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Volumn 3, Issue 4, 2010, Pages 1139-1161

Lysostaphin: A staphylococcal bacteriolysin with potential clinical applications

Author keywords

Antimicrobial peptides; Bacteriocins; Lysostaphin; Staphylococci; Staphylococcins

Indexed keywords

ANTIINFECTIVE AGENT; BACTROBAN NASAL; BETA LACTAM ANTIBIOTIC; CEFAPIRIN; LYSOSTAPHIN; METICILLIN; NAFCILLIN; NEOSPORIN; PLACEBO; PSEUDOMONIC ACID; UNCLASSIFIED DRUG; VANCOMYCIN;

EID: 77952183463     PISSN: None     EISSN: 14248247     Source Type: Journal    
DOI: 10.3390/ph3041139     Document Type: Review
Times cited : (131)

References (92)
  • 1
    • 35448976652 scopus 로고    scopus 로고
    • The diversity of bacteriocins in Gram-positive bacteria
    • Riley, M.A.; Chavan, M.A., Eds, Springer: New York, NY, USA
    • Heng, N.C.K.; Wescombe, P.A., Burton, J.P.; Jack, R.W.; Tagg, J.R. The diversity of bacteriocins in Gram-positive bacteria. In Bacteriocins: Ecology and Evolution; Riley, M.A.; Chavan, M.A., Eds, Springer: New York, NY, USA, 2007; pp. 45-92.
    • (2007) Bacteriocins: Ecology and Evolution , pp. 45-92
    • Heng, N.C.K.1    Wescombe, P.A.2    Burton, J.P.3    Jack, R.W.4    Tagg, J.R.5
  • 2
    • 65949089371 scopus 로고    scopus 로고
    • Lantibiotics: Mode of action, biosynthesis and bioengineering
    • Bierbaum, G.; Sahl, H.-G. Lantibiotics: mode of action, biosynthesis and bioengineering. Curr. Pharm. Biotechnol. 2009, 10, 2-18.
    • (2009) Curr. Pharm. Biotechnol , vol.10 , pp. 2-18
    • Bierbaum, G.1    Sahl, H.-G.2
  • 3
    • 65149100197 scopus 로고    scopus 로고
    • Structure-function relationships of the non-lanthionine-containing peptide (class II) bacteriocins produced by Gram-positive bacteria
    • Nissen-Meyer, J.; Rogne, P.; Oppegård, C.; Haugen, H.S.; Kristiansen, P.E. Structure-function relationships of the non-lanthionine-containing peptide (class II) bacteriocins produced by Gram-positive bacteria. Curr. Pharm. Biotechnol. 2009, 10, 10-37.
    • (2009) Curr. Pharm. Biotechnol , vol.10 , pp. 10-37
    • Nissen-Meyer, J.1    Rogne, P.2    Oppegård, C.3    Haugen, H.S.4    Kristiansen, P.E.5
  • 4
    • 27244436751 scopus 로고    scopus 로고
    • Bacteriocins: Developing innate immunity for food
    • Cotter, P.D.; Hill, C.; Ross, R.P. Bacteriocins: developing innate immunity for food. Nat. Rev. Microbiol. 2005, 3, 777-788.
    • (2005) Nat. Rev. Microbiol , vol.3 , pp. 777-788
    • Cotter, P.D.1    Hill, C.2    Ross, R.P.3
  • 6
    • 65949109030 scopus 로고    scopus 로고
    • Staphylococcal antimicrobial peptides: Relevant properties and potential biotechnological applications
    • Bastos, M.C.F.; Ceotto, H.; Coelho, M.L.V.; Nascimento, J.S. Staphylococcal antimicrobial peptides: relevant properties and potential biotechnological applications. Curr. Pharm. Biotechnol. 2009, 10, 38-61.
    • (2009) Curr. Pharm. Biotechnol , vol.10 , pp. 38-61
    • Bastos, M.C.F.1    Ceotto, H.2    Coelho, M.L.V.3    Nascimento, J.S.4
  • 7
    • 77952139763 scopus 로고    scopus 로고
    • List of prokaryotic names with standing in nomenclature-Genus
    • accessed April 2010
    • Euzéby, J.P. List of prokaryotic names with standing in nomenclature-Genus Staphylococcus. http://www.bacterio.cict.fr, accessed April 2010.
    • Staphylococcus
    • Euzéby, J.P.1
  • 8
    • 0346649986 scopus 로고    scopus 로고
    • Staphylococcus, Micrococcus, and other catalase-positive cocci
    • In, Murray, P.R.; Baron, E.J.; Jorgensen, J.H.; Landry, M.L.; Pfaller, M.A., Eds.; ASM Press: Washington D.C., USA
    • Bannerman, T.L.; Peacock, S.J. Staphylococcus, Micrococcus, and other catalase-positive cocci. In Manual of Clinical Microbiology; Murray, P.R.; Baron, E.J.; Jorgensen, J.H.; Landry, M.L.; Pfaller, M.A., Eds.; ASM Press: Washington D.C., USA, 2007; pp. 384-404.
    • (2007) Manual of Clinical Microbiology , pp. 384-404
    • Bannerman, T.L.1    Peacock, S.J.2
  • 10
    • 0242595611 scopus 로고    scopus 로고
    • Cycling chemotherapy: A promising approach to reducing the morbidity and mortality of nosocomial infections
    • Evans, H.L.; Saywer, R.G. Cycling chemotherapy: a promising approach to reducing the morbidity and mortality of nosocomial infections. Drugs Today 2003, 39, 733-738.
    • (2003) Drugs Today , vol.39 , pp. 733-738
    • Evans, H.L.1    Saywer, R.G.2
  • 12
    • 0001115492 scopus 로고
    • Lysostaphin: A new bacteriolytic agent for the Staphylococcus
    • Schindler, C.A.; Schuhardt, V.T. Lysostaphin: A new bacteriolytic agent for the Staphylococcus. Proc. Natl. Acad. Sci. USA 1964, 51, 414-421.
