메뉴 건너뛰기




Volumn 10, Issue 5, 2007, Pages 461-472

Taking aim on bacterial pathogens: from phage therapy to enzybiotics

Author keywords

[No Author keywords available]

Indexed keywords

ANTIBIOTIC AGENT; DISPERSIN B; ENDOLYSIN; ENZYME; HYDROLASE; LYSOSTAPHIN; PEPTIDOGLYCAN; PSEUDOMONIC ACID; UNCLASSIFIED DRUG;

EID: 35948990424     PISSN: 13695274     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.mib.2007.08.002     Document Type: Review
Times cited : (215)

References (62)
  • 1
    • 30644463696 scopus 로고    scopus 로고
    • Phage therapy: facts and fiction
    • Skurnik M., and Strauch E. Phage therapy: facts and fiction. Int J Med Microbiol 296 (2006) 5-14
    • (2006) Int J Med Microbiol , vol.296 , pp. 5-14
    • Skurnik, M.1    Strauch, E.2
  • 2
    • 34250892577 scopus 로고    scopus 로고
    • Bacteriophages: an appraisal of their role in the treatment of bacterial infections
    • Hanlon G.W. Bacteriophages: an appraisal of their role in the treatment of bacterial infections. Int J Antimicrob Agents 30 (2007) 118-128
    • (2007) Int J Antimicrob Agents , vol.30 , pp. 118-128
    • Hanlon, G.W.1
  • 3
    • 33645135864 scopus 로고    scopus 로고
    • Bacteriophage precision drug against bacterial infections
    • Sandeep K. Bacteriophage precision drug against bacterial infections. Curr Sci 90 (2006) 361-363
    • (2006) Curr Sci , vol.90 , pp. 361-363
    • Sandeep, K.1
  • 4
    • 33646596612 scopus 로고    scopus 로고
    • Bacteriophages and biotechnology: vaccines, gene therapy and antibacterials
    • Clark J.R., and March J.B. Bacteriophages and biotechnology: vaccines, gene therapy and antibacterials. Trends Biotechnol 24 (2006) 212-218
    • (2006) Trends Biotechnol , vol.24 , pp. 212-218
    • Clark, J.R.1    March, J.B.2
  • 5
    • 33845688395 scopus 로고    scopus 로고
    • Reinventing phage therapy: are the parts greater than the sum?
    • Fischetti V.A., Nelson D., and Schuch R. Reinventing phage therapy: are the parts greater than the sum?. Nat Biotechnol 12 (2006) 1508-1511
    • (2006) Nat Biotechnol , vol.12 , pp. 1508-1511
    • Fischetti, V.A.1    Nelson, D.2    Schuch, R.3
  • 6
    • 58749117049 scopus 로고    scopus 로고
    • Introduction
    • Kutter E., and Sulakvelidze A. (Eds), CRC Press, Boca Raton
    • Kutter E., and Sulakvelidze A. Introduction. In: Kutter E., and Sulakvelidze A. (Eds). Bacteriophages Biology and Applications (2005), CRC Press, Boca Raton 1-4
    • (2005) Bacteriophages Biology and Applications , pp. 1-4
    • Kutter, E.1    Sulakvelidze, A.2
  • 7
    • 0347356354 scopus 로고    scopus 로고
    • Old dogma, new tricks-21st century phage therapy
    • Thiel K. Old dogma, new tricks-21st century phage therapy. Nat Biotechnol 22 (2004) 31-36
    • (2004) Nat Biotechnol , vol.22 , pp. 31-36
    • Thiel, K.1
  • 8
    • 15244342831 scopus 로고    scopus 로고
    • The potential role of endogenous bacteriophages in controlling invading pathogens
    • Górski A., and Weber-Da{ogonek}browska B. The potential role of endogenous bacteriophages in controlling invading pathogens. Cell Mol Life Sci 62 (2005) 511-519
    • (2005) Cell Mol Life Sci , vol.62 , pp. 511-519
    • Górski, A.1    Weber-Dabrowska, B.2
  • 11
    • 0034774475 scopus 로고    scopus 로고
    • Phages of dairy bacteria
    • Brüssow H. Phages of dairy bacteria. Annu Rev Microbiol 55 (2001) 283-303
    • (2001) Annu Rev Microbiol , vol.55 , pp. 283-303
