메뉴 건너뛰기




Volumn 10, Issue 3, 2015, Pages 377-390

Breaking barriers: Expansion of the use of endolysins as novel antibacterials against Gram-negative bacteria

Author keywords

Antibiotic resistance; Art 175; Artilysin ; Endolysin; Gram negative; Novel antibiotics; Outer membrane

Indexed keywords

ANTIINFECTIVE AGENT; ARTILYSIN; ENDOLYSIN; LYSOZYME; UNCLASSIFIED DRUG; PEPTIDOGLYCAN; PROTEINASE;

EID: 84926179791     PISSN: 17460913     EISSN: 17460921     Source Type: Journal    
DOI: 10.2217/FMB.15.8     Document Type: Review
Times cited : (154)

References (67)
  • 1
    • 0000378637 scopus 로고
    • On the antibacterial action of cultures of a penicillium, with special reference to their use in the isolation of B. influenza
    • Fleming A. On the antibacterial action of cultures of a penicillium, with special reference to their use in the isolation of B. influenza. Brit. J. Exp. Path. 10(3), 226-236 (1929).
    • (1929) Brit. J. Exp. Path. , vol.10 , Issue.3 , pp. 226-236
    • Fleming, A.1
  • 2
    • 84877279350 scopus 로고    scopus 로고
    • Platforms for antibiotic discovery
    • Lewis K. Platforms for antibiotic discovery. Nat. Rev. Drug Disc. 12(5), 371-387 (2013).
    • (2013) Nat. Rev. Drug Disc. , vol.12 , Issue.5 , pp. 371-387
    • Lewis, K.1
  • 3
    • 67650436176 scopus 로고    scopus 로고
    • Drug discovery and natural products: End of an era or an endless frontier
    • Li JW-H, Vederas JC. Drug discovery and natural products: end of an era or an endless frontier. Science 325(5937), 161-165 (2009).
    • (2009) Science , vol.325 , Issue.5937 , pp. 161-165
    • Li, J.W.-H.1    Vederas, J.C.2
  • 4
    • 84904688494 scopus 로고    scopus 로고
    • Challenges and future prospects of antibiotic therapy: From peptides to phages utilization
    • Mandal SM, Roy A, Ghosh AK, Hazra TP, Basak A, Franco OL. Challenges and future prospects of antibiotic therapy: from peptides to phages utilization. Front. Pharmacol. 5, 105 (2014).
    • (2014) Front. Pharmacol. , vol.5 , pp. 105
    • Mandal, S.M.1    Roy, A.2    Ghosh, A.K.3    Hazra, T.P.4    Basak, A.5    Franco, O.L.6
  • 5
    • 84867073569 scopus 로고    scopus 로고
    • Bacteriophage endolysins as novel antimicrobials
    • Schmelcher M, Donovan DM, Loessner MJ. Bacteriophage endolysins as novel antimicrobials. Future Microbiol. 7(10), 1147-1171 (2012).
    • (2012) Future Microbiol. , vol.7 , Issue.10 , pp. 1147-1171
    • Schmelcher, M.1    Donovan, D.M.2    Loessner, M.J.3
  • 6
    • 0000646464 scopus 로고
    • On a remarkable bacteriolytic element found in tissues and secretion
    • Fleming A. On a remarkable bacteriolytic element found in tissues and secretion. Proc. Roy. Soc. Ser. B 93, 306-317 (1922).
    • (1922) Proc. Roy. Soc. Ser. B , vol.93 , pp. 306-317
    • Fleming, A.1
  • 7
    • 0141450720 scopus 로고    scopus 로고
    • Antimicrobial properties of lysozyme in relation to foodborne vegetative bacteria
    • Masschalck B, Michiels CW. Antimicrobial properties of lysozyme in relation to foodborne vegetative bacteria. Crit. Rev. Microbiol. 29(3), 191-214 (2003).
    • (2003) Crit. Rev. Microbiol. , vol.29 , Issue.3 , pp. 191-214
    • Masschalck, B.1    Michiels, C.W.2
  • 9
    • 34547897398 scopus 로고    scopus 로고
    • Muralytic activity and modular structure of the endolysins of Pseudomonas aeruginosa bacteriophages phiKZ and EL
    • Briers Y, Volckaert G, Cornelissen A et al. Muralytic activity and modular structure of the endolysins of Pseudomonas aeruginosa bacteriophages phiKZ and EL. Mol. Microbiol. 65(5), 1334-1344 (2007).