    • (1964) Proc. Natl. Acad. Sci. USA , vol.51 , pp. 414-421
    • Schindler, C.A.1    Schuhardt, V.T.2
  • 13
    • 0030716395 scopus 로고    scopus 로고
    • Specificities of FemA and FemB for different glycine residues: FemB cannot substitute for FemA in staphylococcal peptidoglycan pentaglycine side chain formation
    • Ehlert, K.; Schrodr, W.; Labischinski, H. Specificities of FemA and FemB for different glycine residues: FemB cannot substitute for FemA in staphylococcal peptidoglycan pentaglycine side chain formation. J. Bacteriol. 1997, 179, 7573-7576.
    • (1997) J. Bacteriol , vol.179 , pp. 7573-7576
    • Ehlert, K.1    Schrodr, W.2    Labischinski, H.3
  • 14
    • 0033529856 scopus 로고    scopus 로고
    • The essential Staphylococcus aureus gene fmhB is involved in the first step of peptidoglycan pentaglycine interpeptide formation
    • Rohrer, S.; Ehlert, K.; Tschierske, M.; Labischinski, H.; Berger-Bächi, B. The essential Staphylococcus aureus gene fmhB is involved in the first step of peptidoglycan pentaglycine interpeptide formation. Proc. Natl. Acad. Sci. USA. 1999, 96, 9351-9356.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 9351-9356
    • Rohrer, S.1    Ehlert, K.2    Tschierske, M.3    Labischinski, H.4    Berger-Bächi, B.5
  • 15
    • 50849108830 scopus 로고    scopus 로고
    • Lysostaphin: An antistaphylococcal agent
    • Kumar, J.K. Lysostaphin: an antistaphylococcal agent. Appl. Microbiol. Biotechnol. 2008, 80, 555-561.
    • (2008) Appl. Microbiol. Biotechnol , vol.80 , pp. 555-561
    • Kumar, J.K.1
  • 16
    • 0017105779 scopus 로고
    • On the morphogenesis of the cell wall of staphylococci
    • Giesbrecht, P.; Wecke, J.; Recnicke, B. On the morphogenesis of the cell wall of staphylococci. Int. Rev. Cytol. 1976, 44, 225-318.
    • (1976) Int. Rev. Cytol , vol.44 , pp. 225-318
    • Giesbrecht, P.1    Wecke, J.2    Recnicke, B.3
  • 19
    • 0014962782 scopus 로고
    • Molecular properties of lysostaphin, a bacteriolytic agent specific for Staphylococcus aureus
    • Trayer, H.R.; Buckley III, C.E. Molecular properties of lysostaphin, a bacteriolytic agent specific for Staphylococcus aureus. J. Biol. Chem. 1970, 245, 4842-4846.
    • (1970) J. Biol. Chem , vol.245 , pp. 4842-4846
    • Trayer, H.R.1    Buckley III, C.E.2
  • 20
    • 0023429365 scopus 로고
    • The molecular organization of the lysostaphin gene and its sequences repeated in tandem
    • Heinrich, P.; Rosenstein, R.; Bohmer, M.; Sonner, P.; Götz, F. The molecular organization of the lysostaphin gene and its sequences repeated in tandem. Mol. Gen. Genet. 1987, 209, 563-569.
    • (1987) Mol. Gen. Genet , vol.209 , pp. 563-569
    • Heinrich, P.1    Rosenstein, R.2    Bohmer, M.3    Sonner, P.4    Götz, F.5
  • 21
    • 0030970757 scopus 로고    scopus 로고
    • Studies on prolysostaphin processing and characterization of the lysostaphin immunity factor (Lif) of Staphylococcus simulans biovar staphylolyticus
    • Thumm, G.; Götz, F. Studies on prolysostaphin processing and characterization of the lysostaphin immunity factor (Lif) of Staphylococcus simulans biovar staphylolyticus. Mol. Microbiol. 1997, 23, 1251-1265.
    • (1997) Mol. Microbiol , vol.23 , pp. 1251-1265
    • Thumm, G.1    Götz, F.2
  • 22
    • 0030984605 scopus 로고    scopus 로고
    • Cloning and sequence analysis of zooA, a Streptococcus zooepidemicus gene encoding a bacteriocin-like inhibitory substance having a domain structure similar to that of lysostaphin
    • Simmonds, R.S.; Simpson, W.J.; Tagg, J.R. Cloning and sequence analysis of zooA, a Streptococcus zooepidemicus gene encoding a bacteriocin-like inhibitory substance having a domain structure similar to that of lysostaphin. Gene 1997, 189, 255-261.
    • (1997) Gene , vol.189 , pp. 255-261
    • Simmonds, R.S.1    Simpson, W.J.2    Tagg, J.R.3
  • 23
    • 0029790464 scopus 로고    scopus 로고
    • Target cell specificity of a bacteriocin molecule: A C-terminal signal directs lysostaphin to the cell wall of Staphylococcus aureus
    • Baba, T.; Schneewindt, O. Target cell specificity of a bacteriocin molecule: a C-terminal signal directs lysostaphin to the cell wall of Staphylococcus aureus. EMBO J. 1996, 15, 4789-4797.
    • (1996) EMBO J , vol.15 , pp. 4789-4797
    • Baba, T.1    Schneewindt, O.2
  • 24
    • 33645237316 scopus 로고    scopus 로고
    • Cross-linked peptidoglycan mediates lysostaphin binding to the cell wall envelope of Staphylococcus aureus
    • Gründling, A.; Schneewind, O. Cross-linked peptidoglycan mediates lysostaphin binding to the cell wall envelope of Staphylococcus aureus. J. Bacteriol. 2006, 188, 2463-2472.
    • (2006) J. Bacteriol , vol.188 , pp. 2463-2472
    • Gründling, A.1    Schneewind, O.2
  • 25
    • 0023100786 scopus 로고
    • Cloning, sequence, and expression of the lysostaphin gene from Staphylococcus simulans
    • Recsei, P.A.; Gruss, A.D.; Novick, R.P. Cloning, sequence, and expression of the lysostaphin gene from Staphylococcus simulans. Proc. Natl. Acad. Sci. USA 1987, 84, 1127-1131.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 1127-1131
    • Recsei, P.A.1    Gruss, A.D.2    Novick, R.P.3
  • 27
    • 0041350932 scopus 로고
    • Plasmid-encoded lysostaphin endopeptidase gene of Staphylococcus simulans biovar staphylolyticus
    • Heath, S.L.; Heath, H.E.; Sloan, G.L. Plasmid-encoded lysostaphin endopeptidase gene of Staphylococcus simulans biovar staphylolyticus. FEMS Microbiol. Lett. 1987, 44, 129-133.