    • Brüssow, H.1
  • 12
    • 0035120334 scopus 로고    scopus 로고
    • Bacteriophage K1-5 encodes two different tail fiber proteins, allowing it to infect and replicate on both K1 and K5 strains of Escherichia coli
    • Scholl D., Rogers S., Adhya S., and Merril C. Bacteriophage K1-5 encodes two different tail fiber proteins, allowing it to infect and replicate on both K1 and K5 strains of Escherichia coli. J Virol 75 (2001) 2509-2515
    • (2001) J Virol , vol.75 , pp. 2509-2515
    • Scholl, D.1    Rogers, S.2    Adhya, S.3    Merril, C.4
  • 13
    • 34547448587 scopus 로고    scopus 로고
    • Dispersing biofilms with engineered enzymatic bacteriophage
    • A study that reveals that an engineered phage expressing biofilm-degrading enzymes is more efficient at removing bacterial biofilms than non-enzymatic phage alone. This treatment may become an additional tool to the standard therapies for use against bacterial biofilms in different settings.
    • Lu T.K., and Collins J.J. Dispersing biofilms with engineered enzymatic bacteriophage. Proc Natl Acad Sci USA 104 (2007) 11197-11202. A study that reveals that an engineered phage expressing biofilm-degrading enzymes is more efficient at removing bacterial biofilms than non-enzymatic phage alone. This treatment may become an additional tool to the standard therapies for use against bacterial biofilms in different settings.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 11197-11202
    • Lu, T.K.1    Collins, J.J.2
  • 14
    • 2142758676 scopus 로고    scopus 로고
    • Prevention and cure of systemic Escherichia coli K1 infection by modification of the bacterial phenotype
    • Mushtaq N., Redpath M.B., Luzio J.P., and Taylor P.W. Prevention and cure of systemic Escherichia coli K1 infection by modification of the bacterial phenotype. Antimicrob Agents Chemother 48 (2004) 1503-1508
    • (2004) Antimicrob Agents Chemother , vol.48 , pp. 1503-1508
    • Mushtaq, N.1    Redpath, M.B.2    Luzio, J.P.3    Taylor, P.W.4
  • 15
    • 13244295472 scopus 로고    scopus 로고
    • The use of a novel biodegradable preparation capable of the sustained release of bacteriophages and ciprofloxacin, in the complex treatment of multidrug-resistant Staphylococcus aureus-infected local radiation injuries caused by exposure to Sr90
    • Jikia D., Chkhaidze N., Imedashvili E., Mgaloblishvili I., Tsilanadze G., Katsarava R., Morris Jr. J.G., and Sulakvelidze A. The use of a novel biodegradable preparation capable of the sustained release of bacteriophages and ciprofloxacin, in the complex treatment of multidrug-resistant Staphylococcus aureus-infected local radiation injuries caused by exposure to Sr90. Clin Exp Dermatol 30 (2005) 23-26
    • (2005) Clin Exp Dermatol , vol.30 , pp. 23-26
    • Jikia, D.1    Chkhaidze, N.2    Imedashvili, E.3    Mgaloblishvili, I.4    Tsilanadze, G.5    Katsarava, R.6    Morris Jr., J.G.7    Sulakvelidze, A.8
  • 16
    • 33645227952 scopus 로고    scopus 로고
    • Bacteriophage endolysins as a novel class of antibacterial agents
    • Borysowski J., Weber-Da{ogonek}browska B., and Górski A. Bacteriophage endolysins as a novel class of antibacterial agents. Exp Biol Med 231 (2006) 366-377
    • (2006) Exp Biol Med , vol.231 , pp. 366-377
    • Borysowski, J.1    Weber-Dabrowska, B.2    Górski, A.3
  • 17
    • 22544471225 scopus 로고    scopus 로고