    • (2007) Mol. Microbiol. , vol.65 , Issue.5 , pp. 1334-1344
    • Briers, Y.1    Volckaert, G.2    Cornelissen, A.3
  • 10
    • 49449108717 scopus 로고    scopus 로고
    • The structural peptidoglycan hydrolase gp181 of bacteriophage KZ
    • Briers Y, Miroshnikov K, Chertkov O et al. The structural peptidoglycan hydrolase gp181 of bacteriophage KZ. Biochem. Biophys. Res. Comm. 374(4), 747-751 (2008).
    • (2008) Biochem. Biophys. Res. Comm. , vol.374 , Issue.4 , pp. 747-751
    • Briers, Y.1    Miroshnikov, K.2    Chertkov, O.3
  • 11
    • 0035957329 scopus 로고    scopus 로고
    • Prevention and elimination of upper respiratory colonization of mice by group A streptococci by using a bacteriophage lytic enzyme
    • Nelson D, Loomis L, Fischetti VA. Prevention and elimination of upper respiratory colonization of mice by group A streptococci by using a bacteriophage lytic enzyme. Proc. Natl. Acad. Sci. USA 98(7), 4107-4112 (2001).
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , Issue.7 , pp. 4107-4112
    • Nelson, D.1    Loomis, L.2    Fischetti, V.A.3
  • 12
    • 0035824437 scopus 로고    scopus 로고
    • Rapid killing of Streptococcus pneumonia with a bacteriophage cell wall hydrolase
    • Loeffler JM, Nelson D, Fischetti VA. Rapid killing of Streptococcus pneumonia with a bacteriophage cell wall hydrolase. Science 294(5549), 2170-2172 (2001).
    • (2001) Science , vol.294 , Issue.5549 , pp. 2170-2172
    • Loeffler, J.M.1    Nelson, D.2    Fischetti, V.A.3
  • 13
    • 84861123085 scopus 로고    scopus 로고
    • Chimeric phage lysins act synergistically with lysostaphin to kill mastitis-causing Staphylococcus aureus in murine mammary glands
    • Schmelcher M, Powell AM, Becker SC, Camp MJ, Donovan DM. Chimeric phage lysins act synergistically with lysostaphin to kill mastitis-causing Staphylococcus aureus in murine mammary glands. Appl. Environ. Microbiol. 78(7), 2297-2305 (2012).
    • (2012) Appl. Environ. Microbiol. , vol.78 , Issue.7 , pp. 2297-2305
    • Schmelcher, M.1    Powell, A.M.2    Becker, S.C.3    Camp, M.J.4    Donovan, D.M.5
  • 14
    • 0037158695 scopus 로고    scopus 로고
    • A bacteriolytic agent that detects and kills Bacillus anthracis
    • Schuch R, Nelson D, Fischetti VA. A bacteriolytic agent that detects and kills Bacillus anthracis. Nature 418(6900), 884-849 (2002).
    • (2002) Nature , vol.418 , Issue.6900 , pp. 884-1849
    • Schuch, R.1    Nelson, D.2    Fischetti, V.A.3
  • 15
    • 35948990424 scopus 로고    scopus 로고
    • Taking aim on bacterial pathogens: From phage therapy to enzybiotics
    • Hermoso JA, García JL, García P. Taking aim on bacterial pathogens: from phage therapy to enzybiotics. Curr. Opin. Microbiol. 10(5), 461-472 (2007).
    • (2007) Curr. Opin. Microbiol. , vol.10 , Issue.5 , pp. 461-472
    • Hermoso, J.A.1    García, J.L.2    García, P.3
  • 16
    • 77955557492 scopus 로고    scopus 로고
    • Bacteriophage endolysins: A novel anti-infective to control Gram-positive pathogens
    • Fischetti VA. Bacteriophage endolysins: a novel anti-infective to control Gram-positive pathogens. Int. J. Med. Microbiol. 300(6), 357-362 (2010).
    • (2010) Int. J. Med. Microbiol. , vol.300 , Issue.6 , pp. 357-362
    • Fischetti, V.A.1
  • 19
    • 0015462556 scopus 로고
    • Peptidoglycan types of bacterial cell walls and their taxonomic implications
    • Schleifer KH, Kandler O. Peptidoglycan types of bacterial cell walls and their taxonomic implications. Bact. Rev. 36(4), 407-477 (1972).
