메뉴 건너뛰기




Volumn 58, Issue 5, 2014, Pages 493-502

Mitrecin A, an endolysin-like bacteriolytic enzyme from a newly isolated soil streptomycete

Author keywords

Antimicrobials; Gene expression; Genomics; Soil; Streptomycetes

Indexed keywords

BACTERIA; CATALYST ACTIVITY; GENE EXPRESSION; RECOMBINANT PROTEINS; SOILS;

EID: 84898847839     PISSN: 02668254     EISSN: 1472765X     Source Type: Journal    
DOI: 10.1111/lam.12220     Document Type: Article
Times cited : (6)

References (46)
  • 1
    • 0026697627 scopus 로고
    • Sequence of the vanY gene required for production of a vancomycin-inducible D, D-carboxypeptidase in Enterococcus faecium BM4147
    • Arthur, M., Molinas, C. and Courvalin, P. (1992) Sequence of the vanY gene required for production of a vancomycin-inducible D, D-carboxypeptidase in Enterococcus faecium BM4147. Gene 120, 111-114.
    • (1992) Gene , vol.120 , pp. 111-114
    • Arthur, M.1    Molinas, C.2    Courvalin, P.3
  • 2
    • 1842611616 scopus 로고    scopus 로고
    • Similar active sites in lysostaphins and D-Ala-D-Ala metallopeptidases
    • Bochtler, M., Odintsov, S.G., Marcyjaniak, M. and Sabala, I. (2004) Similar active sites in lysostaphins and D-Ala-D-Ala metallopeptidases. Protein Sci 13, 854-861.
    • (2004) Protein Sci , vol.13 , pp. 854-861
    • Bochtler, M.1    Odintsov, S.G.2    Marcyjaniak, M.3    Sabala, I.4
  • 4
    • 67649695570 scopus 로고    scopus 로고
    • A hidden reservoir of integrative elements is the major source of recently acquired foreign genes and ORFans in archaeal and bacterial genomes
    • Cortez, D., Forterre, P. and Gribaldo, S. (2009) A hidden reservoir of integrative elements is the major source of recently acquired foreign genes and ORFans in archaeal and bacterial genomes. Genome Biol 10, R65.
    • (2009) Genome Biol , vol.10
    • Cortez, D.1    Forterre, P.2    Gribaldo, S.3
  • 6
    • 80052741109 scopus 로고    scopus 로고
    • The cell wall binding domain of Listeria bacteriophage endolysin PlyP35 recognizes terminal GlcNAc residues in cell wall teichoic acid
    • Eugster, M.R., Haug, M.C., Huwiler, S.G. and Loessner, M.J. (2011) The cell wall binding domain of Listeria bacteriophage endolysin PlyP35 recognizes terminal GlcNAc residues in cell wall teichoic acid. Mol Microbiol 81, 1419-1432.
    • (2011) Mol Microbiol , vol.81 , pp. 1419-1432
    • Eugster, M.R.1    Haug, M.C.2    Huwiler, S.G.3    Loessner, M.J.4
  • 7
    • 80054771169 scopus 로고    scopus 로고
    • Streptomyces scopuliridis sp. nov., a bacteriocin-producing soil streptomycete
    • Farris, M.H., Duffy, C., Findlay, R.H. and Olson, J.B. (2011) Streptomyces scopuliridis sp. nov., a bacteriocin-producing soil streptomycete. Int J Syst Evol Microbiol 61, 2112-2116.
    • (2011) Int J Syst Evol Microbiol , vol.61 , pp. 2112-2116
    • Farris, M.H.1    Duffy, C.2    Findlay, R.H.3    Olson, J.B.4
  • 9
    • 79959931985 scopus 로고    scopus 로고
    • HMMER web server: interactive sequence similarity searching
    • Finn, R.D., Clements, J. and Eddy, S.R. (2011) HMMER web server: interactive sequence similarity searching. Nucleic Acids Res 39, W29-W37.
    • (2011) Nucleic Acids Res , vol.39
    • Finn, R.D.1    Clements, J.2    Eddy, S.R.3
  • 10
    • 77955557492 scopus 로고    scopus 로고
    • Bacteriophage endolysins: a novel anti-infective to control Gram-positive pathogens
    • Fischetti, V.A. (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
  • 12
    • 77954309652 scopus 로고    scopus 로고
    • Synergy between the phage endolysin LysH5 and nisin to kill Staphylococcus aureus in pasteurized milk
    • Garcia, P., Martinez, B., Rodriguez, L. and Rodriguez, A. (2010) Synergy between the phage endolysin LysH5 and nisin to kill Staphylococcus aureus in pasteurized milk. Int J Food Microbiol 141, 151-155.