    • Bacteriophage endolysins-current state of research and applications
    • Loessner M.J. Bacteriophage endolysins-current state of research and applications. Curr Opin Microbiol 8 (2005) 480-487
    • (2005) Curr Opin Microbiol , vol.8 , pp. 480-487
    • Loessner, M.J.1
  • 18
    • 1442300823 scopus 로고    scopus 로고
    • Peptidoglycan hydrolytic activities associated with bacteriophage virions
    • Moak M., and Molineux I.J. Peptidoglycan hydrolytic activities associated with bacteriophage virions. Mol Microbiol 51 (2004) 1169-1183
    • (2004) Mol Microbiol , vol.51 , pp. 1169-1183
    • Moak, M.1    Molineux, I.J.2
  • 19
    • 13444283414 scopus 로고    scopus 로고
    • Control of bacteriophage T4 tail lysozyme activity during the infection process
    • Kanamaru S., Ishiwata Y., Suzuki T., Rossmann M.G., and Arisaka F. Control of bacteriophage T4 tail lysozyme activity during the infection process. J Mol Biol (2005) 1013-1020
    • (2005) J Mol Biol , pp. 1013-1020
    • Kanamaru, S.1    Ishiwata, Y.2    Suzuki, T.3    Rossmann, M.G.4    Arisaka, F.5
  • 20
    • 33746087272 scopus 로고    scopus 로고
    • PlyC: a multimeric bacteriophage lysine
    • This study describes the first example of a multimeric endolysin composed of two separate gene products.
    • Nelson D., Schuch R., Chahales P., Zhu S., and Fischetti V.A. PlyC: a multimeric bacteriophage lysine. Proc Natl Acad Sci USA 103 (2006) 10765-10770. This study describes the first example of a multimeric endolysin composed of two separate gene products.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 10765-10770
    • Nelson, D.1    Schuch, R.2    Chahales, P.3    Zhu, S.4    Fischetti, V.A.5
  • 21
    • 39649099979 scopus 로고    scopus 로고
    • Scheurwater E, Reid CW, Clarke AJ: Lytic transglycosylases: Bacterial space-making autolysins. Int J Biochem Cell Biol 2007, doi:10.1016/j.biocel.2007.03.018, in press.
  • 22
    • 11844266530 scopus 로고    scopus 로고
    • Disulfide isomerization after membrane release of its SAR domain activates P1 lysozyme
    • A very interesting study showing the structural changes involved in export and activation of the secreted but transiently membrane-tethered P1 signal arrest release (SAR) endolysin.
    • Xu M., Arulandu A., Struck D.K., Swanson S., Sacchettini J.C., and Young R. Disulfide isomerization after membrane release of its SAR domain activates P1 lysozyme. Science 307 (2005) 113-117. A very interesting study showing the structural changes involved in export and activation of the secreted but transiently membrane-tethered P1 signal arrest release (SAR) endolysin.
    • (2005) Science , vol.307 , pp. 113-117
    • Xu, M.1    Arulandu, A.2    Struck, D.K.3    Swanson, S.4    Sacchettini, J.C.5    Young, R.6
  • 23
    • 33846443610 scopus 로고    scopus 로고
    • Coliphage N4 N-acetylmuramidase defines a new family of murein hydrolases
    • This study describes a new coliphage-encoded murein hydrolase that localizes primarily to the cell inner membrane and that represents the first primary structure of a new family of muramidases.
    • Stojković E.A., and Rothman-Denes L.B. Coliphage N4 N-acetylmuramidase defines a new family of murein hydrolases. J Mol Biol 366 (2007) 406-419. This study describes a new coliphage-encoded murein hydrolase that localizes primarily to the cell inner membrane and that represents the first primary structure of a new family of muramidases.