    • (1972) Bact. Rev. , vol.36 , Issue.4 , pp. 407-477
    • Schleifer, K.H.1    Kandler, O.2
  • 20
    • 22544471225 scopus 로고    scopus 로고
    • Bacteriophage endolysins - current state of research and applications
    • Loessner MJ. Bacteriophage endolysins - current state of research and applications. Curr. Opin. Microbiol. 8(4), 480-487 (2005).
    • (2005) Curr. Opin. Microbiol. , vol.8 , Issue.4 , pp. 480-487
    • Loessner, M.J.1
  • 21
    • 84893014085 scopus 로고    scopus 로고
    • Novel highly thermostable endolysin from Thermus scotoductus MAT2119 bacteriophage Ph2119 with amino acid sequence similarity to eukaryotic peptidoglycan recognition proteins
    • Plotka M, Kaczorowska AK, Stefanska A et al. Novel highly thermostable endolysin from Thermus scotoductus MAT2119 bacteriophage Ph2119 with amino acid sequence similarity to eukaryotic peptidoglycan recognition proteins. Appl. Environ. Microbiol. 80(3), 886-895 (2014).
    • (2014) Appl. Environ. Microbiol. , vol.80 , Issue.3 , pp. 886-895
    • Plotka, M.1    Kaczorowska, A.K.2    Stefanska, A.3
  • 22
    • 84918802390 scopus 로고    scopus 로고
    • Characterization and detection of endolysin gene from three Acinetobacter baumannii bacteriophages isolated from sewage water
    • Kitti T, Thummeepak R, Thanwisai A et al. Characterization and detection of endolysin gene from three Acinetobacter baumannii bacteriophages isolated from sewage water. Indian J. Microbiol. 54(4), 383-388 (2014).
    • (2014) Indian J. Microbiol. , vol.54 , Issue.4 , pp. 383-388
    • Kitti, T.1    Thummeepak, R.2    Thanwisai, A.3
  • 23
    • 84907855839 scopus 로고    scopus 로고
    • A thermostable Salmonella phage endolysin, Lys68, with broad bactericidal properties against Gram-negative pathogens in presence of weak acids
    • Oliveira H, Thiagarajan V, Walmagh M et al. A thermostable Salmonella phage endolysin, Lys68, with broad bactericidal properties against Gram-negative pathogens in presence of weak acids. PLoS One 9(10), e108376 (2014).
    • (2014) PLoS One , vol.9 , Issue.10 , pp. e108376
    • Oliveira, H.1    Thiagarajan, V.2    Walmagh, M.3
  • 24
    • 84915822150 scopus 로고    scopus 로고
    • Peptidoglycan degrading activity of the broad-range Salmonella bacteriophage S-394 recombinant endolysin
    • Legotsky SA, Vlasova KY, Priyma AD et al. Peptidoglycan degrading activity of the broad-range Salmonella bacteriophage S-394 recombinant endolysin. Biochimie 107(Pt B), 293-299 (2014).
    • (2014) Biochimie , vol.107 , pp. 293-299
    • Legotsky, S.A.1    Vlasova, K.Y.2    Priyma, A.D.3
  • 25
    • 84901247145 scopus 로고    scopus 로고
    • The novel Shewanella putrefaciens-infecting bacteriophage Spp001: Genome sequence and lytic enzymes
    • Han F, Li M, Lin H, Wang J, Cao L, Khan MN. The novel Shewanella putrefaciens-infecting bacteriophage Spp001: genome sequence and lytic enzymes. J. Ind. Microbiol. Biotechnol. 41(6), 1017-1026 (2014).
    • (2014) J. Ind. Microbiol. Biotechnol. , vol.41 , Issue.6 , pp. 1017-1026
    • Han, F.1    Li, M.2    Lin, H.3    Wang, J.4    Cao, L.5    Khan, M.N.6
  • 26
    • 84902603132 scopus 로고    scopus 로고
    • Exogenous lytic activity of SPN9CC endolysin against gram-negative bacteria
    • Lim JA, Shin H, Heu S, Ryu S. Exogenous lytic activity of SPN9CC endolysin against gram-negative bacteria. J. Microbiol. Biotechnol. 24(6), 803-811 (2014).