    • (1987) FEMS Microbiol. Lett , vol.44 , pp. 129-133
    • Heath, S.L.1    Heath, H.E.2    Sloan, G.L.3
  • 28
    • 0024397418 scopus 로고
    • Plasmid-encoded lysostaphin endopeptidase resistance of Staphylococcus simulans biovar staphylolyticus
    • Heath, H.E.; Heath, S.L.; Nitterauer, J.D.; Rose, K.E.; Sloan, G.L. Plasmid-encoded lysostaphin endopeptidase resistance of Staphylococcus simulans biovar staphylolyticus. Biochem. Biophys. Res. Commun. 1989, 160, 1106-1109.
    • (1989) Biochem. Biophys. Res. Commun , vol.160 , pp. 1106-1109
    • Heath, H.E.1    Heath, S.L.2    Nitterauer, J.D.3    Rose, K.E.4    Sloan, G.L.5
  • 29
    • 0028230459 scopus 로고
    • Expression of the lysostaphin gene of Staphylococcus simulans in a eukaryotic system
    • Williamson, C.M.; Bramley, A.J.; Lax, A.J. Expression of the lysostaphin gene of Staphylococcus simulans in a eukaryotic system. Appl. Environ. Microbiol. 1994, 60, 771-776.
    • (1994) Appl. Environ. Microbiol , vol.60 , pp. 771-776
    • Williamson, C.M.1    Bramley, A.J.2    Lax, A.J.3
  • 30
    • 26844475027 scopus 로고    scopus 로고
    • Industrial scale production and purification of a heterologous protein in Lactococcus lactis using the nisin-controlled gene expression system NICE: The case of lysostaphin
    • Mierau, I.; Leij, P.; van Swam, I.; Blommestein, B.; Floris, E.; Mond, J.; Smid, E.J. Industrial scale production and purification of a heterologous protein in Lactococcus lactis using the nisin-controlled gene expression system NICE: The case of lysostaphin. Microb. Cell Fact. 2005, 4, 15.
    • (2005) Microb. Cell Fact , vol.4 , pp. 15
    • Mierau, I.1    Leij, P.2    van Swam, I.3    Blommestein, B.4    Floris, E.5    Mond, J.6    Smid, E.J.7
  • 31
    • 26844435071 scopus 로고    scopus 로고
    • Optimization of the Lactococcus lactis nisin-controlled gene expression system NICE for industrial applications
    • Mierau, I.; Olieman, C.; Mond, J.; Smid, E.J. Optimization of the Lactococcus lactis nisin-controlled gene expression system NICE for industrial applications. Microb. Cell Fact. 2005, 4, 16.
    • (2005) Microb. Cell Fact , vol.4 , pp. 16
    • Mierau, I.1    Olieman, C.2    Mond, J.3    Smid, E.J.4
  • 32
    • 0031046570 scopus 로고    scopus 로고
    • Purification and molecular characterization of glycylglycine endopeptidase produced by Staphylococcus capitis
    • Sugai, M.; Fujiwara, T.; Akiyama, T.; Ohara, M.; Komatsuzawa, H.; Inoue, S.; Suginaka, H. Purification and molecular characterization of glycylglycine endopeptidase produced by Staphylococcus capitis. J. Bacteriol. 1997, 179, 1193-1202.
    • (1997) J. Bacteriol , vol.179 , pp. 1193-1202
    • Sugai, M.1    Fujiwara, T.2    Akiyama, T.3    Ohara, M.4    Komatsuzawa, H.5    Inoue, S.6    Suginaka, H.7
  • 33
    • 0030747364 scopus 로고    scopus 로고
    • epr, which encodes glycylglycine endopeptidase resistance, is homologous to femAB and affects serine content of peptidoglycan cross bridges in Staphylococcus capitis and Staphylococcus aureus
    • Sugai, M.; Fujiwara, T.; Ohta, K.; Komatsuzawa, H.; Ohara, M.; Suginaka, H. epr, which encodes glycylglycine endopeptidase resistance, is homologous to femAB and affects serine content of peptidoglycan cross bridges in Staphylococcus capitis and Staphylococcus aureus. J. Bacteriol. 1997, 179, 4311-4318.
    • (1997) J. Bacteriol , vol.179 , pp. 4311-4318
    • Sugai, M.1    Fujiwara, T.2    Ohta, K.3    Komatsuzawa, H.4    Ohara, M.5    Suginaka, H.6
  • 34
    • 0018930402 scopus 로고
    • Facile penetration of the Staphylococcus aureus capsule by lysostaphin
    • King, B.F.; Biel, M.L.; Wilkinson, B.J. Facile penetration of the Staphylococcus aureus capsule by lysostaphin. Infect. Immun. 1980, 29, 892-896.
    • (1980) Infect. Immun , vol.29 , pp. 892-896
    • King, B.F.1    Biel, M.L.2    Wilkinson, B.J.3
  • 35
    • 0001371631 scopus 로고
    • Purification and properties of lysostaphin-A lytic agent for Staphylococcus aureus
    • Schindler, C.A.; Schuhardt, V.T. Purification and properties of lysostaphin-A lytic agent for Staphylococcus aureus. Biochem. Biophys. Acta 1965, 97, 242-250.
    • (1965) Biochem. Biophys. Acta , vol.97 , pp. 242-250
    • Schindler, C.A.1    Schuhardt, V.T.2
  • 36
    • 0014320852 scopus 로고
    • Comparative inhibition of methicillin-resistant strains of Staphylococcus aureus by lysostaphin and other antibiotics
    • Zygmunt, W.A.; Harrison, E.F.; Browder, H.P.; Tavormina, P.A. Comparative inhibition of methicillin-resistant strains of Staphylococcus aureus by lysostaphin and other antibiotics. Appl. Microbiol. 1968, 16, 1174-1178.