    • (2007) J Mol Biol , vol.366 , pp. 406-419
    • Stojković, E.A.1    Rothman-Denes, L.B.2
  • 24
    • 0037727706 scopus 로고    scopus 로고
    • Amidase domains from bacterial and phage autolysins define a family of γ-d,l-glutamate-specific amidohydrolases
    • Rigden D.J., Jedrzejas M.J., and Galperin M.Y. Amidase domains from bacterial and phage autolysins define a family of γ-d,l-glutamate-specific amidohydrolases. Trends Biochem Sci 28 (2003) 230-234
    • (2003) Trends Biochem Sci , vol.28 , pp. 230-234
    • Rigden, D.J.1    Jedrzejas, M.J.2    Galperin, M.Y.3
  • 25
    • 7944231131 scopus 로고    scopus 로고
    • Recent trends on the molecular biology of pneumococcal capsules, lytic enzymes, and bacteriophage
    • López R., and García E. Recent trends on the molecular biology of pneumococcal capsules, lytic enzymes, and bacteriophage. FEMS Microbiol Rev 28 (2004) 553-580
    • (2004) FEMS Microbiol Rev , vol.28 , pp. 553-580
    • López, R.1    García, E.2
  • 29
    • 33751529207 scopus 로고    scopus 로고
    • Insights into molecular plasticity of choline binding proteins (pneumococcal surface proteins) by SAXS
    • Buey R.M., Monterroso B., Menéndez M., Diakun G., Chacón P., Hermoso J.A., and Díaz J.F. Insights into molecular plasticity of choline binding proteins (pneumococcal surface proteins) by SAXS. J Mol Biol 365 (2007) 411-424
    • (2007) J Mol Biol , vol.365 , pp. 411-424
    • Buey, R.M.1    Monterroso, B.2    Menéndez, M.3    Diakun, G.4    Chacón, P.5    Hermoso, J.A.6    Díaz, J.F.7
  • 31
    • 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., and Hilgenfeld R. A new lysozyme fold. Crystal structure of the muramidase from Streptomyces coelicolor at 1.65 Å resolution. J Biol Chem 276 (2001) 31994-31999
    • (2001) J Biol Chem , vol.276 , pp. 31994-31999
    • Rau, A.1    Hogg, T.2    Marquardt, R.3    Hilgenfeld, R.4
  • 32
    • 33644852491 scopus 로고    scopus 로고
    • Cell wall-targeting domain of glycylglycine endopeptidase distinguishes among peptidoglycan cross-bridges
    • Lu J.Z., Fujiwara T., Komatsuzawa H., Sugai M., and Sakon J. Cell wall-targeting domain of glycylglycine endopeptidase distinguishes among peptidoglycan cross-bridges. J Biol Chem 281 (2006) 549-558
    • (2006) J Biol Chem , vol.281 , pp. 549-558
    • Lu, J.Z.1    Fujiwara, T.2    Komatsuzawa, H.3    Sugai, M.4    Sakon, J.5
  • 33
    • 33644869510 scopus 로고    scopus 로고
    • Extension to 2268 atoms of direct methods in the ab initio determination of the unknown structure of bacteriophage P22 lysozyme
    • Mooers B.H.M., and Matthews B.W. Extension to 2268 atoms of direct methods in the ab initio determination of the unknown structure of bacteriophage P22 lysozyme. Acta Cryst Sect D 62 (2006) 165-176
    • (2006) Acta Cryst Sect D , vol.62 , pp. 165-176
    • Mooers, B.H.M.1    Matthews, B.W.2
  • 34
    • 27444432629 scopus 로고    scopus 로고
    • Structure and lytic activity of a Bacillus anthracis prophage endolysin
    • This study presents the crystal structure of the catalytic module of PlyL endolysin. Lytic activity of the catalytic module is higher than full-length protein. Authors propose an interesting model in which cell wall binding module only allows the catalytic module to function in the presence of a specific cell wall.
    • Low L.Y., Yang C., Perego M., Osterman A., and Liddington R.C. Structure and lytic activity of a Bacillus anthracis prophage endolysin. J Biol Chem 280 (2005) 35433-35439. This study presents the crystal structure of the catalytic module of PlyL endolysin. Lytic activity of the catalytic module is higher than full-length protein. Authors propose an interesting model in which cell wall binding module only allows the catalytic module to function in the presence of a specific cell wall.