    • (2014) J. Microbiol. Biotechnol. , vol.24 , Issue.6 , pp. 803-811
    • Lim, J.A.1    Shin, H.2    Heu, S.3    Ryu, S.4
  • 27
    • 84897957323 scopus 로고    scopus 로고
    • Structure of bacteriophage SPN1S endolysin reveals an unusual two-module fold for the peptidoglycan lytic and binding activity
    • Park Y, Lim JA, Kong M, Ryu S, Rhee S. Structure of bacteriophage SPN1S endolysin reveals an unusual two-module fold for the peptidoglycan lytic and binding activity. Mol. Microbiol. 92(2), 316-325 (2014).
    • (2014) Mol. Microbiol. , vol.92 , Issue.2 , pp. 316-325
    • Park, Y.1    Lim, J.A.2    Kong, M.3    Ryu, S.4    Rhee, S.5
  • 28
    • 84891085220 scopus 로고    scopus 로고
    • Genomic investigation of lysogen formation and host lysis systmes of the Salmonella temperate bacteriophage SPN9CC
    • Shin H, Lee JH, Yoon H, Kang DH, Ryu S. Genomic investigation of lysogen formation and host lysis systmes of the Salmonella temperate bacteriophage SPN9CC. Appl. Environ. Microbiol. 80(1), 374-384 (2014).
    • (2014) Appl. Environ. Microbiol. , vol.80 , Issue.1 , pp. 374-384
    • Shin, H.1    Lee, J.H.2    Yoon, H.3    Kang, D.H.4    Ryu, S.5
  • 29
    • 84875774723 scopus 로고    scopus 로고
    • Molecular aspects and comparative genomics of bacteriophage endolysins
    • Oliveira H, Melo LDR, Santos SB, Nóbrega FL et al. Molecular aspects and comparative genomics of bacteriophage endolysins. J. Virol. 87(8), 4558-4570 (2013).
    • (2013) J. Virol. , vol.87 , Issue.8 , pp. 4558-4570
    • Oliveira, H.1    Melo, L.D.R.2    Santos, S.B.3    Nóbrega, F.L.4
  • 30
    • 0025037846 scopus 로고
    • Modular organization of the lytic enzymes of Streptococcus pneumoniae and its bacteriophages
    • García P, García JL, García E, Sanchez- Puelles JM, Lopez R. Modular organization of the lytic enzymes of Streptococcus pneumoniae and its bacteriophages. Gene 86(1), 81-88 (1990).
    • (1990) Gene , vol.86 , Issue.1 , pp. 81-88
    • García, P.1    García, J.L.2    García, E.3    Sanchez-Puelles, J.M.4    Lopez, R.5
  • 31
    • 80052741109 scopus 로고    scopus 로고
    • The cell wall binding domain of Listeria bacteriophage endolysin PlyP35 recognizes terminal GlcNAc residues in cell wall teichoic acid
    • Eugster MR, Haug MC, Huwiler SG, Loessner MJ. The cell wall binding domain of Listeria bacteriophage endolysin PlyP35 recognizes terminal GlcNAc residues in cell wall teichoic acid. Mol. Microbiol. 81(6), 1419-1432 (2011).
    • (2011) Mol. Microbiol. , vol.81 , Issue.6 , pp. 1419-1432
    • Eugster, M.R.1    Haug, M.C.2    Huwiler, S.G.3    Loessner, M.J.4
  • 32
    • 65049090481 scopus 로고    scopus 로고
    • The high-affinity peptidoglycan binding domain of Pseudomonas phage endolysin KZ144
    • Briers Y, Schelcher M, Loessner MJ et al. The high-affinity peptidoglycan binding domain of Pseudomonas phage endolysin KZ144. Biochem. Biophys. Res. Commun. 383(2), 187-191 (2009).
    • (2009) Biochem. Biophys. Res. Commun. , vol.383 , Issue.2 , pp. 187-191
    • Briers, Y.1    Schelcher, M.2    Loessner, M.J.3
  • 33
    • 0036231904 scopus 로고    scopus 로고
    • C-terminal domains of Listeria monocytogenes bacteriophage murein hydrolases determine specific recognition and high-affinity binding to bacterial cell wall carbohydrates
    • Loessner MJ, Kramer K, Ebel F, Scherer S. C-terminal domains of Listeria monocytogenes bacteriophage murein hydrolases determine specific recognition and high-affinity binding to bacterial cell wall carbohydrates. Mol. Microbiol. 44(2), 335-349 (2002).
