bayer CR, Aldape MJ, Wallace RJ, Titball RW, Stevens DL (2006) Clostridium perfringens phospholipase C-induced platelet/leukocyte interactions impede neutrophil diapedesis. J Med Microbiol 55:495-504
    • (2006) J Med Microbiol , vol.55 , pp. 495-504
    • Bryant, A.E.1    Bayer, C.R.2    Aldape, M.J.3    Wallace, R.J.4    Titball, R.W.5    Stevens, D.L.6
  • 3
    • 0030924599 scopus 로고    scopus 로고
    • Molecular characterization of a germination-specific muramidase from Clostridium perfringens S40 spores and nucleotide sequence of the corresponding gene
    • Chen Y, Miyata S, Makino S, Moriyama R (1997) Molecular characterization of a germination-specific muramidase from Clostridium perfringens S40 spores and nucleotide sequence of the corresponding gene. J Bacteriol 179:3181-3187 (Pubitemid 27202991)
    • (1997) Journal of Bacteriology , vol.179 , Issue.10 , pp. 3181-3187
    • Chen, Y.1    Miyata, S.2    Makino, S.3    Moriyama, R.4
  • 4
    • 61549096565 scopus 로고    scopus 로고
    • Necrotic enteritis in chickens: A paradigm of enteric infection by Clostridium perfringens type A
    • Cooper KK, Songer JG (2009) Necrotic enteritis in chickens: a paradigm of enteric infection by Clostridium perfringens type A. Anaerobe 15:55-60
    • (2009) Anaerobe , vol.15 , pp. 55-60
    • Cooper, K.K.1    Songer, J.G.2
  • 5
    • 62149112257 scopus 로고    scopus 로고
    • Production and application of bacteriophage and bacteriophage-encoded lysins
    • Courchesne NM, Parisien A, Lan CQ (2009) Production and application of bacteriophage and bacteriophage-encoded lysins. Recent Pat Biotechnol 3:37-45
    • (2009) Recent Pat Biotechnol , vol.3 , pp. 37-45
    • Courchesne, N.M.1    Parisien, A.2    Lan, C.Q.3
  • 6
    • 0026591303 scopus 로고
    • Purification and characterization of an extracellular muramidase of Clostridium acetobutylicum ATCC824 that acts on non-N-acetylated peptidoglycan
    • Croux C, Canard B, Goma G, Soucaille P (1992) Purification and characterization of an extracellular muramidase of Clostridium acetobutylicum ATCC824 that acts on non-N-acetylated peptidoglycan. Appl Environ Microbiol 58:1075-1081
    • (1992) Appl Environ Microbiol , vol.58 , pp. 1075-1081
    • Croux, C.1    Canard, B.2    Goma, G.3    Soucaille, P.4
  • 8
    • 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
  • 9
    • 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
  • 10
    • 19344374675 scopus 로고    scopus 로고
    • Antimicrobial resistance determinants and future control
    • Harbarth S, Samore MH (2005) Antimicrobial resistance determinants and future control. Emerg Infect Dis 11:794-801 (Pubitemid 40720837)
    • (2005) Emerging Infectious Diseases , vol.11 , Issue.6 , pp. 794-801
    • Harbarth, S.1    Samore, M.H.2
  • 11
    • 0037350314 scopus 로고    scopus 로고
    • Characterization of AcmB, an N-acetylglucosaminidase autolysin from Lactococcus lactis
    • DOI 10.1099/mic.0.25875-0
    • Huard C, Miranda G, Wessner F, Bolotin A, Hansen J, Foster SJ, Chapot-Chartier MP (2003) Characterization of AcmB, an N-acetylglucosaminidase autolysin from Lactococcus lactis. Microbiology 149:695-705 (Pubitemid 36395104)
    • (2003) Microbiology , vol.149 , Issue.3 , pp. 695-705
    • Huard, C.1    Miranda, G.2    Wessner, F.3    Bolotin, A.4    Hansen, J.5    Foster, S.J.6    Chapot-Chartier, M.-P.7
  • 12
    • 52349103639 scopus 로고    scopus 로고
    • Diversity of Firmicutes peptidoglycan hydrolases and specificities of those involved in daughter cell separation