    • (2005) J Biol Chem , vol.280 , pp. 35433-35439
    • Low, L.Y.1    Yang, C.2    Perego, M.3    Osterman, A.4    Liddington, R.C.5
  • 35
    • 0028223308 scopus 로고
    • The structure of bacteriophage T7 lysozyme, a zinc amidase and an inhibitor of T7 RNA polymerase
    • Cheng X., Zhang X., Pflugrath J.W., and Studier F.W. The structure of bacteriophage T7 lysozyme, a zinc amidase and an inhibitor of T7 RNA polymerase. Proc Natl Acad Sci USA 91 (1994) 4034-4038
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 4034-4038
    • Cheng, X.1    Zhang, X.2    Pflugrath, J.W.3    Studier, F.W.4
  • 36
    • 0345269183 scopus 로고    scopus 로고
    • NMR structure of Citrobacter freundii AmpD, comparison with bacteriophage T7 lysozyme and homology with PGRP domains
    • Liepinsh E., Genereux C., Dehareng D., Joris B., and Otting G. NMR structure of Citrobacter freundii AmpD, comparison with bacteriophage T7 lysozyme and homology with PGRP domains. J Mol Biol 327 (2003) 833-842
    • (2003) J Mol Biol , vol.327 , pp. 833-842
    • Liepinsh, E.1    Genereux, C.2    Dehareng, D.3    Joris, B.4    Otting, G.5
  • 37
    • 0042195829 scopus 로고    scopus 로고
    • Crystal structure of peptidoglycan recognition protein LB from Drosophila melanogaster
    • Kim M.S., Byun M., and Oh B.H. Crystal structure of peptidoglycan recognition protein LB from Drosophila melanogaster. Nat Immunol 4 (2003) 787-793
    • (2003) Nat Immunol , vol.4 , pp. 787-793
    • Kim, M.S.1    Byun, M.2    Oh, B.H.3
  • 38
    • 33751066117 scopus 로고    scopus 로고
    • The crystal structure of the bacteriophage PSA endolysin reveals a unique fold responsible for specific recognition of Listeria cell walls
    • This study presents the complete structure of an endolysin (PlyPSA), carrying both the catalytic and cell wall binding (CWBM) modules. The CWBM features a novel fold that has an internal duplication of a β-barrel-like motif.
    • Korndörfer I.P., Danzer J., Schmelcher M., Zimmer M., Skerra A., and Loessner M.J. The crystal structure of the bacteriophage PSA endolysin reveals a unique fold responsible for specific recognition of Listeria cell walls. J Mol Biol 364 (2006) 678-689. This study presents the complete structure of an endolysin (PlyPSA), carrying both the catalytic and cell wall binding (CWBM) modules. The CWBM features a novel fold that has an internal duplication of a β-barrel-like motif.
    • (2006) J Mol Biol , vol.364 , pp. 678-689
    • Korndörfer, I.P.1    Danzer, J.2    Schmelcher, M.3    Zimmer, M.4    Skerra, A.5    Loessner, M.J.6
  • 40
    • 34548300011 scopus 로고    scopus 로고
    • Elucidation of the molecular recognition of bacterial cell wall by modular pneumococcal phage endolysin CPL-1
    • This report provides for the first time a structural picture at the atomic level of the interaction between a pneumococcal endolysin (Cpl-1) and its substrate, the bacterial peptidoglycan. This work demonstrates how this enzyme recognizes the peptidoglycan and reveals in detail the complexity underlying the binding and the mechanism of the hydrolytic activity of Cpl-1. This analysis is the first for a member of the glycosyl hydrolase family 25.
    • Pérez-Dorado I., Campillo N.E., Monterroso B., Hesek D., Lee M., Páez J.A., García P., Martínez-Ripoll M., García J.L., Mobashery S., et al. Elucidation of the molecular recognition of bacterial cell wall by modular pneumococcal phage endolysin CPL-1. J Biol Chem 282 (2007) 24990-24999. This report provides for the first time a structural picture at the atomic level of the interaction between a pneumococcal endolysin (Cpl-1) and its substrate, the bacterial peptidoglycan. This work demonstrates how this enzyme recognizes the peptidoglycan and reveals in detail the complexity underlying the binding and the mechanism of the hydrolytic activity of Cpl-1. This analysis is the first for a member of the glycosyl hydrolase family 25.