    • (1968) Appl. Microbiol , vol.16 , pp. 1174-1178
    • Zygmunt, W.A.1    Harrison, E.F.2    Browder, H.P.3    Tavormina, P.A.4
  • 37
    • 0014323136 scopus 로고
    • Susceptibility of coagulase-negative staphylococci to lysostaphin ant other antibiotics
    • Zygmunt, W.A.; Browder, H.P.; Tavormina, P.A. Susceptibility of coagulase-negative staphylococci to lysostaphin ant other antibiotics. Appl. Microbiol. 1968, 16, 1168-1173.
    • (1968) Appl. Microbiol , vol.16 , pp. 1168-1173
    • Zygmunt, W.A.1    Browder, H.P.2    Tavormina, P.A.3
  • 38
    • 33645237316 scopus 로고    scopus 로고
    • Cross-linked peptidoglycan mediates lysostaphin binding to the cell wall envelope of Staphylococcus aureus
    • Grüdling, A.; Schneewind, O. Cross-linked peptidoglycan mediates lysostaphin binding to the cell wall envelope of Staphylococcus aureus. J. Bacteriol. 2006, 188, 2463-2472.
    • (2006) J. Bacteriol , vol.188 , pp. 2463-2472
    • Grüdling, A.1    Schneewind, O.2
  • 39
    • 0015462556 scopus 로고
    • Peptidoglycan types of bacterial cell walls and their taxonomic implications
    • Schleifer, K.H.; Kandler, O. Peptidoglycan types of bacterial cell walls and their taxonomic implications. Bacteriol. Rev. 1972, 36, 407-477.
    • (1972) Bacteriol. Rev , vol.36 , pp. 407-477
    • Schleifer, K.H.1    Kandler, O.2
  • 40
    • 0020265937 scopus 로고
    • Description of a new species of the genus Staphylococcus: Staphylococcus carnosus
    • Schleifer, K.H.; Fisher, U. Description of a new species of the genus Staphylococcus: Staphylococcus carnosus. Int. J. Syst. Bacteriol. 1982, 32, 153-156.
    • (1982) Int. J. Syst. Bacteriol , vol.32 , pp. 153-156
    • Schleifer, K.H.1    Fisher, U.2
  • 41
    • 0028954924 scopus 로고
    • Structure of the cell wall anchor of surface proteins in Staphylococcus aureus
    • Schneewindt, O.; Fowler, A.; Faull, K.F. Structure of the cell wall anchor of surface proteins in Staphylococcus aureus. Science 1995, 268, 103-106.
    • (1995) Science , vol.268 , pp. 103-106
    • Schneewindt, O.1    Fowler, A.2    Faull, K.F.3
  • 42
    • 57349182243 scopus 로고    scopus 로고
    • Direct observation of Staphylococcus aureus cell wall digestion by lysostaphin
    • Francius, G.; Domenech, O.; Mingeot-Leclercq, M.P.; Dufrêne, Y.F. Direct observation of Staphylococcus aureus cell wall digestion by lysostaphin. J. Bacteriol. 2008, 190, 7904-7909.
    • (2008) J. Bacteriol , vol.190 , pp. 7904-7909
    • Francius, G.1    Domenech, O.2    Mingeot-Leclercq, M.P.3    Dufrêne, Y.F.4
  • 43
    • 0032779487 scopus 로고    scopus 로고
    • Lysostaphin treatment of experimental aortic valve endocarditis caused by a Staphylococcus aureus isolate with reduced susceptibility to vancomycin
    • Patron, R.L.; Climo, M.W.; Goldstein, B.P.; Archer, G.L. Lysostaphin treatment of experimental aortic valve endocarditis caused by a Staphylococcus aureus isolate with reduced susceptibility to vancomycin. Antimicrob. Agents Chemother. 1999, 43, 1754-1755.
    • (1999) Antimicrob. Agents Chemother , vol.43 , pp. 1754-1755
    • Patron, R.L.1    Climo, M.W.2    Goldstein, B.P.3    Archer, G.L.4
  • 44
    • 0029833708 scopus 로고    scopus 로고
    • New biologically active hybrid bacteriocins constructed by combining regions from various pediocin-like bacteriocins: The C-terminal region is important for determining specificity
    • Fimland, G.; Blingsmo, R.; Sletten, K.; Jung, G.; Nes, I.F.; Nissen-Meyer, J. New biologically active hybrid bacteriocins constructed by combining regions from various pediocin-like bacteriocins: the C-terminal region is important for determining specificity. Appl. Environ. Microbiol. 1996, 62, 3313-3318.
    • (1996) Appl. Environ. Microbiol , vol.62 , pp. 3313-3318
    • Fimland, G.1    Blingsmo, R.2    Sletten, K.3    Jung, G.4    Nes, I.F.5    Nissen-Meyer, J.6
  • 45
    • 23044447134 scopus 로고    scopus 로고
    • Comparison of four methods for determining lysostaphin susceptibility of various strains of Staphylococcus aureus
    • Kusuma, C.M.; Kokai-Kun, J.F. Comparison of four methods for determining lysostaphin susceptibility of various strains of Staphylococcus aureus. Antimicrob. Agents Chemother. 2005, 49, 3256-3263.
    • (2005) Antimicrob. Agents Chemother , vol.49 , pp. 3256-3263
    • Kusuma, C.M.1    Kokai-Kun, J.F.2
  • 46
    • 0028961002 scopus 로고
    • The lysostaphin endopeptidase resistance gene (epr) specifies modification of peptidoglycan cross bridges in Staphylococcus simulans and Staphylococcus aureus
    • DeHart, H.; Heath, H.; Heath, L.; LeBlanc, P.; Sloan, G. The lysostaphin endopeptidase resistance gene (epr) specifies modification of peptidoglycan cross bridges in Staphylococcus simulans and Staphylococcus aureus. Appl. Environ. Microbiol. 1995, 61, 1475-1479.
    • (1995) Appl. Environ. Microbiol , vol.61 , pp. 1475-1479
    • Dehart, H.1    Heath, H.2    Heath, L.3    Leblanc, P.4    Sloan, G.5
  • 47
    • 0034000620 scopus 로고    scopus 로고
    • Site-specific serine incorporation by Lif and Epr into positions 3 and 5 of the staphylococcal peptidoglycan interpeptide bridge
    • Ehlert, K.; Tschierske, M.; Mori, C.; Schöder, W., Berger-Bächi, B. Site-specific serine incorporation by Lif and Epr into positions 3 and 5 of the staphylococcal peptidoglycan interpeptide bridge. J. Bacteriol. 2000, 182, 2635-2638.