    • (2010) Int J Food Microbiol , vol.141 , pp. 151-155
    • Garcia, P.1    Martinez, B.2    Rodriguez, L.3    Rodriguez, A.4
  • 14
    • 84861138482 scopus 로고    scopus 로고
    • Isolation of a Paenibacillus sp. strain and structural elucidation of its broad-spectrum lipopeptide antibiotic
    • Guo, Y., Huang, E., Yuan, C., Zhang, L. and Yousef, A.E. (2012) Isolation of a Paenibacillus sp. strain and structural elucidation of its broad-spectrum lipopeptide antibiotic. Appl Environ Microbiol 78, 3156-3165.
    • (2012) Appl Environ Microbiol , vol.78 , pp. 3156-3165
    • Guo, Y.1    Huang, E.2    Yuan, C.3    Zhang, L.4    Yousef, A.E.5
  • 15
    • 79959752636 scopus 로고    scopus 로고
    • P-27/HP endolysin as antibacterial agent for antibiotic resistant Staphylococcus aureus of human infections
    • Gupta, R. and Prasad, Y. (2011) P-27/HP endolysin as antibacterial agent for antibiotic resistant Staphylococcus aureus of human infections. Curr Microbiol 63, 39-45.
    • (2011) Curr Microbiol , vol.63 , pp. 39-45
    • Gupta, R.1    Prasad, Y.2
  • 17
    • 22544460255 scopus 로고    scopus 로고
    • The viriosphere, diversity, and genetic exchange within phage communities
    • Hambly, E. and Suttle, C.A. (2005) The viriosphere, diversity, and genetic exchange within phage communities. Curr Opin Microbiol 8, 444-450.
    • (2005) Curr Opin Microbiol , vol.8 , pp. 444-450
    • Hambly, E.1    Suttle, C.A.2
  • 18
    • 35948990424 scopus 로고    scopus 로고
    • Taking aim on bacterial pathogens: from phage therapy to enzybiotics
    • Hermoso, J.A., Garcia, J.L. and 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
    • 0014466655 scopus 로고
    • Poorly lytic bacteriophage from Dactylosporangium thailandensis (Actinomycetales)
    • Higgins, M.L. and Lechevalier, M.P. (1969) Poorly lytic bacteriophage from Dactylosporangium thailandensis (Actinomycetales). J Virol 3, 210-216.
    • (1969) J Virol , vol.3 , pp. 210-216
    • Higgins, M.L.1    Lechevalier, M.P.2
  • 20
    • 0043163537 scopus 로고    scopus 로고
    • Alternatives to antibiotics: bacteriocins, antimicrobial peptides and bacteriophages
    • Joerger, R.D. (2003) Alternatives to antibiotics: bacteriocins, antimicrobial peptides and bacteriophages. Poult Sci 82, 640-647.
    • (2003) Poult Sci , vol.82 , pp. 640-647
    • Joerger, R.D.1
  • 22
    • 18444403557 scopus 로고    scopus 로고
    • Growth and preservation of Streptomyces
    • Streptomyces, P. Norwich, England: The John Innes Foundation.
    • Kieser, T., Bibb, M.J., Buttner, M.J., Chater, K.F. and Hopwood, D.A. (2000) Growth and preservation of Streptomyces. In Genetics ed. Streptomyces, P. pp. 46-47. Norwich, England: The John Innes Foundation.
    • (2000) Genetics , pp. 46-47
    • Kieser, T.1    Bibb, M.J.2    Buttner, M.J.3    Chater, K.F.4    Hopwood, D.A.5
  • 23
    • 33947396809 scopus 로고    scopus 로고
    • Use of high-affinity cell wall-binding domains of bacteriophage endolysins for immobilization and separation of bacterial cells
    • Kretzer, J.W., Lehmann, R., Schmelcher, M., Banz, M., Kim, K.P., Korn, C. and Loessner, M.J. (2007) Use of high-affinity cell wall-binding domains of bacteriophage endolysins for immobilization and separation of bacterial cells. Appl Environ Microbiol 73, 1992-2000.
    • (2007) Appl Environ Microbiol , vol.73 , pp. 1992-2000
    • Kretzer, J.W.1    Lehmann, R.2    Schmelcher, M.3    Banz, M.4    Kim, K.P.5    Korn, C.6    Loessner, M.J.7
  • 24
    • 0015041802 scopus 로고
    • Metachromatic agar-diffusion methods for detecting staphylococcal nuclease activity
    • Lachica, R.V., Genigeorgis, C. and Hoeprich, P.D. (1971) Metachromatic agar-diffusion methods for detecting staphylococcal nuclease activity. Appl Microbiol 21, 585-587.