    • (2007) J Biol Chem , vol.282 , pp. 24990-24999
    • Pérez-Dorado, I.1    Campillo, N.E.2    Monterroso, B.3    Hesek, D.4    Lee, M.5    Páez, J.A.6    García, P.7    Martínez-Ripoll, M.8    García, J.L.9    Mobashery, S.10
  • 42
    • 0000287448 scopus 로고
    • Studies on bacteriophages of hemolytic streptococci. I. Factors influencing the interaction of phage and susceptible host cell
    • Krause R.M. Studies on bacteriophages of hemolytic streptococci. I. Factors influencing the interaction of phage and susceptible host cell. J Exp Med 106 (1957) 365-384
    • (1957) J Exp Med , vol.106 , pp. 365-384
    • Krause, R.M.1
  • 43
    • 0035957329 scopus 로고    scopus 로고
    • Prevention and elimination colonization of mice by group A streptococci by using a bacteriophage lytic enzyme
    • Nelson D., Loomis L., and Fischetti V.A. Prevention and elimination colonization of mice by group A streptococci by using a bacteriophage lytic enzyme. Proc Natl Acad Sci USA 98 (2001) 4107-4112
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 4107-4112
    • Nelson, D.1    Loomis, L.2    Fischetti, V.A.3
  • 44
    • 3042856527 scopus 로고    scopus 로고
    • Identification of a broadly active phage lytic enzyme with lethal activity against antibiotic-resistant Enterococcus faecalis and Enterococcus faecium
    • Yoong P., Schuch R., Nelson D., and Fischetti V.A. Identification of a broadly active phage lytic enzyme with lethal activity against antibiotic-resistant Enterococcus faecalis and Enterococcus faecium. J Bacteriol 186 (2004) 4808-4812
    • (2004) J Bacteriol , vol.186 , pp. 4808-4812
    • Yoong, P.1    Schuch, R.2    Nelson, D.3    Fischetti, V.A.4
  • 45
    • 0036840423 scopus 로고    scopus 로고
    • The murein hydrolase of the bacteriophage φ{symbol}3626 dual lysis system is active against all tested Clostridium perfringens strains
    • Zimmer M., Vukov N., Scherer S., and Loessner M.J. The murein hydrolase of the bacteriophage φ{symbol}3626 dual lysis system is active against all tested Clostridium perfringens strains. Appl Environ Microbiol 68 (2002) 5311-5317
    • (2002) Appl Environ Microbiol , vol.68 , pp. 5311-5317
    • Zimmer, M.1    Vukov, N.2    Scherer, S.3    Loessner, M.J.4
  • 46
    • 11244288460 scopus 로고    scopus 로고
    • Removal of group B streptococci colonizing the vagina and oropharynx of mice with a bacteriophage lytic enzyme
    • Cheng Q., Nelson D., Zhu S., and Fischetti V.A. Removal of group B streptococci colonizing the vagina and oropharynx of mice with a bacteriophage lytic enzyme. Antimicrob Agents Chemother 49 (2005) 111-117
    • (2005) Antimicrob Agents Chemother , vol.49 , pp. 111-117
    • Cheng, Q.1    Nelson, D.2    Zhu, S.3    Fischetti, V.A.4
  • 47
    • 0037158695 scopus 로고    scopus 로고
    • A bacteriolytic agent that detects and kills Bacillus anthracis
    • Schuch R., Nelson D., and Fischetti V.A. A bacteriolytic agent that detects and kills Bacillus anthracis. Nature 418 (2002) 884-889
    • (2002) Nature , vol.418 , pp. 884-889
    • Schuch, R.1    Nelson, D.2    Fischetti, V.A.3
  • 48
    • 10744225724 scopus 로고    scopus 로고
    • Phage lytic enzymes as therapy for antibiotic resistant Streptococcus pneumoniae infection in a murine sepsis model
    • Jado I., López R., García E., Fenoll A., Casal J., and García P. Phage lytic enzymes as therapy for antibiotic resistant Streptococcus pneumoniae infection in a murine sepsis model. J Antimicrob Chemother 52 (2003) 967-973
    • (2003) J Antimicrob Chemother , vol.52 , pp. 967-973
    • Jado, I.1    López, R.2    García, E.3    Fenoll, A.4    Casal, J.5    García, P.6
  • 49
    • 34047201129 scopus 로고    scopus 로고
    • Novel strategy to prevent otitis media caused by colonizing Streptococcus pneumoniae
    • An elegant study from Fischetti's lab where the first mouse model of acute otitis media in which infection develops similarly to that observed in children was set up. Once again, purified Cpl-1, the lysozyme encoded by the pneumococcal phage Cp-1, demonstrated its potent killing effect against pneumococci.
