메뉴 건너뛰기




Volumn 99, Issue 12, 2015, Pages 5137-5149

EC300: a phage-based, bacteriolysin-like protein with enhanced antibacterial activity against Enterococcus faecalis

Author keywords

Chimerical enzyme; Endolysin; Enterococcus faecalis; Peptidoglycan hydrolase; Virion associated lysin

Indexed keywords

ANTIBIOTICS; BACILLI; ENZYMES; PROTEINS;

EID: 84929948662     PISSN: 01757598     EISSN: 14320614     Source Type: Journal    
DOI: 10.1007/s00253-015-6483-7     Document Type: Article
Times cited : (26)

References (78)
  • 2
    • 80055121440 scopus 로고    scopus 로고
    • Lysis from without
    • PID: 21687534
    • Abedon ST (2011) Lysis from without. Bacteriophage 1:46–49. doi:10.4161/bact.1.1.13980
    • (2011) Bacteriophage , vol.1 , pp. 46-49
    • Abedon, S.T.1
  • 3
    • 0030801002 scopus 로고    scopus 로고
    • Gapped BLAST and PSI-BLAST: a new generation of protein database search programs
    • COI: 1:CAS:528:DyaK2sXlvFyhu7w%3D, PID: 9254694
    • Altschul SF, Madden TL, Schäffer AA, Zhang J, Zhang Z, Miller W, Lipman DJ (1997) Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucleic Acids Res 25:3389–3402. doi:10.1093/nar/25.17.3389
    • (1997) Nucleic Acids Res , vol.25 , pp. 3389-3402
    • Altschul, S.F.1    Madden, T.L.2    Schäffer, A.A.3    Zhang, J.4    Zhang, Z.5    Miller, W.6    Lipman, D.J.7
  • 4
    • 18244415313 scopus 로고    scopus 로고
    • Evolutionary history, structural features and biochemical diversity of the NLPC/P60 superfamily of enzymes
    • PID: 12620121
    • Anantharaman V, Aravind L (2003) Evolutionary history, structural features and biochemical diversity of the NLPC/P60 superfamily of enzymes. Genome Biol 4:R11. doi:10.1186/gb-2003-4-2-r11
    • (2003) Genome Biol , vol.4 , pp. R11
    • Anantharaman, V.1    Aravind, L.2
  • 5
    • 55249117030 scopus 로고    scopus 로고
    • Emergence and management of drug-resistant enterococcal infections
    • COI: 1:CAS:528:DC%2BD1cXht1Glu7vJ, PID: 18847403
    • Arias CA, Murray BE (2008) Emergence and management of drug-resistant enterococcal infections. Expert Rev Anti Infect Ther 6:637–655. doi:10.1586/14787210.6.5.637
    • (2008) Expert Rev Anti Infect Ther , vol.6 , pp. 637-655
    • Arias, C.A.1    Murray, B.E.2
  • 6
    • 23144452801 scopus 로고    scopus 로고
    • GeneMark: web software for gene finding in prokaryotes, eukaryotes and viruses
    • COI: 1:CAS:528:DC%2BD2MXlslyqur4%3D, PID: 15980510
    • Besemer J, Borodovsky M (2005) GeneMark: web software for gene finding in prokaryotes, eukaryotes and viruses. Nucleic Acids Res 33(Web Server issue):W451–W454. doi:10.1093/nar/gki487
    • (2005) Nucleic Acids Res , vol.33 , Issue.Web Server issue , pp. W451-W454
    • Besemer, J.1    Borodovsky, M.2
  • 7
    • 46649087608 scopus 로고    scopus 로고
    • Phage T5 straight tail fiber is a multifunctional protein acting as a tape measure and carrying fusogenic and muralytic activities
    • COI: 1:CAS:528:DC%2BD1cXls12mtbc%3D, PID: 18348984
    • Boulanger P, Jacquot P, Plançon L, Chami M, Engel A, Parquet C, Herbeuval C, Letellier L (2008) Phage T5 straight tail fiber is a multifunctional protein acting as a tape measure and carrying fusogenic and muralytic activities. J Biol Chem 283:13556–13564. doi:10.1074/jbc.M800052200
    • (2008) J Biol Chem , vol.283 , pp. 13556-13564
    • Boulanger, P.1    Jacquot, P.2    Plançon, L.3    Chami, M.4    Engel, A.5    Parquet, C.6    Herbeuval, C.7    Letellier, L.8
  • 8
    • 0024413198 scopus 로고
    • Accuracy and precision in the determination of Stokes radii and molecular masses of proteins by gel filtration chromatography
    • PID: 2777944
    • Cabré F, Canela EI, Canela MA (1989) Accuracy and precision in the determination of Stokes radii and molecular masses of proteins by gel filtration chromatography. J Chromatogr 472:347–356. doi:10.1016/S0021-9673(00)94133-5
    • (1989) J Chromatogr , vol.472 , pp. 347-356
    • Cabré, F.1    Canela, E.I.2    Canela, M.A.3
  • 9
    • 77954850130 scopus 로고    scopus 로고
    • The mycobacteriophage Ms6 encodes a chaperone-like protein involved in the endolysin delivery to the peptidoglycan
    • PID: 20545844
    • Catalão MJ, Gil F, Moniz-Pereira J, Pimentel M (2010) The mycobacteriophage Ms6 encodes a chaperone-like protein involved in the endolysin delivery to the peptidoglycan. Mol Microbiol 77:672–686. doi:10.1111/j.1365-2958.2010.07239.x