    • (1971) Appl Microbiol , vol.21 , pp. 585-587
    • Lachica, R.V.1    Genigeorgis, C.2    Hoeprich, P.D.3
  • 25
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 27
    • 0001857117 scopus 로고
    • 16S/23S rRNA Sequencing
    • Stackebrandt, E. and Goodfellow, M. New York, NY: John Wiley & Sons Ltd.
    • Lane, D.J. (1991) 16S/23S rRNA Sequencing. In Nucleic Acid Techniques in Bacterial Systematics, ed. Stackebrandt, E. and Goodfellow, M. pp. 115-175. New York, NY: John Wiley & Sons Ltd.
    • (1991) Nucleic Acid Techniques in Bacterial Systematics , pp. 115-175
    • Lane, D.J.1
  • 28
    • 0030854739 scopus 로고    scopus 로고
    • tRNAscan-SE: a program for improved detection of transfer RNA genes in genomic sequence
    • Lowe, T.M. and Eddy, S.R. (1997) tRNAscan-SE: a program for improved detection of transfer RNA genes in genomic sequence. Nucleic Acids Res 25, 955-964.
    • (1997) Nucleic Acids Res , vol.25 , pp. 955-964
    • Lowe, T.M.1    Eddy, S.R.2
  • 30
    • 84861152858 scopus 로고    scopus 로고
    • Lytic activity of LysH5 endolysin secreted by Lactococcus lactis using the secretion signal sequence of bacteriocin Lcn972
    • Rodriguez-Rubio, L., Gutierrez, D., Martinez, B., Rodriguez, A. and Garcia, P. (2012) Lytic activity of LysH5 endolysin secreted by Lactococcus lactis using the secretion signal sequence of bacteriocin Lcn972. Appl Environ Microbiol 78, 3469-3472.
    • (2012) Appl Environ Microbiol , vol.78 , pp. 3469-3472
    • Rodriguez-Rubio, L.1    Gutierrez, D.2    Martinez, B.3    Rodriguez, A.4    Garcia, P.5
  • 32
    • 77956573488 scopus 로고    scopus 로고
    • Rapid multiplex detection and differentiation of Listeria cells by use of fluorescent phage endolysin cell wall binding domains
    • Schmelcher, M., Shabarova, T., Eugster, M.R., Eichenseher, F., Tchang, V.S., Banz, M. and Loessner, M.J. (2010) Rapid multiplex detection and differentiation of Listeria cells by use of fluorescent phage endolysin cell wall binding domains. Appl Environ Microbiol 76, 5745-5756.
    • (2010) Appl Environ Microbiol , vol.76 , pp. 5745-5756
    • Schmelcher, M.1    Shabarova, T.2    Eugster, M.R.3    Eichenseher, F.4    Tchang, V.S.5    Banz, M.6    Loessner, M.J.7
  • 33
    • 84861123085 scopus 로고    scopus 로고
    • Chimeric phage lysins act synergistically with lysostaphin to kill mastitis-causing Staphylococcus aureus in murine mammary glands
    • Schmelcher, M., Powell, A.M., Becker, S.C., Camp, M.J. and Donovan, D.M. (2012) Chimeric phage lysins act synergistically with lysostaphin to kill mastitis-causing Staphylococcus aureus in murine mammary glands. Appl Environ Microbiol 78, 2297-2305.
    • (2012) Appl Environ Microbiol , vol.78 , pp. 2297-2305
    • Schmelcher, M.1    Powell, A.M.2    Becker, S.C.3    Camp, M.J.4    Donovan, D.M.5
  • 34
    • 38049047599 scopus 로고    scopus 로고
    • Application of bacteriocins in vegetable food biopreservation
    • Settanni, L. and Corsetti, A. (2008) Application of bacteriocins in vegetable food biopreservation. Int J Food Microbiol 121, 123-138.
    • (2008) Int J Food Microbiol , vol.121 , pp. 123-138
    • Settanni, L.1    Corsetti, A.2
  • 35
    • 84857766056 scopus 로고    scopus 로고
    • Identification, purification and characterization of laterosporulin, a novel bacteriocin produced by Brevibacillus sp. strain GI-9
    • Singh, P.K., Ashish, C., Sharma, V., Patil, P.B. and Korpole, S. (2012) Identification, purification and characterization of laterosporulin, a novel bacteriocin produced by Brevibacillus sp. strain GI-9. PLoS One 7, e31498.
    • (2012) PLoS One , vol.7
    • Singh, P.K.1    Ashish, C.2    Sharma, V.3    Patil, P.B.4    Korpole, S.5
  • 36
    • 77952890163 scopus 로고    scopus 로고