    • (2000) J. Bacteriol , vol.182 , pp. 2635-2638
    • Ehlert, K.1    Tschierske, M.2    Mori, C.3    Schöder, W.4    Berger-Bächi, B.5
  • 48
    • 0018367443 scopus 로고
    • Relationship between lysostaphin endopeptidase production and cell wall composition of Staphylococcus aureus
    • Robinson, J.M.; Hardman, J.K.; Sloan, G.L. Relationship between lysostaphin endopeptidase production and cell wall composition of Staphylococcus aureus. J. Bacteriol. 1979, 137, 1158-1164.
    • (1979) J. Bacteriol , vol.137 , pp. 1158-1164
    • Robinson, J.M.1    Hardman, J.K.2    Sloan, G.L.3
  • 49
    • 0014262071 scopus 로고
    • Use of lysostaphin in the isolation of highly polymerized deoxyribonucleic acid and in the taxonomy of aerobic Micrococcaceae
    • Klesius, P.H.; Schuhardt, V.Y. Use of lysostaphin in the isolation of highly polymerized deoxyribonucleic acid and in the taxonomy of aerobic Micrococcaceae. J. Bacteriol. 1968, 95, 739-743.
    • (1968) J. Bacteriol , vol.95 , pp. 739-743
    • Klesius, P.H.1    Schuhardt, V.Y.2
  • 50
    • 0022653926 scopus 로고
    • Rapide lysostaphin test to differentiate Staphylococcus and Micrococcus species
    • Geary, C.; Stevens, M. Rapide lysostaphin test to differentiate Staphylococcus and Micrococcus species. J. Clin. Microbiol. 1986, 23, 1044-1045.
    • (1986) J. Clin. Microbiol , vol.23 , pp. 1044-1045
    • Geary, C.1    Stevens, M.2
  • 51
    • 0014052472 scopus 로고
    • Lysostaphin: An enzymatic approach to staphylococcal disease. I. In vitro studies
    • Schaffner, W.; Melly, M.A.; Hash, J.H; Koenig, M.G. Lysostaphin: an enzymatic approach to staphylococcal disease. I. In vitro studies. Yale J. Biol. Med. 1967, 39, 215-229.
    • (1967) Yale J. Biol. Med , vol.39 , pp. 215-229
    • Schaffner, W.1    Melly, M.A.2    Hash, J.H.3    Koenig, M.G.4
  • 52
    • 0037311091 scopus 로고    scopus 로고
    • Improved pharmacokinetics and reduced antibody reactivity of lysostaphin conjugated to polyethylene glycol
    • Walsh, S.; Shah, A; Mood, J. Improved pharmacokinetics and reduced antibody reactivity of lysostaphin conjugated to polyethylene glycol. Antimicrob. Agents Chemother. 2002, 47, 554-558.
    • (2002) Antimicrob. Agents Chemother , vol.47 , pp. 554-558
    • Walsh, S.1    Shah, A.2    Mood, J.3
  • 53
    • 0015440733 scopus 로고
    • Lysostaphin: Model for a specific enzymatic approach to infectious disease
    • Zygmunt, W.A.; Tavormina, P.A. Lysostaphin: model for a specific enzymatic approach to infectious disease. Prog. Drug Res. 1972, 16, 309-333.
    • (1972) Prog. Drug Res , vol.16 , pp. 309-333
    • Zygmunt, W.A.1    Tavormina, P.A.2
  • 55
    • 65949105016 scopus 로고
    • Comparative in vitro activities of lysostaphin and other antistaphylococcal antibiotics on clinical isolates of Staphylococcus aureus
    • Harrison, F.E.; Cropp, C.B. Comparative in vitro activities of lysostaphin and other antistaphylococcal antibiotics on clinical isolates of Staphylococcus aureus. Appl. Microbiol. 1965, 13, 212-215.
    • (1965) Appl. Microbiol , vol.13 , pp. 212-215
    • Harrison, F.E.1    Cropp, C.B.2
  • 56
    • 35148844847 scopus 로고
    • Microbiological activities of lysostaphin and penicillins against bacteriophage 80/81 strains of Staphylococcus aureus
    • Zygmunt, W.A.; Harrison, E.F.; Browder, H.P. Microbiological activities of lysostaphin and penicillins against bacteriophage 80/81 strains of Staphylococcus aureus. Appl. Microbiol. 1965, 13, 491-493.
    • (1965) Appl. Microbiol , vol.13 , pp. 491-493
    • Zygmunt, W.A.1    Harrison, E.F.2    Browder, H.P.3
  • 57
    • 0024556174 scopus 로고
    • Susceptibility of methicillin-resistant Staphylococcus aureus to lysostaphin
    • Huber, M.M.; Huber, T.W. Susceptibility of methicillin-resistant Staphylococcus aureus to lysostaphin. J. Clin. Microbiol. 1989, 27, 1122-1124.
    • (1989) J. Clin. Microbiol , vol.27 , pp. 1122-1124
    • Huber, M.M.1    Huber, T.W.2
  • 58
    • 0242385447 scopus 로고    scopus 로고
    • In vitro activity of recombinant lysostaphin against Staphylococcus aureus isolates from anterior nares and blood
    • von Eiff, C.; Kokai-Kun, J.F.; Becker, K.; Peters, G. In vitro activity of recombinant lysostaphin against Staphylococcus aureus isolates from anterior nares and blood. Antimicrob. Agents Chemother. 2003, 47, 3613-3615.
    • (2003) Antimicrob. Agents Chemother , vol.47 , pp. 3613-3615
    • von Eiff, C.1    Kokai-Kun, J.F.2    Becker, K.3    Peters, G.4
  • 59
    • 0027739318 scopus 로고
    • In vitro activity of recombinant lysostaphin-antibiotic combinations toward methicillin-resistant Staphylococcus aureus
    • Polak, J.; Della Latta, P.; Blackburn, P. In vitro activity of recombinant lysostaphin-antibiotic combinations toward methicillin-resistant Staphylococcus aureus. Diagn. Microbiol. Infect. Dis. 1993, 17, 265-270.