    • (2010) Mol Microbiol , vol.77 , pp. 672-686
    • Catalão, M.J.1    Gil, F.2    Moniz-Pereira, J.3    Pimentel, M.4
  • 11
    • 0024558335 scopus 로고
    • One-step preparation of competent Escherichia coli: transformation and storage of bacterial cells in the same solution
    • COI: 1:CAS:528:DyaL1MXitV2iurY%3D, PID: 2648393
    • Chung CT, Niemela SL, Miller RH (1989) One-step preparation of competent Escherichia coli: transformation and storage of bacterial cells in the same solution. Proc Natl Acad Sci U S A 86:2172–2175. doi:10.1073/pnas.86.7.2172
    • (1989) Proc Natl Acad Sci U S A , vol.86 , pp. 2172-2175
    • Chung, C.T.1    Niemela, S.L.2    Miller, R.H.3
  • 12
    • 27244436751 scopus 로고    scopus 로고
    • Bacteriocins: developing innate immunity for food
    • COI: 1:CAS:528:DC%2BD2MXhtVGrurbF, PID: 16205711
    • Cotter PD, Hill C, Ross RP (2005) Bacteriocins: developing innate immunity for food. Nat Rev Microbiol 3:777–788. doi:10.1038/nrmicro1273
    • (2005) Nat Rev Microbiol , vol.3 , pp. 777-788
    • Cotter, P.D.1    Hill, C.2    Ross, R.P.3
  • 13
    • 0027204227 scopus 로고
    • Interchange of functional domains switches enzyme specificity: construction of a chimeric pneumococcal-clostridial cell wall lytic enzyme
    • COI: 1:CAS:528:DyaK3sXms1Ggs7k%3D, PID: 7934908
    • Croux C, Ronda C, Lopez R, Garcia JL (1993) Interchange of functional domains switches enzyme specificity: construction of a chimeric pneumococcal-clostridial cell wall lytic enzyme. Mol Microbiol 9:1019–1025. doi:10.1111/j.1365-2958.1993.tb01231.x
    • (1993) Mol Microbiol , vol.9 , pp. 1019-1025
    • Croux, C.1    Ronda, C.2    Lopez, R.3    Garcia, J.L.4
  • 14
    • 77950126213 scopus 로고    scopus 로고
    • Synergism between a novel chimeric lysin and oxacillin protects against infection by methicillin-resistant Staphylococcus aureus
    • COI: 1:CAS:528:DC%2BC3cXksFOisbc%3D, PID: 20086153
    • Daniel A, Euler C, Collin M, Chahales P, Gorelick KJ, Fischetti VA (2010) Synergism between a novel chimeric lysin and oxacillin protects against infection by methicillin-resistant Staphylococcus aureus. Antimicrob Agents Chemother 54:1603–1612. doi:10.1128/AAC. 01625-09
    • (2010) Antimicrob Agents Chemother , vol.54 , pp. 1603-1612
    • Daniel, A.1    Euler, C.2    Collin, M.3    Chahales, P.4    Gorelick, K.J.5    Fischetti, V.A.6
  • 15
    • 33646102467 scopus 로고    scopus 로고
    • Peptidoglycan hydrolase fusions maintain their parental specificities
    • COI: 1:CAS:528:DC%2BD28XktFansb8%3D, PID: 16598006
    • Donovan DM, Dong S, Garrett W, Rousseau GM, Moineau S, Pritchard DG (2006) Peptidoglycan hydrolase fusions maintain their parental specificities. Appl Environ Microbiol 72:2988–2996. doi:10.1128/aem. 72.4.2988-2996.2006
    • (2006) Appl Environ Microbiol , vol.72 , pp. 2988-2996
    • Donovan, D.M.1    Dong, S.2    Garrett, W.3    Rousseau, G.M.4    Moineau, S.5    Pritchard, D.G.6
  • 16
    • 60149103898 scopus 로고    scopus 로고
    • Loop-length dependent SVM prediction of domain linkers for high-throughput structural proteomics
    • COI: 1:CAS:528:DC%2BD1MXhvFCksL8%3D, PID: 18844295
    • Ebina T, Toh H, Kuroda Y (2009) Loop-length dependent SVM prediction of domain linkers for high-throughput structural proteomics. Biopolymers 92:1–8. doi:10.1002/bip.21105
    • (2009) Biopolymers , vol.92
    • Ebina, T.1    Toh, H.2    Kuroda, Y.3
  • 17
    • 0027379284 scopus 로고
    • An overview of nosocomial infections, including the role of the microbiology laboratory
    • COI: 1:STN:280:DyaK2c%2FpsVWqtg%3D%3D, PID: 8269394
    • Emori TG, Gaynes RP (1993) An overview of nosocomial infections, including the role of the microbiology laboratory. Clin Microbiol Rev 6:428–442. doi:10.1128/CMR.6.4.428
    • (1993) Clin Microbiol Rev , vol.6 , pp. 428-442
    • Emori, T.G.1    Gaynes, R.P.2
  • 20
    • 67650744795 scopus 로고    scopus 로고
    • The ecology, epidemiology and virulence of Enterococcus
    • COI: 1:CAS:528:DC%2BD1MXotVaqsL8%3D, PID: 19383684
    • Fisher K, Phillips C (2009) The ecology, epidemiology and virulence of Enterococcus. Microbiology 155:1749–1757. doi:10.1099/mic. 0.026385-0
    • (2009) Microbiology , vol.155 , pp. 1749-1757
    • Fisher, K.1    Phillips, C.2