    • Layec S, Decaris B, Leblond-Bourget N (2008) Diversity of Firmicutes peptidoglycan hydrolases and specificities of those involved in daughter cell separation. Res Microbiol 159:507-515
    • (2008) Res Microbiol , vol.159 , pp. 507-515
    • Layec, S.1    Decaris, B.2    Leblond-Bourget, N.3
  • 13
    • 0037224191 scopus 로고    scopus 로고
    • Synergistic lethal effect of a combination of phage lytic enzymes with different activities on penicillin-sensitive and -resistant Streptococcus pneumoniae strains
    • DOI 10.1128/AAC.47.1.375-377.2003
    • Loeffler JM, Fischetti VA (2003) Synergistic lethal effect of a combination of phage lytic enzymes with different activities on penicillin-sensitive and -resistant Streptococcus pneumoniae strains. Antimicrob Agents Chemother 47:375-377 (Pubitemid 36070389)
    • (2003) Antimicrobial Agents and Chemotherapy , vol.47 , Issue.1 , pp. 375-377
    • Loeffler, J.M.1    Fischetti, V.A.2
  • 14
    • 0035824437 scopus 로고    scopus 로고
    • Rapid killing of Streptococcus pneumoniae with a bacteriophage cell wall hydrolase
    • DOI 10.1126/science.1066869
    • Loeffler JM, Nelson D, Fischetti VA (2001) Rapid killing of Streptococcus pneumoniae with a bacteriophage cell wall hydrolase. Science 294:2170-2172 (Pubitemid 33150674)
    • (2001) Science , vol.294 , Issue.5549 , pp. 2170-2172
    • Loeffler, J.M.1    Nelson, D.2    Fischetti, V.A.3
  • 15
    • 0242286566 scopus 로고    scopus 로고
    • Phage Lytic Enzyme Cpl-1 as a Novel Antimicrobial for Pneumococcal Bacteremia
    • DOI 10.1128/IAI.71.11.6199-6204.2003
    • Loeffler JM, Djurkovic S, Fischetti VA (2003) Phage lytic enzyme Cpl-1 as a novel antimicrobial for pneumococcal bacteremia. Infect Immun 71:6199-6204 (Pubitemid 37337675)
    • (2003) Infection and Immunity , vol.71 , Issue.11 , pp. 6199-6204
    • Loeffler, J.M.1    Djurkovic, S.2    Fischetti, V.A.3
  • 19
    • 26944443097 scopus 로고    scopus 로고
    • Identification of a protein Ser/Thr kinase cascade that regulates essential transcriptional activators in Myxococcus xanthus development
    • DOI 10.1111/j.1365-2958.2005.04826.x
    • Nariya H, Inouye S (2005) Identification of a protein Ser/Thr kinase cascade that regulates essential transcriptional activators in Myxococcus xanthus development. Mol Microbiol 58:367-379 (Pubitemid 41476155)
    • (2005) Molecular Microbiology , vol.58 , Issue.2 , pp. 367-379
    • Nariya, H.1    Inouye, S.2
  • 20
    • 79953204649 scopus 로고    scopus 로고
    • Development and application of a method for counterselectable in-frame deletion in Clostridium perfringens
    • Nariya H, Miyata S, Suzuki M, Tamai E, Okabe A (2011) Development and application of a method for counterselectable in-frame deletion in Clostridium perfringens. Appl Environ Microbiol 77:1375-1382
    • (2011) Appl Environ Microbiol , vol.77 , pp. 1375-1382
    • Nariya, H.1    Miyata, S.2    Suzuki, M.3    Tamai, E.4    Okabe, A.5
  • 22
    • 12944302098 scopus 로고    scopus 로고
    • Lack of development of new antimicrobial drugs: A potential serious threat to public health
    • DOI 10.1016/S1473-3099(05)01283-1, PII S1473309905012831
    • Norrby SR, Nord CE, Finch R, European Society of Clinical Microbiology and Infectious Diseases (2005) Lack of development of new antimicrobial drugs: a potential serious threat to public health. Lancet Infect Dis 5:115-119 (Pubitemid 40174782)
    • (2005) Lancet Infectious Diseases , vol.5 , Issue.2 , pp. 115-119
    • Norrby, S.R.1    Nord, C.E.2    Finch, R.3
  • 23
    • 66749132773 scopus 로고    scopus 로고
    • Bacteriophage and their lysins for elimination of infectious bacteria