    • Antibacterial and biofilm removal activity of a podoviridae Staphylococcus aureus bacteriophage SAP-2 and a derived recombinant cell-wall-degrading enzyme
    • Son, J.S., Lee, S.J., Jun, S.Y., Yoon, S.J., Kang, S.H., Paik, H.R., Kang, J.O. and Choi, Y.J. (2010a) Antibacterial and biofilm removal activity of a podoviridae Staphylococcus aureus bacteriophage SAP-2 and a derived recombinant cell-wall-degrading enzyme. Appl Microbiol Biotechnol 86, 1439-1449.
    • (2010) Appl Microbiol Biotechnol , vol.86 , pp. 1439-1449
    • Son, J.S.1    Lee, S.J.2    Jun, S.Y.3    Yoon, S.J.4    Kang, S.H.5    Paik, H.R.6    Kang, J.O.7    Choi, Y.J.8
  • 37
    • 77950681219 scopus 로고    scopus 로고
    • Complete genome sequence of a newly isolated lytic bacteriophage, EFAP-1 of Enterococcus faecalis, and antibacterial activity of its endolysin EFAL-1
    • Son, J.S., Jun, S.Y., Kim, E.B., Park, J.E., Paik, H.R., Yoon, S.J., Kang, S.H. and Choi, Y.J. (2010b) Complete genome sequence of a newly isolated lytic bacteriophage, EFAP-1 of Enterococcus faecalis, and antibacterial activity of its endolysin EFAL-1. J Appl Microbiol 108, 1769-1779.
    • (2010) J Appl Microbiol , vol.108 , pp. 1769-1779
    • Son, J.S.1    Jun, S.Y.2    Kim, E.B.3    Park, J.E.4    Paik, H.R.5    Yoon, S.J.6    Kang, S.H.7    Choi, Y.J.8
  • 39
    • 0027968068 scopus 로고
    • CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson, J.D., Higgins, D.G. and Gibson, T.J. (1994) CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res 22, 4673-4680.
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 40
    • 84860644406 scopus 로고    scopus 로고
    • Rare actinomycetes: a potential storehouse for novel antibiotics
    • Tiwari, K. and Gupta, R.K. (2012) Rare actinomycetes: a potential storehouse for novel antibiotics. Crit Rev Biotechnol 32, 108-132.
    • (2012) Crit Rev Biotechnol , vol.32 , pp. 108-132
    • Tiwari, K.1    Gupta, R.K.2
  • 41
    • 84870502596 scopus 로고    scopus 로고
    • A bacteriophage endolysin-based electrochemical impedance biosensor for the rapid detection of Listeria cells
    • Tolba, M., Ahmed, M.U., Tlili, C., Eichenseher, F., Loessner, M.J. and Zourob, M. (2012) A bacteriophage endolysin-based electrochemical impedance biosensor for the rapid detection of Listeria cells. Analyst 137, 5749-5756.
    • (2012) Analyst , vol.137 , pp. 5749-5756
    • Tolba, M.1    Ahmed, M.U.2    Tlili, C.3    Eichenseher, F.4    Loessner, M.J.5    Zourob, M.6
  • 43
    • 80052295744 scopus 로고    scopus 로고
    • Antimicrobial edible films and coatings for fresh and minimally processed fruits and vegetables: a review
    • Valencia-Chamorro, S.A., Palou, L., Del Rio, M.A. and Perez-Gago, M.B. (2011) Antimicrobial edible films and coatings for fresh and minimally processed fruits and vegetables: a review. Crit Rev Food Sci Nutr 51, 872-900.
    • (2011) Crit Rev Food Sci Nutr , vol.51 , pp. 872-900
    • Valencia-Chamorro, S.A.1    Palou, L.2    Del Rio, M.A.3    Perez-Gago, M.B.4
  • 45
    • 0026067797 scopus 로고
    • 16S ribosomal DNA amplification for phylogenetic study
    • Weisburg, W.G., Barns, S.M., Pelletier, D.A. and Lane, D.J. (1991) 16S ribosomal DNA amplification for phylogenetic study. J Bacteriol 173, 697-703.
    • (1991) J Bacteriol , vol.173 , pp. 697-703
    • Weisburg, W.G.1    Barns, S.M.2    Pelletier, D.A.3    Lane, D.J.4
  • 46
    • 0024287661 scopus 로고
    • A dye release assay for determination of lysostaphin activity
    • Zhou, R., Chen, S. and Recsei, P. (1988) A dye release assay for determination of lysostaphin activity. Anal Biochem 171, 141-144.
    • (1988) Anal Biochem , vol.171 , pp. 141-144
    • Zhou, R.1    Chen, S.2    Recsei, P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.