  • 21
    • 78649712445 scopus 로고    scopus 로고
    • The continuing crisis in antibiotic resistance
    • French GL (2010) The continuing crisis in antibiotic resistance. Int J Antimicrob Agents 3:S3–S7. doi:10.1016/S0924-8579(10)70003-0
    • (2010) Int J Antimicrob Agents , vol.3 , pp. S3-S7
    • French, G.L.1
  • 22
    • 68949098479 scopus 로고    scopus 로고
    • The autolysin LytA contributes to efficient bacteriophage progeny release in Streptococcus pneumoniae
    • COI: 1:CAS:528:DC%2BD1MXhtFKksL%2FM, PID: 19581370
    • Frias MJ, Melo-Cristino J, Ramirez M (2009) The autolysin LytA contributes to efficient bacteriophage progeny release in Streptococcus pneumoniae. J Bacteriol 191:5428–5440. doi:10.1128/JB.00477-09
    • (2009) J Bacteriol , vol.191 , pp. 5428-5440
    • Frias, M.J.1    Melo-Cristino, J.2    Ramirez, M.3
  • 23
    • 77954309652 scopus 로고    scopus 로고
    • Synergy between the phage endolysin LysH5 and nisin to kill Staphylococcus aureus in pasteurized milk
    • PID: 20537744
    • García P, Martínez B, Rodríguez L, Rodríguez A (2010) Synergy between the phage endolysin LysH5 and nisin to kill Staphylococcus aureus in pasteurized milk. Int J Food Microbiol 141:151–155. doi:10.1016/j.ijfoodmicro.2010.04.029
    • (2010) Int J Food Microbiol , vol.141 , pp. 151-155
    • García, P.1    Martínez, B.2    Rodríguez, L.3    Rodríguez, A.4
  • 24
    • 84875808358 scopus 로고    scopus 로고
    • Genomic transition of enterococci from gut commensals to leading causes of multidrug-resistant hospital infection in the antibiotic era
    • PID: 23395351
    • Gilmore MS, Lebreton F, van Schaik W (2013) Genomic transition of enterococci from gut commensals to leading causes of multidrug-resistant hospital infection in the antibiotic era. Curr Opin Microbiol 16:10–16. doi:10.1016/j.mib.2013.01.006
    • (2013) Curr Opin Microbiol , vol.16 , pp. 10-16
    • Gilmore, M.S.1    Lebreton, F.2    van Schaik, W.3
  • 25
    • 78650865739 scopus 로고    scopus 로고
    • LysGH15, a novel bacteriophage lysin, protects a murine bacteremia model efficiently against lethal methicillin-resistant Staphylococcus aureus infection
    • COI: 1:CAS:528:DC%2BC3MXjtFSgtLc%3D, PID: 21048011
    • Gu J, Xu W, Lei L, Huang J, Feng X, Sun C, Du C, Zuo J, Li Y, Du T, Li L, Han W (2011) LysGH15, a novel bacteriophage lysin, protects a murine bacteremia model efficiently against lethal methicillin-resistant Staphylococcus aureus infection. J Clin Microbiol 49:111–117. doi:10.1128/JCM. 01144-10
    • (2011) J Clin Microbiol , vol.49 , pp. 111-117
    • Gu, J.1    Xu, W.2    Lei, L.3    Huang, J.4    Feng, X.5    Sun, C.6    Du, C.7    Zuo, J.8    Li, Y.9    Du, T.10    Li, L.11    Han, W.12
  • 26
    • 84862632796 scopus 로고    scopus 로고
    • Enterococci of animal origin and their significance for public health
    • COI: 1:CAS:528:DC%2BC38XhtFOhtrzP, PID: 22487203
    • Hammerum AM (2012) Enterococci of animal origin and their significance for public health. Clin Microbiol Infect 18:619–625. doi:10.1111/j.1469-0691.2012.03829.x
    • (2012) Clin Microbiol Infect , vol.18 , pp. 619-625
    • Hammerum, A.M.1
  • 27
    • 4444277132 scopus 로고    scopus 로고
    • Assembly and stability of nisin-lipid II pores
    • COI: 1:CAS:528:DC%2BD2cXmslShsrY%3D, PID: 15350143
    • Hasper HE, de Kruijff B, Breukink E (2004) Assembly and stability of nisin-lipid II pores. Biochemistry 43:11567–1175. doi:10.1021/bi049476b
    • (2004) Biochemistry , vol.43 , pp. 11175-11567
    • Hasper, H.E.1    de Kruijff, B.2    Breukink, E.3
  • 28
    • 0024520745 scopus 로고
    • Site-directed mutagenesis by overlap extension using the polymerase chain reaction
    • COI: 1:CAS:528:DyaL1MXktVaitrk%3D, PID: 2744487
    • Ho SN, Hunt HD, Horton RM, Pullen JK, Pease LR (1989) Site-directed mutagenesis by overlap extension using the polymerase chain reaction. Gene 77:51–59. doi:10.1016/0378-1119(89)90358-2
    • (1989) Gene , vol.77 , pp. 51-59
    • Ho, S.N.1    Hunt, H.D.2    Horton, R.M.3    Pullen, J.K.4    Pease, L.R.5
  • 29
    • 0025985759 scopus 로고
    • Bacteremia caused by hemolytic, high-level gentamicin-resistant Enterococcus faecalis
    • COI: 1:STN:280:DyaK38%2FislKltA%3D%3D, PID: 1929336
    • Huycke MM, Spiegel CA, Gilmore MS (1991) Bacteremia caused by hemolytic, high-level gentamicin-resistant Enterococcus faecalis. Antimicrob Agents Chemother 35:1626–1634. doi:10.1128/AAC.35.8.1626