    • (1993) Diagn. Microbiol. Infect. Dis , vol.17 , pp. 265-270
    • Polak, J.1    della Latta, P.2    Blackburn, P.3
  • 60
    • 34250029920 scopus 로고    scopus 로고
    • Potent, synergistic inhibition of Staphylococcus aureus upon exposure to a combination of the endopeptidase lysostaphin and the cationic peptide ranalexin
    • Graham, S.; Coote, P.J. Potent, synergistic inhibition of Staphylococcus aureus upon exposure to a combination of the endopeptidase lysostaphin and the cationic peptide ranalexin. J. Antimicrob. Chemother. 2007, 59, 759-762.
    • (2007) J. Antimicrob. Chemother , vol.59 , pp. 759-762
    • Graham, S.1    Coote, P.J.2
  • 61
    • 0347906291 scopus 로고    scopus 로고
    • The preventable proportion of nosocomial infections: An overview of published reports
    • Harbarth, S.; Sax, H.; Gastmeier, P. The preventable proportion of nosocomial infections: an overview of published reports. J. Hosp. Infect. 2003, 54, 258-266.
    • (2003) J. Hosp. Infect , vol.54 , pp. 258-266
    • Harbarth, S.1    Sax, H.2    Gastmeier, P.3
  • 62
    • 0036217211 scopus 로고    scopus 로고
    • Staphylococcus epidermidis infections
    • Vuong, C.; Otto, M. Staphylococcus epidermidis infections. Microbes Infect. 2002, 4, 481-489.
    • (2002) Microbes Infect , vol.4 , pp. 481-489
    • Vuong, C.1    Otto, M.2
  • 63
    • 0036864706 scopus 로고    scopus 로고
    • Four-year evolution of frequency of occurrence and antimicrobial susceptibility patterns of bacteria from bloodstream infections in Latin American medical centers
    • Sader, H.S.; Jones, R.N.; Andrade-Baiocchi, S.; Biedenbach, D.J. Four-year evolution of frequency of occurrence and antimicrobial susceptibility patterns of bacteria from bloodstream infections in Latin American medical centers. Diagn. Microbiol. Infect. Dis. 2003, 44, 273-280.
    • (2003) Diagn. Microbiol. Infect. Dis , vol.44 , pp. 273-280
    • Sader, H.S.1    Jones, R.N.2    Andrade-Baiocchi, S.3    Biedenbach, D.J.4
  • 64
    • 0242354001 scopus 로고    scopus 로고
    • Lysostaphin disrupts Staphylococcus aureus and Staphylococcus epidermidis biofilms on artificial surfaces. Antimicrob
    • Wu, J.A.; Kusuma, C.; Mond, J.J.; Kokai-Kun, J.F. Lysostaphin disrupts Staphylococcus aureus and Staphylococcus epidermidis biofilms on artificial surfaces. Antimicrob. Agents Chemother. 2003, 47, 3407-3414.
    • (2003) Agents Chemother , vol.47 , pp. 3407-3414
    • Wu, J.A.1    Kusuma, C.2    Mond, J.J.3    Kokai-Kun, J.F.4
  • 65
    • 3042670681 scopus 로고    scopus 로고
    • Lysostaphin-coated catheters eradicate Staphylococcus aureus challenge and block surface colonization
    • Shah, A.; Mond, J.; Walsh, S. Lysostaphin-coated catheters eradicate Staphylococcus aureus challenge and block surface colonization. Antimicrob. Agents Chemother. 2004, 48, 2704-2707.
    • (2004) Antimicrob. Agents Chemother , vol.48 , pp. 2704-2707
    • Shah, A.1    Mond, J.2    Walsh, S.3
  • 66
    • 0000921589 scopus 로고
    • Lysostaphin therapy in mice infected with Staphylococcus aureus
    • Schudhardt, V.T; Schindler, C.A. Lysostaphin therapy in mice infected with Staphylococcus aureus. J. Bacteriol. 1964, 88, 815-816.
    • (1964) J. Bacteriol , vol.88 , pp. 815-816
    • Schudhardt, V.T.1    Schindler, C.A.2
  • 67
    • 0014323240 scopus 로고
    • Lysostaphin: An enzymatic approach to staphylococcal disease. III. Combined lysostaphin-methicillin therapy of established staphylococcal abscesses in mice
    • Dixon, R.E.; Goodman, J.S.; Koenig, M.G. Lysostaphin: an enzymatic approach to staphylococcal disease. III. Combined lysostaphin-methicillin therapy of established staphylococcal abscesses in mice. Yale J. Biol. Med. 1968, 41, 62-68.
    • (1968) Yale J. Biol. Med , vol.41 , pp. 62-68
    • Dixon, R.E.1    Goodman, J.S.2    Koenig, M.G.3
  • 68
    • 0014055217 scopus 로고
    • Lysostaphin in experimental renal infection
    • Harrison, E.F.; Zygmunt, W.A. Lysostaphin in experimental renal infection. J. Bacteriol. 1967, 93, 520-524.
    • (1967) J. Bacteriol , vol.93 , pp. 520-524
    • Harrison, E.F.1    Zygmunt, W.A.2
  • 69
    • 0031805819 scopus 로고    scopus 로고
    • Lysostaphin treatment of experimental methicillin-resistant Staphylococcus aureus aortic valve endocarditis
    • Climo, M.W.; Patron, R.L.; Goldstein, B.P.; Archer, G.L. Lysostaphin treatment of experimental methicillin-resistant Staphylococcus aureus aortic valve endocarditis. Antimicrob. Agents Chemother. 1998, 42, 1355-1360.
    • (1998) Antimicrob. Agents Chemother , vol.42 , pp. 1355-1360
    • Climo, M.W.1    Patron, R.L.2    Goldstein, B.P.3    Archer, G.L.4
  • 70
    • 0036093480 scopus 로고    scopus 로고
    • Combinations of lysostaphin with β-lactams are synergistic against oxacillin-resistant Staphylococcus epidermidis
    • Kiri, N.; Archer, G.; Climo, M.W. Combinations of lysostaphin with β-lactams are synergistic against oxacillin-resistant Staphylococcus epidermidis. Antimicrob. Agents Chemother. 2002, 46, 2017-2020.