    • McCullers J.A., Karlström Ǻ., Iverson A.R., Loeffler J.M., and Fischetti V.A. Novel strategy to prevent otitis media caused by colonizing Streptococcus pneumoniae. PLoS Pathog 3 (2007) e28. An elegant study from Fischetti's lab where the first mouse model of acute otitis media in which infection develops similarly to that observed in children was set up. Once again, purified Cpl-1, the lysozyme encoded by the pneumococcal phage Cp-1, demonstrated its potent killing effect against pneumococci.
    • (2007) PLoS Pathog , vol.3
    • McCullers, J.A.1    Karlström, Ǻ.2    Iverson, A.R.3    Loeffler, J.M.4    Fischetti, V.A.5
  • 50
    • 0038673555 scopus 로고    scopus 로고
    • Lysostaphin cream eradicates Staphylococcus aureus nasal colonization in a cotton rat model
    • Kokai-Kun J.F., Walsh S.M., Chanturiya T., and Mond J.J. Lysostaphin cream eradicates Staphylococcus aureus nasal colonization in a cotton rat model. Antimicrob Agents Chemother 47 (2003) 1589-1597
    • (2003) Antimicrob Agents Chemother , vol.47 , pp. 1589-1597
    • Kokai-Kun, J.F.1    Walsh, S.M.2    Chanturiya, T.3    Mond, J.J.4
  • 51
    • 33845701683 scopus 로고    scopus 로고
    • Antimicrobial activity of lysostaphin and a Listeria monocytogenes bacteriophage endolysin produced and secreted by lactic acid bacteria
    • Turner M.S., Waldherr F., Loessner M.J., and Giffard P.M. Antimicrobial activity of lysostaphin and a Listeria monocytogenes bacteriophage endolysin produced and secreted by lactic acid bacteria. Syst Appl Microbiol 30 (2007) 58-67
    • (2007) Syst Appl Microbiol , vol.30 , pp. 58-67
    • Turner, M.S.1    Waldherr, F.2    Loessner, M.J.3    Giffard, P.M.4
  • 53
    • 35948931348 scopus 로고    scopus 로고
    • Pneumococcal LytA autolysin, a potent therapeutic agent in experimental peritonitis-sepsis caused by highly β-lactam-resistant Streptococcus pneumoniae
    • The first demonstration of the powerful action of the purified major pneumococcal autolysin, amidase LytA, to act as a true enzybiotic in a mouse model.
    • Rodríguez-Cerrato V., García P., Huelves L., García E., del Prado G., Gracia M., Ponte C., López R., and Soriano F. Pneumococcal LytA autolysin, a potent therapeutic agent in experimental peritonitis-sepsis caused by highly β-lactam-resistant Streptococcus pneumoniae. Antimicrob Agents Chemother 51 (2007) 3371-3373. The first demonstration of the powerful action of the purified major pneumococcal autolysin, amidase LytA, to act as a true enzybiotic in a mouse model.