    • (1991) Antimicrob Agents Chemother , vol.35 , pp. 1626-1634
    • Huycke, M.M.1    Spiegel, C.A.2    Gilmore, M.S.3
  • 30
    • 80051828382 scopus 로고    scopus 로고
    • In vitro activity against Staphylococcus aureus of a novel antimicrobial agent, PRF-119, a recombinant chimeric bacteriophage endolysin
    • COI: 1:CAS:528:DC%2BC3MXhtFaitrzM, PID: 21746950
    • Idelevich EA, von Eiff C, Friedrich AW, Iannelli D, Xia G, Peters G, Peschel A, Wanninger I, Becker K (2011) In vitro activity against Staphylococcus aureus of a novel antimicrobial agent, PRF-119, a recombinant chimeric bacteriophage endolysin. Antimicrob Agents Chemother 55:4416–4419. doi:10.1128/AAC. 00217-11
    • (2011) Antimicrob Agents Chemother , vol.55 , pp. 4416-4419
    • Idelevich, E.A.1    von Eiff, C.2    Friedrich, A.W.3    Iannelli, D.4    Xia, G.5    Peters, G.6    Peschel, A.7    Wanninger, I.8    Becker, K.9
  • 31
    • 84880576108 scopus 로고    scopus 로고
    • Determination of the mode of action of enterolysin A, produced by Enterococcus faecalis B9510
    • COI: 1:CAS:528:DC%2BC3sXhtFClsrnI, PID: 23639072
    • Khan H, Flint SH, Yu PL (2013) Determination of the mode of action of enterolysin A, produced by Enterococcus faecalis B9510. J Appl Microbiol 115:484–494. doi:10.1111/jam.12240
    • (2013) J Appl Microbiol , vol.115 , pp. 484-494
    • Khan, H.1    Flint, S.H.2    Yu, P.L.3
  • 32
    • 0142196566 scopus 로고    scopus 로고
    • Taxonomy, ecology and antibiotic resistance of enterococci from food and the gastro-intestinal tract
    • PID: 14596985
    • Klein G (2003) Taxonomy, ecology and antibiotic resistance of enterococci from food and the gastro-intestinal tract. Int J Food Microbiol 88:123–131. doi:10.1016/S0168-1605(03)00175-2
    • (2003) Int J Food Microbiol , vol.88 , pp. 123-131
    • Klein, G.1
  • 33
    • 62449232344 scopus 로고    scopus 로고
    • Enumeration of bacteriophages by double agar overlay plaque assay
    • COI: 1:CAS:528:DC%2BD1MXitlagur8%3D, PID: 19066811
    • Kropinski AM, Mazzocco A, Waddell TE, Lingohr E, Johnson RP (2009) Enumeration of bacteriophages by double agar overlay plaque assay. Methods Mol Biol 501:69–76. doi:10.1007/978-1-60327-164-6_7
    • (2009) Methods Mol Biol , vol.501 , pp. 69-76
    • Kropinski, A.M.1    Mazzocco, A.2    Waddell, T.E.3    Lingohr, E.4    Johnson, R.P.5
  • 35
    • 50849108830 scopus 로고    scopus 로고
    • Lysostaphin: an antistaphylococcal agent
    • COI: 1:CAS:528:DC%2BD1cXhtVKisLvL, PID: 18607587
    • Kumar JK (2008) Lysostaphin: an antistaphylococcal agent. Appl Microbiol Biotechnol 80:555–561. doi:10.1007/s00253-008-1579-y
    • (2008) Appl Microbiol Biotechnol , vol.80 , pp. 555-561
    • Kumar, J.K.1
  • 36
    • 84859970549 scopus 로고    scopus 로고
    • The Bacillus subtilis cannibalism toxin SDP collapses the proton motive force and induces autolysis
    • COI: 1:CAS:528:DC%2BC38XnvVGqurc%3D, PID: 22469514
    • Lamsa A, Liu WT, Dorrestein PC, Pogliano K (2012) The Bacillus subtilis cannibalism toxin SDP collapses the proton motive force and induces autolysis. Mol Microbiol 84:486–500. doi:10.1111/j.1365-2958.2012.08038.x
    • (2012) Mol Microbiol , vol.84 , pp. 486-500
    • Lamsa, A.1    Liu, W.T.2    Dorrestein, P.C.3    Pogliano, K.4
  • 37
    • 0242286566 scopus 로고    scopus 로고
    • Phage lytic enzyme Cpl-1 as a novel antimicrobial for pneumococcal bacteremia
    • COI: 1:CAS:528:DC%2BD3sXoslegu7g%3D, PID: 14573637
    • Loeffler JM, Djurkovic S, Fischetti VA (2003) Phage lytic enzyme Cpl-1 as a novel antimicrobial for pneumococcal bacteremia. Infect Immun 71:6199–61204. doi:10.1128/IAI. 71.11.6199-6204.2003
    • (2003) Infect Immun , vol.71 , pp. 6199-61204
    • Loeffler, J.M.1    Djurkovic, S.2    Fischetti, V.A.3
  • 38
    • 0018692485 scopus 로고
    • Renal filtration, transport, and metabolism of low-molecular-weight proteins: a review
    • COI: 1:CAS:528:DyaE1MXmtVOqurc%3D, PID: 393891
    • Maack T, Johnson V, Kau ST, Figueiredo J, Sigulem D (1979) Renal filtration, transport, and metabolism of low-molecular-weight proteins: a review. Kidney Int 16:251–270. doi:10.1038/ki.1979.128
    • (1979) Kidney Int , vol.16 , pp. 251-270
    • Maack, T.1    Johnson, V.2    Kau, S.T.3    Figueiredo, J.4    Sigulem, D.5