    • (2002) Mol. Microbiol. , vol.44 , Issue.2 , pp. 335-349
    • Loessner, M.J.1    Kramer, K.2    Ebel, F.3    Scherer, S.4
  • 34
    • 84870749535 scopus 로고    scopus 로고
    • Characterization of modular bacteriophage endolysins from Myoviridae phages OBP, 201φ2-1 and PVP-SE1
    • Walmagh M, Briers Y, dos Santos SB, Azeredo J, Lavigne R. Characterization of modular bacteriophage endolysins from Myoviridae phages OBP, 201φ2-1 and PVP-SE1. PLoS ONE 7(5), e36991 (2012).
    • (2012) PLoS ONE , vol.7 , Issue.5 , pp. e36991
    • Walmagh, M.1    Briers, Y.2    Dos Santos, S.B.3    Azeredo, J.4    Lavigne, R.5
  • 35
    • 84926196818 scopus 로고    scopus 로고
    • Engineering β - glycoside hydrolases
    • Lilia Alberghina (Ed.) Harwood Academic Publishers, London, UK
    • Warren RAJ. Engineering β - glycoside hydrolases. In: Protein engineering in industrial biotechnology. Lilia Alberghina (Ed.). Harwood Academic Publishers, London, UK, 162-181 (2005).
    • (2005) Protein Engineering in Industrial Biotechnology , pp. 162-181
    • Warren, R.A.J.1
  • 36
    • 0026802197 scopus 로고
    • Agents that increase the permeability of the outer membrane
    • Vaara M. Agents that increase the permeability of the outer membrane. Microbiol. Rev. 56(3), 395-411 (1992).
    • (1992) Microbiol. Rev. , vol.56 , Issue.3 , pp. 395-411
    • Vaara, M.1
  • 37
    • 0021989093 scopus 로고
    • Molecular basis of bacterial outer membrane permeability
    • Nikaido H, Vaara M. Molecular basis of bacterial outer membrane permeability. Microbiol. Rev. 49(1), 1-32 (1985).
    • (1985) Microbiol. Rev. , vol.49 , Issue.1 , pp. 1-32
    • Nikaido, H.1    Vaara, M.2
  • 38
    • 0034967750 scopus 로고    scopus 로고
    • Antibacterial activity of Bacillus amyloliquefaciens phage endolysin without holin conjugation
    • Morita M, Tanji Y, Mizoguchi K, Soejima A, Orito Y, Unno H. Antibacterial activity of Bacillus amyloliquefaciens phage endolysin without holin conjugation. J Biosci. Bioeng. 91(5), 469-473 (2001).
    • (2001) J Biosci. Bioeng. , vol.91 , Issue.5 , pp. 469-473
    • Morita, M.1    Tanji, Y.2    Mizoguchi, K.3    Soejima, A.4    Orito, Y.5    Unno, H.6
  • 39
    • 0035968116 scopus 로고    scopus 로고
    • Functional analysis of antibacterial activity of Bacillus amyloliquefaciens phage endolysin against Gram-negative bacteria
    • Morita M, Tanji Y, Orito Y, Mizoguchi K, Soejima A, Unno H. Functional analysis of antibacterial activity of Bacillus amyloliquefaciens phage endolysin against Gram-negative bacteria. FEBS Lett. 500(1-2), 56-59 (2001).
    • (2001) FEBS Lett. , vol.500 , Issue.1-2 , pp. 56-59
    • Morita, M.1    Tanji, Y.2    Orito, Y.3    Mizoguchi, K.4    Soejima, A.5    Unno, H.6
  • 40
    • 3843065569 scopus 로고    scopus 로고
    • Bacillus amyloliquefaciens phage endolysin can enhance permeability of Pseudomonas aeruginosa outer membrane and induce cell lysis
    • Orito Y, Morita M, Hori K, Unno H, Tanji Y. Bacillus amyloliquefaciens phage endolysin can enhance permeability of Pseudomonas aeruginosa outer membrane and induce cell lysis. Appl. Microbiol. Biotechnol. 65(1), 105-109 (2004).