    • (2007) Antimicrob Agents Chemother , vol.51 , pp. 3371-3373
    • Rodríguez-Cerrato, V.1    García, P.2    Huelves, L.3    García, E.4    del Prado, G.5    Gracia, M.6    Ponte, C.7    López, R.8    Soriano, F.9
  • 54
    • 0242286566 scopus 로고    scopus 로고
    • Phage lytic enzyme Cpl-1 as a novel antimicrobial for pneumococcal bacteremia
    • Loeffler J.M., Djurkovic S., and Fischetti V.A. Phage lytic enzyme Cpl-1 as a novel antimicrobial for pneumococcal bacteremia. Infect Immun 71 (2003) 6199-6204
    • (2003) Infect Immun , vol.71 , pp. 6199-6204
    • Loeffler, J.M.1    Djurkovic, S.2    Fischetti, V.A.3
  • 55
  • 56
    • 0037379524 scopus 로고    scopus 로고
    • Use of genetically engineered phage to deliver antimicrobial agents to bacteria: an alternative therapy for treatment of bacterial infections
    • Westwater C., Kasman L.M., Schofield D.A., Werner P.A., Dolan J.W., Schmidt M.G., and Norris J.S. Use of genetically engineered phage to deliver antimicrobial agents to bacteria: an alternative therapy for treatment of bacterial infections. Antimicrob Agents Chemother 47 (2003) 1301-1307
    • (2003) Antimicrob Agents Chemother , vol.47 , pp. 1301-1307
    • Westwater, C.1    Kasman, L.M.2    Schofield, D.A.3    Werner, P.A.4    Dolan, J.W.5    Schmidt, M.G.6    Norris, J.S.7
  • 57
    • 33751234484 scopus 로고    scopus 로고
    • Augmentation of the antimicrobial efficacy of antibiotics by filamentous phage
    • Hagens S., Habel A., and Bläsi U. Augmentation of the antimicrobial efficacy of antibiotics by filamentous phage. Microb Drug Resist 12 (2006) 164-168
    • (2006) Microb Drug Resist , vol.12 , pp. 164-168
    • Hagens, S.1    Habel, A.2    Bläsi, U.3
  • 59
    • 0035824437 scopus 로고    scopus 로고
    • Rapid killing of Streptococcus pneumoniae with a bacteriophage cell wall hydrolase
    • Loeffler J.M., Nelson D., and Fischetti V.A. Rapid killing of Streptococcus pneumoniae with a bacteriophage cell wall hydrolase. Science 294 (2001) 2170-2172
    • (2001) Science , vol.294 , pp. 2170-2172
    • Loeffler, J.M.1    Nelson, D.2    Fischetti, V.A.3
  • 60
    • 14744269239 scopus 로고    scopus 로고
    • Synergistic killing of Streptococcus pneumoniae with the bacteriophage lytic enzyme Cpl-1 and penicillin or gentamicin depends on the level of penicillin resistance
    • Djurkovic S., Loeffler J.M., and Fischetti V.A. Synergistic killing of Streptococcus pneumoniae with the bacteriophage lytic enzyme Cpl-1 and penicillin or gentamicin depends on the level of penicillin resistance. Antimicrob Agents Chemother 49 (2005) 1225-1228
    • (2005) Antimicrob Agents Chemother , vol.49 , pp. 1225-1228
    • Djurkovic, S.1    Loeffler, J.M.2    Fischetti, V.A.3
  • 61
    • 35448950078 scopus 로고    scopus 로고
    • In vitro interactions of LytA, the major pneumococcal autolysin, with two bacteriophage lytic enzymes (Cpl-1 and Pal), cefotaxime and moxifloxacin against antibiotic-susceptible and -resistant Streptococcus pneumoniae strains
    • Rodríguez-Cerrato V., García P., del Prado G., García E., Gracia M., Huelves L., Ponte C., López R., and Soriano F. In vitro interactions of LytA, the major pneumococcal autolysin, with two bacteriophage lytic enzymes (Cpl-1 and Pal), cefotaxime and moxifloxacin against antibiotic-susceptible and -resistant Streptococcus pneumoniae strains. J Antimicr Chemother 60 (2007) 1159-1162
    • (2007) J Antimicr Chemother , vol.60 , pp. 1159-1162
    • Rodríguez-Cerrato, V.1    García, P.2    del Prado, G.3    García, E.4    Gracia, M.5    Huelves, L.6    Ponte, C.7    López, R.8    Soriano, F.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.