  • 39
    • 84876308417 scopus 로고    scopus 로고
    • Chimeric Ply187 endolysin kills Staphylococcus aureus more effectively than the parental enzyme
    • COI: 1:CAS:528:DC%2BC3sXntlersL0%3D, PID: 23413880
    • Mao J, Schmelcher M, Harty WJ, Foster-Frey J, Donovan DM (2013) Chimeric Ply187 endolysin kills Staphylococcus aureus more effectively than the parental enzyme. FEMS Microbiol Lett 342:30–36. doi:10.1111/1574-6968.12104
    • (2013) FEMS Microbiol Lett , vol.342 , pp. 30-36
    • Mao, J.1    Schmelcher, M.2    Harty, W.J.3    Foster-Frey, J.4    Donovan, D.M.5
  • 41
    • 67349180746 scopus 로고    scopus 로고
    • Assessment of high-level gentamicin and glycopeptide-resistant Enterococcus faecalis and E. faecium clonal structure in a Portuguese hospital over a 3-year period
    • COI: 1:CAS:528:DC%2BD1MXmvFGnsb8%3D, PID: 19184139
    • Mato R, Almeida F, Pires R, Rodrigues P, Ferreira T, Santos-Sanches I (2009) Assessment of high-level gentamicin and glycopeptide-resistant Enterococcus faecalis and E. faecium clonal structure in a Portuguese hospital over a 3-year period. Eur J Clin Microbiol Infect Dis 28:855–859. doi:10.1007/s10096-009-0704-x
    • (2009) Eur J Clin Microbiol Infect Dis , vol.28 , pp. 855-859
    • Mato, R.1    Almeida, F.2    Pires, R.3    Rodrigues, P.4    Ferreira, T.5    Santos-Sanches, I.6
  • 42
    • 0025100795 scopus 로고
    • The life and times of the Enterococcus
    • Murray BE (1990) The life and times of the Enterococcus. Clin Microbiol Rev 3:46–65. doi:10.1128/CMR.3.1.46
    • (1990) Clin Microbiol Rev , vol.3 , pp. 46-65
    • Murray, B.E.1
  • 43
    • 37549067712 scopus 로고    scopus 로고
    • Nisin-triggered activity of Lys44, the secreted endolysin from Oenococcus oeni phage fOg44
    • COI: 1:CAS:528:DC%2BD1cXhsF2quw%3D%3D, PID: 17981964
    • Nascimento JG, Guerreiro-Pereira MC, Costa SF, São-José C, Santos MA (2008) Nisin-triggered activity of Lys44, the secreted endolysin from Oenococcus oeni phage fOg44. J Bacteriol 190:457–461. doi:10.1128/JB.01195-07
    • (2008) J Bacteriol , vol.190 , pp. 457-461
    • Nascimento, J.G.1    Guerreiro-Pereira, M.C.2    Costa, S.F.3    São-José, C.4    Santos, M.A.5
  • 45
    • 59149090570 scopus 로고    scopus 로고
    • MetaGeneAnnotator: detecting species-specific patterns of ribosomal binding site for precise gene prediction in anonymous prokaryotic and phage genomes
    • COI: 1:CAS:528:DC%2BD1MXmtV2rug%3D%3D, PID: 18940874
    • Noguchi H, Taniguchi T, Itoh T (2008) MetaGeneAnnotator: detecting species-specific patterns of ribosomal binding site for precise gene prediction in anonymous prokaryotic and phage genomes. DNA Res 15:387–396. doi:10.1093/dnares/dsn027
    • (2008) DNA Res , vol.15 , pp. 387-396
    • Noguchi, H.1    Taniguchi, T.2    Itoh, T.3
  • 46
    • 84887476185 scopus 로고    scopus 로고
    • In vitro characterization of PlySK1249, a novel phage lysin, and assessment of its antibacterial activity in a mouse model of Streptococcus agalactiae bacteremia
    • COI: 1:CAS:528:DC%2BC3sXhvVCjur%2FK, PID: 24100496
    • Oechslin F, Daraspe J, Giddey M, Moreillon P, Resch G (2013) In vitro characterization of PlySK1249, a novel phage lysin, and assessment of its antibacterial activity in a mouse model of Streptococcus agalactiae bacteremia. Antimicrob Agents Chemother 57:6276–6283. doi:10.1128/AAC. 01701-13
    • (2013) Antimicrob Agents Chemother , vol.57 , pp. 6276-6283
    • Oechslin, F.1    Daraspe, J.2    Giddey, M.3    Moreillon, P.4    Resch, G.5
  • 47
    • 78751697614 scopus 로고    scopus 로고
    • A novel chimeric lysin shows superiority to mupirocin for skin decolonization of methicillin-resistant and -sensitive Staphylococcus aureus strains
    • COI: 1:CAS:528:DC%2BC3MXisVyjtrg%3D, PID: 21098252
    • Pastagia M, Euler C, Chahales P, Fuentes-Duculan J, Krueger JG, Fischetti VA (2011) A novel chimeric lysin shows superiority to mupirocin for skin decolonization of methicillin-resistant and -sensitive Staphylococcus aureus strains. Antimicrob Agents Chemother 55:738–744. doi:10.1128/AAC. 00890-10
    • (2011) Antimicrob Agents Chemother , vol.55 , pp. 738-744
    • Pastagia, M.1    Euler, C.2    Chahales, P.3    Fuentes-Duculan, J.4    Krueger, J.G.5    Fischetti, V.A.6
  • 50
    • 33751384637 scopus 로고    scopus 로고