    • (2004) Appl. Microbiol. Biotechnol. , vol.65 , Issue.1 , pp. 105-109
    • Orito, Y.1    Morita, M.2    Hori, K.3    Unno, H.4    Tanji, Y.5
  • 41
    • 79954652277 scopus 로고    scopus 로고
    • Antibacterial activity of Acinetobacter baumannii phage AB2 (LysAB2) against both Gram-positive and Gram-negative bacteria
    • Lai M-J, Lin N-T, Hu A et al. Antibacterial activity of Acinetobacter baumannii phage AB2 (LysAB2) against both Gram-positive and Gram-negative bacteria. Appl. Microbiol. Biotechnol. 90(2), 529-539 (2011).
    • (2011) Appl. Microbiol. Biotechnol. , vol.90 , Issue.2 , pp. 529-539
    • Lai, M.-J.1    Lin, N.-T.2    Hu, A.3
  • 42
    • 84880302580 scopus 로고    scopus 로고
    • Identification and characterization of the putative phage-related endolysins through full genome sequence analysis is Acinetobacter baumannii ATCC 17978
    • Lai M-J, Soo P-S, Lin N-T et al. Identification and characterization of the putative phage-related endolysins through full genome sequence analysis is Acinetobacter baumannii ATCC 17978. Int. J. Antimicrob. Agents 42(2), 141-148 (2013).
    • (2013) Int. J. Antimicrob. Agents , vol.42 , Issue.2 , pp. 141-148
    • Lai, M.-J.1    Soo, P.-S.2    Lin, N.-T.3
  • 44
    • 0003016036 scopus 로고
    • Transgenic potato plants resistant to the phytopathogenic bacterium Erwinia carotovora
    • Düring K, Porsch P, Fladung M, Lörz H. Transgenic potato plants resistant to the phytopathogenic bacterium Erwinia carotovora. Plant J. 3(4), 587-598 (1993).
    • (1993) Plant J. , vol.3 , Issue.4 , pp. 587-598
    • Düring, K.1    Porsch, P.2    Fladung, M.3    Lörz, H.4
  • 46
    • 84902603132 scopus 로고    scopus 로고
    • Exogenous lytic activity of SPN9CC endolysin against Gram-negative bacteria
    • Kim JA, Shin H, Heu S, Ryu S. Exogenous lytic activity of SPN9CC endolysin against Gram-negative bacteria. J. Microbiol. Biotechnol. 24(6), 803-811 (2014).
    • (2014) J. Microbiol. Biotechnol. , vol.24 , Issue.6 , pp. 803-811
    • Kim, J.A.1    Shin, H.2    Heu, S.3    Ryu, S.4
  • 47
    • 37449031844 scopus 로고    scopus 로고
    • The pinholin of lambdoid phage 21: Control of lysis by membrane depolarization
    • Park T, Struck DK, Dankenbring CA, Young R. The pinholin of lambdoid phage 21: control of lysis by membrane depolarization. J. Bacteriol. 189(24), 9135-9139 (2007).
    • (2007) J. Bacteriol. , vol.189 , Issue.24 , pp. 9135-9139
    • Park, T.1    Struck, D.K.2    Dankenbring, C.A.3    Young, R.4
  • 48
    • 77950211683 scopus 로고    scopus 로고
    • Mutational analysis of the S21 pinholin
    • Pang T, Park T, Young R. Mutational analysis of the S21 pinholin. Mol. Microbil. 76(1), 68-77 (2010).
    • (2010) Mol. Microbil. , vol.76 , Issue.1 , pp. 68-77
    • Pang, T.1    Park, T.2    Young, R.3
  • 49
    • 33644915278 scopus 로고    scopus 로고
    • Inactivation of Vibrio parahaemolyticus and Vibrio vulnificus in phosphate-buffered saline and in inoculated whole oysters by high-pressure processing
    • Koo J, Jahncke ML, Reno PW, Hu X, Mallikarjunan P. Inactivation of Vibrio parahaemolyticus and Vibrio vulnificus in phosphate-buffered saline and in inoculated whole oysters by high-pressure processing. J. Food Prot. 69(3), 596-601 (2006).
    • (2006) J. Food Prot. , vol.69 , Issue.3 , pp. 596-601
    • Koo, J.1    Jahncke, M.L.2    Reno, P.W.3    Hu, X.4    Mallikarjunan, P.5
  • 50
    • 0035916960 scopus 로고    scopus 로고
    • High pressure increases bactericidal activity and spectrum of lactoferrin, lactoferricin and nisin
    • Masschalck B, Van Houdt R, Michiels CW. High pressure increases bactericidal activity and spectrum of lactoferrin, lactoferricin and nisin. Int. J. Food Microbiol. 64(3), 325-332 (2001).