    • (2002) Antimicrob. Agents Chemother , vol.46 , pp. 2017-2020
    • Kiri, N.1    Archer, G.2    Climo, M.W.3
  • 71
    • 0035040527 scopus 로고    scopus 로고
    • Mechanism and suppression of lysostaphin resistance in oxacillin-resistant Staphylococcus aureus
    • Climo, M.W.; Ehlert, K.; Archer, G.L. Mechanism and suppression of lysostaphin resistance in oxacillin-resistant Staphylococcus aureus. Antimicrob. Agents Chemother. 2001, 45, 1431-1437.
    • (2001) Antimicrob. Agents Chemother , vol.45 , pp. 1431-1437
    • Climo, M.W.1    Ehlert, K.2    Archer, G.L.3
  • 72
    • 65349104002 scopus 로고    scopus 로고
    • Treatment of methicillin-resistant Staphylococcus aureus in neonatal mice: Lysostaphin vs. vancomycin
    • Placencia, F.X.; Kong, L.; Weisman, L.E. Treatment of methicillin-resistant Staphylococcus aureus in neonatal mice: lysostaphin vs. vancomycin. Pediatr. Res. 2009, 65, 420-424.
    • (2009) Pediatr. Res , vol.65 , pp. 420-424
    • Placencia, F.X.1    Kong, L.2    Weisman, L.E.3
  • 73
    • 34250195356 scopus 로고    scopus 로고
    • Lysostaphin in treatment of neonatal Staphylococcus aureus infection
    • Oluola, O.; Kong, L.; Fein, M.; Weisman, L.E. Lysostaphin in treatment of neonatal Staphylococcus aureus infection. Antimicrob. Agents Chemother. 2007, 51, 2198-2220.
    • (2007) Antimicrob. Agents Chemother , vol.51 , pp. 2198-2220
    • Oluola, O.1    Kong, L.2    Fein, M.3    Weisman, L.E.4
  • 74
    • 35448975717 scopus 로고    scopus 로고
    • Lysostaphin as a treatment for systemic Staphylococcus aureus infection in a mouse model
    • Kokai-Kun, J.F.; Chanturiya, T.; Mond, J.J. Lysostaphin as a treatment for systemic Staphylococcus aureus infection in a mouse model. J. Antimicrob. Chemother. 2007, 60, 1051-1059.
    • (2007) J. Antimicrob. Chemother , vol.60 , pp. 1051-1059
    • Kokai-Kun, J.F.1    Chanturiya, T.2    Mond, J.J.3
  • 75
    • 67249101090 scopus 로고    scopus 로고
    • Lysostaphin eradicates established Staphylococcus aureus biofilms in jugular vein catheterized mice
    • Kokai-Kun, J.F.; Chanturiya, T.; Mond, J.J. Lysostaphin eradicates established Staphylococcus aureus biofilms in jugular vein catheterized mice. J. Antimicrob. Chemother. 2009, 64, 94-100.
    • (2009) J. Antimicrob. Chemother , vol.64 , pp. 94-100
    • Kokai-Kun, J.F.1    Chanturiya, T.2    Mond, J.J.3
  • 76
    • 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.; Mond, J.J. Lysostaphin cream eradicates Staphylococcus aureus nasal colonization in a cotton rat model. Antimicrob. Agents Chemother. 2003, 47, 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
  • 77
    • 0015114260 scopus 로고
    • Efficacy and safety of topical lysostaphin treatment of persistent nasal carriage of Staphylococcus aureus
    • Quickel Jr., K.E.; Selden, R.; Caldwell, J.R.; Nora, N.F.; Schaffner, W. Efficacy and safety of topical lysostaphin treatment of persistent nasal carriage of Staphylococcus aureus. Appl. Microbiol. 1971, 22, 446-450.
    • (1971) Appl. Microbiol , vol.22 , pp. 446-450
    • Quickel Jr., K.E.1    Selden, R.2    Caldwell, J.R.3    Nora, N.F.4    Schaffner, W.5
  • 78
    • 52149109984 scopus 로고    scopus 로고
    • Mammary tissue damage during bovine mastitis: Causes and control
    • Zhao, X.; Lacasse, P. Mammary tissue damage during bovine mastitis: causes and control. J. Anim. Sci. 2008, 86, 57-65.
    • (2008) J. Anim. Sci , vol.86 , pp. 57-65
    • Zhao, X.1    Lacasse, P.2
  • 79
    • 0036719741 scopus 로고    scopus 로고
    • Bovine mastitis: An evolving disease
    • Bradley, A.J. Bovine mastitis: an evolving disease. Vet. J. 2002, 164, 116-128.
    • (2002) Vet. J , vol.164 , pp. 116-128
    • Bradley, A.J.1
  • 80
    • 33747623729 scopus 로고    scopus 로고
    • The role of cow, pathogen, and treatment regimen in the therapeutic success of bovine Staphylococcus aureus mastitis
    • Barkema, H.W.; Schukken, Y.H.; Zadoks, R.N. The role of cow, pathogen, and treatment regimen in the therapeutic success of bovine Staphylococcus aureus mastitis. J. Dairy Sci. 2006, 89, 1877-1895.
    • (2006) J. Dairy Sci , vol.89 , pp. 1877-1895
    • Barkema, H.W.1    Schukken, Y.H.2    Zadoks, R.N.3
  • 81
    • 77952211953 scopus 로고
    • Lysostaphin efficacy for treatment of Staphylococcus aureus intramammary infection
    • Sears, P.M.; Smith, B.S.; Pollak, J.; Gusik, S.N.; Blackburn, P. Lysostaphin efficacy for treatment of Staphylococcus aureus intramammary infection. J. Dairy Sci. 1988, 71 (Suppl. 1), 244.
    • (1988) J. Dairy Sci , vol.71 , Issue.SUPPL. 1 , pp. 244
    • Sears, P.M.1    Smith, B.S.2    Pollak, J.3    Gusik, S.N.4    Blackburn, P.5
  • 82
    • 0026297279 scopus 로고
    • Lysostaphin: Use of a recombinant bactericidal enzyme as a mastitis therapeutic
    • Oldham, E.R.; Daley, M.J. Lysostaphin: use of a recombinant bactericidal enzyme as a mastitis therapeutic. J. Dairy Sci. 1991, 74, 4175-4182.