    • A peptidoglycan hydrolase motif within the mycobacteriophage TM4 tape measure protein promotes efficient infection of stationary phase cells
    • COI: 1:CAS:528:DC%2BD2sXit1Khsw%3D%3D, PID: 17083467
    • Piuri M, Hatfull GF (2006) A peptidoglycan hydrolase motif within the mycobacteriophage TM4 tape measure protein promotes efficient infection of stationary phase cells. Mol Microbiol 62:1569–1585. doi:10.1111/j.1365-2958.2006.05473.x
    • (2006) Mol Microbiol , vol.62 , pp. 1569-1585
    • Piuri, M.1    Hatfull, G.F.2
  • 51
    • 33645897695 scopus 로고    scopus 로고
    • Epidemiology and clinical outcome of enterococcal bacterium in an acute care hospital
    • COI: 1:STN:280:DC%2BD283ivVKhtw%3D%3D, PID: 16203039
    • Poh CH, Oh HM, Tan AL (2006) Epidemiology and clinical outcome of enterococcal bacterium in an acute care hospital. J Infect 52:383–386. doi:10.1016/j.jinf.2005.07.011
    • (2006) J Infect , vol.52 , pp. 383-386
    • Poh, C.H.1    Oh, H.M.2    Tan, A.L.3
  • 54
    • 80255133188 scopus 로고    scopus 로고
    • A stable phage lysin (Cpl-1) dimer with increased antipneumococcal activity and decreased plasma clearance
    • COI: 1:CAS:528:DC%2BC3MXhtl2gsrzE, PID: 21982146
    • Resch G, Moreillon P, Fischetti VA (2011) A stable phage lysin (Cpl-1) dimer with increased antipneumococcal activity and decreased plasma clearance. Int J Antimicrob Agents 38:516–521. doi:10.1016/j.ijantimicag.2011.08.009
    • (2011) Int J Antimicrob Agents , vol.38 , pp. 516-521
    • Resch, G.1    Moreillon, P.2    Fischetti, V.A.3
  • 55
    • 84866150170 scopus 로고    scopus 로고
    • The tape measure protein of the Staphylococcus aureus bacteriophage vB_SauS-phiIPLA35 has an active muramidase domain
    • PID: 22729533
    • Rodríguez-Rubio L, Gutiérrez D, Martínez B, Rodríguez A, Götz F, García P (2012a) The tape measure protein of the Staphylococcus aureus bacteriophage vB_SauS-phiIPLA35 has an active muramidase domain. Appl Environ Microbiol 78:6369–6371. doi:10.1128/AEM. 01236-12
    • (2012) Appl Environ Microbiol , vol.78 , pp. 6369-6371
    • Rodríguez-Rubio, L.1    Gutiérrez, D.2    Martínez, B.3    Rodríguez, A.4    Götz, F.5    García, P.6
  • 56
    • 84861148398 scopus 로고    scopus 로고
    • Enhanced staphylolytic activity of the Staphylococcus aureus bacteriophage vB_SauS-phiIPLA88 HydH5 virion-associated peptidoglycan hydrolase: fusions, deletions, and synergy with LysH5
    • PID: 22267667
    • Rodríguez-Rubio L, Martínez B, Rodríguez A, Donovan DM, García P (2012b) Enhanced staphylolytic activity of the Staphylococcus aureus bacteriophage vB_SauS-phiIPLA88 HydH5 virion-associated peptidoglycan hydrolase: fusions, deletions, and synergy with LysH5. Appl Environ Microbiol 78:2241–2248. doi:10.1128/AEM. 07621-11
    • (2012) Appl Environ Microbiol , vol.78 , pp. 2241-2248
    • Rodríguez-Rubio, L.1    Martínez, B.2    Rodríguez, A.3    Donovan, D.M.4    García, P.5
  • 57
    • 84885202794 scopus 로고    scopus 로고
    • Bacteriophage virion-associated peptidoglycan hydrolases: potential new enzybiotics
    • PID: 22991936
    • Rodríguez-Rubio L, Martínez B, Donovan DM, Rodríguez A, García P (2013) Bacteriophage virion-associated peptidoglycan hydrolases: potential new enzybiotics. Crit Rev Microbiol 39:427–434. doi:10.3109/1040841X.2012.723675
    • (2013) Crit Rev Microbiol , vol.39 , pp. 427-434
    • Rodríguez-Rubio, L.1    Martínez, B.2    Donovan, D.M.3    Rodríguez, A.4    García, P.5
  • 60
    • 0033808851 scopus 로고    scopus 로고
    • The N-terminal region of the Oenococcus oeni bacteriophage fOg44 lysin behaves as a bona fide signal peptide in Escherichia coli and as a cis-inhibitory element, preventing lytic activity on oenococcal cells
    • PID: 11004183
    • São-José C, Parreira R, Vieira G, Santos MA (2000) The N-terminal region of the Oenococcus oeni bacteriophage fOg44 lysin behaves as a bona fide signal peptide in Escherichia coli and as a cis-inhibitory element, preventing lytic activity on oenococcal cells. J Bacteriol 182:5823–5831. doi:10.1128/JB.182.20.5823-5831.2000
    • (2000) J Bacteriol , vol.182 , pp. 5823-5831
    • São-José, C.1    Parreira, R.2    Vieira, G.3    Santos, M.A.4
  • 61
    • 77953941334 scopus 로고    scopus 로고
    • Pathogenesis and immunity in enterococcal infections
    • COI: 1:CAS:528:DC%2BC3cXot1Gmsrg%3D, PID: 20569264