    • (2001) Int. J. Food Microbiol. , vol.64 , Issue.3 , pp. 325-332
    • Masschalck, B.1    Van Houdt, R.2    Michiels, C.W.3
  • 51
    • 38849130696 scopus 로고    scopus 로고
    • Analysis of outer membrane permeability of Pseudomonas aeruginosa and bactericidal activity of endolysins KZ144 and EL188 under high hydrostatic pressure
    • Briers Y, Cornelissen A, Aertsen A et al. Analysis of outer membrane permeability of Pseudomonas aeruginosa and bactericidal activity of endolysins KZ144 and EL188 under high hydrostatic pressure. FEMS Microbiol. Lett. 280(1), 113-119 (2008).
    • (2008) FEMS Microbiol. Lett. , vol.280 , Issue.1 , pp. 113-119
    • Briers, Y.1    Cornelissen, A.2    Aertsen, A.3
  • 52
    • 33645897033 scopus 로고    scopus 로고
    • Comparison of bactericidal activity of six lysozymes at atmospheric pressure and under high hydrostatic pressure
    • Nakimbugwe D, Masschalck B, Atanassova M, Zewdie-Bosüner A, Michiels CW. Comparison of bactericidal activity of six lysozymes at atmospheric pressure and under high hydrostatic pressure. Int. J. Food Microbiol. 108(3), 355-363 (2006).
    • (2006) Int. J. Food Microbiol. , vol.108 , Issue.3 , pp. 355-363
    • Nakimbugwe, D.1    Masschalck, B.2    Atanassova, M.3    Zewdie-Bosüner, A.4    Michiels, C.W.5
  • 53
    • 33749069072 scopus 로고    scopus 로고
    • Inactivation of gram-negative bacteria in milk and banana juice by hen egg white and lambda lysozyme under high hydrostatic pressure
    • Nakimbugwe D, Masschalck B, Anim G, Michiels CW. Inactivation of gram-negative bacteria in milk and banana juice by hen egg white and lambda lysozyme under high hydrostatic pressure. Int. J. Food Microbiol. 112(1), 19-25 (2006).
    • (2006) Int. J. Food Microbiol. , vol.112 , Issue.1 , pp. 19-25
    • Nakimbugwe, D.1    Masschalck, B.2    Anim, G.3    Michiels, C.W.4
  • 54
    • 79551681153 scopus 로고    scopus 로고
    • Use of bacteriophage endolysin EL188 and outer membrane permeabilizers against Pseudomonas aeruginosa
    • Briers Y, Walmagh M, Lavigne R. Use of bacteriophage endolysin EL188 and outer membrane permeabilizers against Pseudomonas aeruginosa. J. Appl. Microbiol. 110(3), 778-785 (2011).
    • (2011) J. Appl. Microbiol. , vol.110 , Issue.3 , pp. 778-785
    • Briers, Y.1    Walmagh, M.2    Lavigne, R.3
  • 55
  • 56
    • 0001256923 scopus 로고    scopus 로고
    • Partially unfolded lysozyme at neutral pH agglutinates and kills Gram-negative and Gram-positive bacteria through membrane damage mechanism
    • Ibrahim HR, Higashiguchi S, Koketsu M et al. Partially unfolded lysozyme at neutral pH agglutinates and kills Gram-negative and Gram-positive bacteria through membrane damage mechanism. J. Agric. Food Chem. 44(12), 3799-3806 (1996).
    • (1996) J. Agric. Food Chem. , vol.44 , Issue.12 , pp. 3799-3806
    • Ibrahim, H.R.1    Higashiguchi, S.2    Koketsu, M.3
  • 57
    • 84862514534 scopus 로고    scopus 로고
    • Structural engineering of a phage lysin that targets Gram-negative pathogens
    • Lukacik P, Barnard T, Keller PW et al. Structural engineering of a phage lysin that targets Gram-negative pathogens. Proc. Natl. Acad. Sci. USA 109(25), 9857-9862 (2012).