    • (1991) J. Dairy Sci , vol.74 , pp. 4175-4182
    • Oldham, E.R.1    Daley, M.J.2
  • 83
    • 0026546247 scopus 로고
    • Lysostaphin immunogenicity of locally administered recombinant protein used in mastitis therapy
    • Daley, M.J.; Oldham, E.R. Lysostaphin immunogenicity of locally administered recombinant protein used in mastitis therapy. Vet. Immunol. Immunopathol. 1992, 31, 301-312.
    • (1992) Vet. Immunol. Immunopathol , vol.31 , pp. 301-312
    • Daley, M.J.1    Oldham, E.R.2
  • 85
    • 0031019864 scopus 로고    scopus 로고
    • Cell wall monoglycine cross-bridges and methicillin hypersusceptibility in a femAB null mutant of methicillin-resistant Staphylococcus aureus
    • Strandén, A.M.; Ehlert, K.; Labischinski, H.; Berger-Bächi, B. Cell wall monoglycine cross-bridges and methicillin hypersusceptibility in a femAB null mutant of methicillin-resistant Staphylococcus aureus. J. Bacteriol. 1997, 179, 9-16.
    • (1997) J. Bacteriol , vol.179 , pp. 9-16
    • Strandén, A.M.1    Ehlert, K.2    Labischinski, H.3    Berger-Bächi, B.4
  • 86
    • 0037416970 scopus 로고    scopus 로고
    • FemABX peptidyl transferases: A link between branched-chain cell wall peptide formation and ß-lactam resistance in Gram-positive cocci
    • Rohrer, S.; Berger-Bächi, B. FemABX peptidyl transferases: a link between branched-chain cell wall peptide formation and ß-lactam resistance in Gram-positive cocci. Antimicrob. Agents Chemother. 2003, 47, 837-846.
    • (2003) Antimicrob. Agents Chemother , vol.47 , pp. 837-846
    • Rohrer, S.1    Berger-Bächi, B.2
  • 87
    • 24344466955 scopus 로고    scopus 로고
    • Beta-lactams against methicillin-resistant Staphylococcus aureus
    • Guignard, B.; Entenza; J.M.; Moreillon, P. Beta-lactams against methicillin-resistant Staphylococcus aureus. Curr. Opin. Pharmacol. 2005, 5, 479-489.
    • (2005) Curr. Opin. Pharmacol , vol.5 , pp. 479-489
    • Guignard, B.1    Entenza2    , J.M.3    Moreillon, P.4
  • 88
    • 0035955327 scopus 로고    scopus 로고
    • Overexpression of sigma factor, sigma (B), urges Staphylococcus aureus to thicken the cell wall and to resist beta-lactams
    • Morikawa, K.; Maruyama, A.; Inose, Y.; Higashide, M.; Hayashi, H.; Ohta, T. Overexpression of sigma factor, sigma (B), urges Staphylococcus aureus to thicken the cell wall and to resist beta-lactams. Biochem. Biophys. Res. Commun. 2001, 288, 385-389.
    • (2001) Biochem. Biophys. Res. Commun , vol.288 , pp. 385-389
    • Morikawa, K.1    Maruyama, A.2    Inose, Y.3    Higashide, M.4    Hayashi, H.5    Ohta, T.6
  • 89
    • 0033840740 scopus 로고    scopus 로고
    • Contribution of a thickened cell wall and its glutamine nonamidated component to the vancomycin resistance expressed by Staphylococcus aureus Mu50
    • Cui, L.; Murakami, H.; Kuwahara-Arai, K.; Hanaki, H.; Hiramatsu, K. Contribution of a thickened cell wall and its glutamine nonamidated component to the vancomycin resistance expressed by Staphylococcus aureus Mu50. Antimicrob. Agents Chemother. 2000, 44, 2276-2285.
    • (2000) Antimicrob. Agents Chemother , vol.44 , pp. 2276-2285
    • Cui, L.1    Murakami, H.2    Kuwahara-Arai, K.3    Hanaki, H.4    Hiramatsu, K.5
  • 90
    • 4644344349 scopus 로고    scopus 로고
    • Cell wall composition and decreased autolytic activity and lysostaphin susceptibility of glycopeptide-intermediate Staphylococcus aureus
    • Koehl, J.L.; Muthaiyan, A.; Jayaswal, R.K.; Ehlert, K.; Labischinski, H.; Wilkinson, B.J. Cell wall composition and decreased autolytic activity and lysostaphin susceptibility of glycopeptide-intermediate Staphylococcus aureus. Antimicrob. Agents Chemother. 2004, 48, 3749-3757.
    • (2004) Antimicrob. Agents Chemother , vol.48 , pp. 3749-3757
    • Koehl, J.L.1    Muthaiyan, A.2    Jayaswal, R.K.3    Ehlert, K.4    Labischinski, H.5    Wilkinson, B.J.6
  • 91
    • 33749005403 scopus 로고    scopus 로고
    • Staphylococcus aureus mutants with increased lysostaphin resistance
    • Gründling, A.; Missiakas, D.M.; Schneewind, O. Staphylococcus aureus mutants with increased lysostaphin resistance. J. Bacteriol. 2006, 188, 6286-6297.
    • (2006) J. Bacteriol , vol.188 , pp. 6286-6297
    • Gründling, A.1    Missiakas, D.M.2    Schneewind, O.3
  • 92
    • 33846623697 scopus 로고    scopus 로고
    • Lysostaphin-resistant variants of Staphylococcus aureus demonstrate reduced fitness in vitro and in vivo
    • Kusuma, C.M.; Jadanova, A.; Chanturiya, T.; Kokai-Kun, J.F. Lysostaphin-resistant variants of Staphylococcus aureus demonstrate reduced fitness in vitro and in vivo. Antimicrob. Agents Chemother. 2007, 51, 475-482.
    • (2007) Antimicrob. Agents Chemother , vol.51 , pp. 475-482
    • Kusuma, C.M.1    Jadanova, A.2    Chanturiya, T.3    Kokai-Kun, J.F.4


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