    • Sava IG, Heikens E, Huebner J (2010) Pathogenesis and immunity in enterococcal infections. Clin Microbiol Infect 16:533–540. doi:10.1111/j.1469-0691.2010.03213.x
    • (2010) Clin Microbiol Infect , vol.16 , pp. 533-540
    • Sava, I.G.1    Heikens, E.2    Huebner, J.3
  • 62
    • 0026062881 scopus 로고
    • Major trends in the microbial etiology of nosocomial infection
    • COI: 1:STN:280:DyaK38%2Fis1aisg%3D%3D, PID: 1928195
    • Schaberg DR, Culver DH, Gaynes RP (1991) Major trends in the microbial etiology of nosocomial infection. Am J Med 91:72s–75s. doi:10.1016/0002-9343(91)90346-Y
    • (1991) Am J Med , vol.91 , pp. 72s-75s
    • Schaberg, D.R.1    Culver, D.H.2    Gaynes, R.P.3
  • 63
    • 84860389171 scopus 로고    scopus 로고
    • Domain shuffling and module engineering of Listeria phage endolysins for enhanced lytic activity and binding affinity
    • Schmelcher M, Tchang VS, Loessner MJ (2011) Domain shuffling and module engineering of Listeria phage endolysins for enhanced lytic activity and binding affinity. Microb Biotechnol 4:651–662. doi:10.1111/j.1751-7915.2011.00263.x
    • (2011) Microb Biotechnol , vol.4 , pp. 651-662
    • Schmelcher, M.1    Tchang, V.S.2    Loessner, M.J.3
  • 64
    • 84867073569 scopus 로고    scopus 로고
    • Bacteriophage endolysins as novel antimicrobials
    • COI: 1:CAS:528:DC%2BC38XhsVCjtb7F, PID: 23030422
    • Schmelcher M, Donovan DM, Loessner MJ (2012a) Bacteriophage endolysins as novel antimicrobials. Future Microbiol 7:1147–1171. doi:10.2217/fmb.12.97
    • (2012) Future Microbiol , vol.7 , pp. 1147-1171
    • Schmelcher, M.1    Donovan, D.M.2    Loessner, M.J.3
  • 65
    • 84861123085 scopus 로고    scopus 로고
    • Chimeric phage lysins act synergistically with lysostaphin to kill mastitis-causing Staphylococcus aureus in murine mammary glands
    • COI: 1:CAS:528:DC%2BC38XktlOrsbg%3D, PID: 22286996
    • Schmelcher M, Powell AM, Becker SC, Camp MJ, Donovan DM (2012b) Chimeric phage lysins act synergistically with lysostaphin to kill mastitis-causing Staphylococcus aureus in murine mammary glands. Appl Environ Microbiol 78:2297–2305. doi:10.1128/AEM. 07050-11
    • (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
  • 66
    • 0031949637 scopus 로고    scopus 로고
    • Antibacterial efficacy of nisin against multidrug-resistant Gram-positive pathogens
    • COI: 1:CAS:528:DyaK1cXisFGjsr0%3D, PID: 9578160
    • Severina E, Severin A, Tomasz A (1998) Antibacterial efficacy of nisin against multidrug-resistant Gram-positive pathogens. J Antimicrob Chemother 41:341–347. doi:10.1093/jac/41.3.341
    • (1998) J Antimicrob Chemother , vol.41 , pp. 341-347
    • Severina, E.1    Severin, A.2    Tomasz, A.3
  • 67
    • 0037071849 scopus 로고    scopus 로고
    • Modulation of virulence within a pathogenicity island in vancomycin-resistant Enterococcus faecalis
    • COI: 1:CAS:528:DC%2BD38XksVGjtbc%3D, PID: 12066186
    • Shankar N, Baghdayan AS, Gilmore MS (2002) Modulation of virulence within a pathogenicity island in vancomycin-resistant Enterococcus faecalis. Nature 417:746–750. doi:10.1038/nature00802
    • (2002) Nature , vol.417 , pp. 746-750
    • Shankar, N.1    Baghdayan, A.S.2    Gilmore, M.S.3
  • 69
    • 78650647679 scopus 로고    scopus 로고
    • Bacillus subtilis CwlP of the SP-{beta} prophage has two novel peptidoglycan hydrolase domains, muramidase and cross-linkage digesting DD-endopeptidase
    • COI: 1:CAS:528:DC%2BC3cXhs1Wju7rJ, PID: 20980266
    • Sudiarta IP, Fukushima T, Sekiguchi J (2010) Bacillus subtilis CwlP of the SP-{beta} prophage has two novel peptidoglycan hydrolase domains, muramidase and cross-linkage digesting DD-endopeptidase. J Biol Chem 285:41232–41243. doi:10.1074/jbc.M110.156273
    • (2010) J Biol Chem , vol.285 , pp. 41232-41243
    • Sudiarta, I.P.1    Fukushima, T.2    Sekiguchi, J.3
  • 70
    • 21444433022 scopus 로고    scopus 로고
    • Phage P68 virion-associated protein 17 displays activity against clinical isolates of Staphylococcus aureus
    • PID: 15980371
    • Takác M, Bläsi U (2005) Phage P68 virion-associated protein 17 displays activity against clinical isolates of Staphylococcus aureus. Antimicrob Agents Chemother 49:2934–2940. doi:10.1128/AAC. 49.7.2934-2940.2005
    • (2005) Antimicrob Agents Chemother , vol.49 , pp. 2934-2940