    • O'Flaherty S, Ross RP, Coffey A (2009) Bacteriophage and their lysins for elimination of infectious bacteria. FEMS Microbiol Rev 33:801-881
    • (2009) FEMS Microbiol Rev , vol.33 , pp. 801-881
    • O'Flaherty, S.1    Ross, R.P.2    Coffey, A.3
  • 24
    • 0033105216 scopus 로고    scopus 로고
    • Clostridium perfringens: Toxinotype and genotype
    • Petit L, Gibert M, Popoff MR (1999) Clostridium perfringens: toxinotype and genotype. Trends Microbiol 7:104-710
    • (1999) Trends Microbiol , vol.7 , pp. 104-710
    • Petit, L.1    Gibert, M.2    Popoff, M.R.3
  • 27
    • 0035943705 scopus 로고    scopus 로고
    • A new lysozyme fold. Crystal structure of the muramidase from Streptomyces coelicolor at 1.65 Å resolution
    • Rau A, Hogg T, Marquardt R, Hilgenfeld R (2001) A new lysozyme fold. Crystal structure of the muramidase from Streptomyces coelicolor at 1.65 Å resolution. J Biol Chem 276:31994-31999
    • (2001) J Biol Chem , vol.276 , pp. 31994-31999
    • Rau, A.1    Hogg, T.2    Marquardt, R.3    Hilgenfeld, R.4
  • 29
    • 0031392579 scopus 로고    scopus 로고
    • Structure of the capsular polysaccharide of Clostridium perfringens Hobbs 10 determined by NMR spectroscopy
    • Sheng S, Cherniak R (1998) Structure of the capsular polysaccharide of Clostridium perfringens Hobbs 10 determined by NMR spectroscopy. Carbohydr Res 305:65-72
    • (1998) Carbohydr Res , vol.305 , pp. 65-72
    • Sheng, S.1    Cherniak, R.2
  • 32
    • 37249051379 scopus 로고    scopus 로고
    • Construction and characterization of a clostripain-like protease-deficient mutant of Clostridium perfringens as a strain for clostridial gene expression
    • DOI 10.1007/s00253-007-1245-9
    • Tanaka H, Tamai E, Miyata S, Taniguchi Y, Nariya H, Hatano N, Houchi H, Okabe A (2008) Construction and characterization of a clostripain-like protease-deficient mutant of Clostridium perfringens as a strain for clostridial gene expression. Appl Microbiol Biotechnol 277:1063-1071 (Pubitemid 350264445)
    • (2008) Applied Microbiology and Biotechnology , vol.77 , Issue.5 , pp. 1063-1071
    • Tanaka, H.1    Tamai, E.2    Miyata, S.3    Taniguchi, Y.4    Nariya, H.5    Hatano, N.6    Houchi, H.7    Okabe, A.8
  • 33
    • 78650169460 scopus 로고    scopus 로고
    • High-level production and purification of clostripain expressed in a virulence-attenuated strain of Clostridium perfringens
    • Tanaka H, Nariya H, Suzuki M, Houchi H, Tamai E, Miyata S, Okabe A (2011) High-level production and purification of clostripain expressed in a virulence-attenuated strain of Clostridium perfringens. Protein Expr Purif 76:83-89
    • (2011) Protein Expr Purif , vol.76 , pp. 83-89
    • Tanaka, H.1    Nariya, H.2    Suzuki, M.3    Houchi, H.4    Tamai, E.5    Miyata, S.6    Okabe, A.7
  • 35
    • 0033768655 scopus 로고    scopus 로고
    • Holins: The protein clocks of bacteriophage infections
    • Wang IN, Smith DL, Young R (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
  • 36
    • 0036840423 scopus 로고    scopus 로고
    • The murein hydrolase of the bacteriophage phi3626 dual lysis system is active against all tested Clostridium perfringens strains
    • Zimmer M, Vukov N, Scherer S, Loessner MJ (2002) The murein hydrolase of the bacteriophage phi3626 dual lysis system is active against all tested Clostridium perfringens strains. Appl Environ Microbiol 68:5311-5317 (Pubitemid 35265662)
    • (2002) Applied and Environmental Microbiology , vol.68 , Issue.11 , pp. 5311-5317
    • Zimmer, M.1    Vukov, N.2    Scherer, S.3    Loessner, M.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.