    • Takác, M.1    Bläsi, U.2
  • 71
    • 84858282874 scopus 로고    scopus 로고
    • Accelerating resistance, inadequate antibacterial drug pipelines and international responses
    • COI: 1:CAS:528:DC%2BC38XjtVOhsrw%3D, PID: 22341298
    • Theuretzbacher U (2012) Accelerating resistance, inadequate antibacterial drug pipelines and international responses. Int J Antimicrob Agents 39:295–299. doi:10.1016/j.ijantimicag.2011.12.006
    • (2012) Int J Antimicrob Agents , vol.39 , pp. 295-299
    • Theuretzbacher, U.1
  • 72
    • 0030970757 scopus 로고    scopus 로고
    • Studies on prolysostaphin processing and characterization of the lysostaphin immunity factor (Lif) of Staphylococcus simulans biovar staphylolyticus
    • COI: 1:CAS:528:DyaK2sXit1ahtbc%3D, PID: 9106216
    • Thumm G, Götz F (1997) Studies on prolysostaphin processing and characterization of the lysostaphin immunity factor (Lif) of Staphylococcus simulans biovar staphylolyticus. Mol Microbiol 23:1251–1265. doi:10.1046/j.1365-2958.1997.2911657.x
    • (1997) Mol Microbiol , vol.23 , pp. 1251-1265
    • Thumm, G.1    Götz, F.2
  • 73
    • 41049116488 scopus 로고    scopus 로고
    • Emergence of CC17 Enterococcus faecium: from commensal to hospital-adapted pathogen
    • COI: 1:CAS:528:DC%2BD1cXks1ahsb4%3D, PID: 18279340
    • Top J, Willems R, Bonten M (2008) Emergence of CC17 Enterococcus faecium: from commensal to hospital-adapted pathogen. FEMS Immunol Med Microbiol 52:297–308. doi:10.1111/j.1574-695X.2008.00383.x
    • (2008) FEMS Immunol Med Microbiol , vol.52 , pp. 297-308
    • Top, J.1    Willems, R.2    Bonten, M.3
  • 74
    • 46949111817 scopus 로고    scopus 로고
    • In silico and in vivo evaluation of bacteriophage ϕEF24C, a candidate for treatment of Enterococcus faecalis infections
    • COI: 1:CAS:528:DC%2BD1cXot1Omt7s%3D, PID: 18456848
    • Uchiyama J, Rashel M, Takemura I, Wakiguchi H, Matsuzaki S (2008) In silico and in vivo evaluation of bacteriophage ϕEF24C, a candidate for treatment of Enterococcus faecalis infections. Appl Environ Microbiol 74:4149–4163. doi:10.1128/AEM. 02371-07
    • (2008) Appl Environ Microbiol , vol.74 , pp. 4149-4163
    • Uchiyama, J.1    Rashel, M.2    Takemura, I.3    Wakiguchi, H.4    Matsuzaki, S.5
  • 75
    • 84855759113 scopus 로고    scopus 로고
    • Role of bacteriophage SPP1 tail spike protein gp21 on host cell receptor binding and trigger of phage DNA ejection
    • COI: 1:CAS:528:DC%2BC38XitVens7s%3D, PID: 22171743
    • Vinga I, Baptista C, Auzat I, Petipas I, Lurz R, Tavares P, Santos MA, São-José C (2012) Role of bacteriophage SPP1 tail spike protein gp21 on host cell receptor binding and trigger of phage DNA ejection. Mol Microbiol 83:289–303. doi:10.1111/j.1365-2958.2011.07931.x
    • (2012) Mol Microbiol , vol.83 , pp. 289-303
    • Vinga, I.1    Baptista, C.2    Auzat, I.3    Petipas, I.4    Lurz, R.5    Tavares, P.6    Santos, M.A.7    São-José, C.8
  • 76
    • 84868028806 scopus 로고    scopus 로고
    • Proteomic response of Bacillus subtilis to lantibiotics reflects differences in interaction with the cytoplasmic membrane
    • COI: 1:CAS:528:DC%2BC38XhsF2iurjI, PID: 22926563
    • Wenzel M, Kohl B, Münch D, Raatschen N, Albada HB, Hamoen L, Metzler-Nolte N, Sahl HG, Bandow JE (2012) Proteomic response of Bacillus subtilis to lantibiotics reflects differences in interaction with the cytoplasmic membrane. Antimicrob Agents Chemother 56:5749–5757. doi:10.1128/AAC. 01380-12
    • (2012) Antimicrob Agents Chemother , vol.56 , pp. 5749-5757
    • Wenzel, M.1    Kohl, B.2    Münch, D.3    Raatschen, N.4    Albada, H.B.5    Hamoen, L.6    Metzler-Nolte, N.7    Sahl, H.G.8    Bandow, J.E.9
  • 78
    • 84891543534 scopus 로고    scopus 로고
    • Novel chimeric lysin with high-level antimicrobial activity against methicillin-resistant Staphylococcus aureus in vitro and in vivo
    • PID: 24189265
    • Yang H, Zhang Y, Yu J, Huang Y, Zhang XE, Wei H (2014) Novel chimeric lysin with high-level antimicrobial activity against methicillin-resistant Staphylococcus aureus in vitro and in vivo. Antimicrob Agents Chemother 58:536–542. doi:10.1128/AAC. 01793-13
    • (2014) Antimicrob Agents Chemother , vol.58 , pp. 536-542
    • Yang, H.1    Zhang, Y.2    Yu, J.3    Huang, Y.4    Zhang, X.E.5    Wei, H.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.