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , Issue.25 , pp. 9857-9862
    • Lukacik, P.1    Barnard, T.2    Keller, P.W.3
  • 58
    • 84870158000 scopus 로고    scopus 로고
    • Using a bacteriocin structure to engineer a phage lysin that targets Yersinia pestis
    • Lukacik P, Barnard TJ, Buchanan SK. Using a bacteriocin structure to engineer a phage lysin that targets Yersinia pestis. Biochem. Soc. Trans. 40(6), 1503-1506 (2012).
    • (2012) Biochem. Soc. Trans. , vol.40 , Issue.6 , pp. 1503-1506
    • Lukacik, P.1    Barnard, T.J.2    Buchanan, S.K.3
  • 59
    • 0018759646 scopus 로고
    • Mode of action of pesticin: N-acetylglucosaminidase activity
    • Ferber DM, Brubaker RR. Mode of action of pesticin: N-acetylglucosaminidase activity. J. Bacteriol. 139(2), 495-501 (1979).
    • (1979) J. Bacteriol. , vol.139 , Issue.2 , pp. 495-501
    • Ferber, D.M.1    Brubaker, R.R.2
  • 61
    • 0033963533 scopus 로고    scopus 로고
    • Extended virulence genotypes of Escherichia coli strains from patients with urosepsis in relation to phylogeny and host compromise
    • Johnson JR, Stell AL. Extended virulence genotypes of Escherichia coli strains from patients with urosepsis in relation to phylogeny and host compromise. J. Infect. Dis. 181(6), 261-272 (2000).
    • (2000) J. Infect. Dis. , vol.181 , Issue.6 , pp. 261-272
    • Johnson, J.R.1    Stell, A.L.2
  • 62
    • 84863613709 scopus 로고    scopus 로고
    • Structural and mechanistic studies of pesticin, a bacterial homolog of phage lysozymes
    • Patzer SI, Albrecht R, Braun V, Zeth K. Structural and mechanistic studies of pesticin, a bacterial homolog of phage lysozymes. J. Biol. Chem. 287(28), 23381-23396 (2012).
    • (2012) J. Biol. Chem. , vol.287 , Issue.28 , pp. 23381-23396
    • Patzer, S.I.1    Albrecht, R.2    Braun, V.3    Zeth, K.4
  • 63
    • 84908289926 scopus 로고    scopus 로고
    • Engineered endolysin-based 'Artilysins' to combat multidrug-resistant Gram-negative pathogens
    • Briers Y, Walmagh M, Van Puyenbroeck V et al. Engineered endolysin-based 'Artilysins' to combat multidrug-resistant Gram-negative pathogens. MBio 5(4), e01379-e01414 (2014).
    • (2014) MBio , vol.5 , Issue.4 , pp. e01379-e01414
    • Briers, Y.1    Walmagh, M.2    Van Puyenbroeck, V.3
  • 64
    • 84903206252 scopus 로고    scopus 로고
    • Art-175 is a highly efficient antibacterial against multidrug resistant strains and persisters of Pseudomonas aeruginosa
    • Briers Y, Walmagh M, Grymonprez B et al. Art-175 is a highly efficient antibacterial against multidrug resistant strains and persisters of Pseudomonas aeruginosa. Antimicrob. Agents Chemother. 58(7), 3774-3784 (2014).
    • (2014) Antimicrob. Agents Chemother. , vol.58 , Issue.7 , pp. 3774-3784
    • Briers, Y.1    Walmagh, M.2    Grymonprez, B.3
  • 65
    • 33748988741 scopus 로고    scopus 로고
    • Tryptophan-and arginine-rich antimicrobial peptides: Structures and mechanisms of action
    • Chan DI, Prenner EJ, Vogel H. Tryptophan-and arginine-rich antimicrobial peptides: structures and mechanisms of action. Biochim. Biophys. Acta 1758(9), 1184-1202 (2006).
    • (2006) Biochim. Biophys. Acta , vol.1758 , Issue.9 , pp. 1184-1202
    • Chan, D.I.1    Prenner, E.J.2    Vogel, H.3
  • 66
    • 0036756135 scopus 로고    scopus 로고
    • Final report on the safety assessment of EDTA, calcium disodium EDTA, diammonium EDTA, dipotassium EDTA, disodium EDTA, TEA-EDTA, tetrasodium EDTA, tripotassium EDTA, trisodium EDTA, HEDTA, and trisodium HEDTA
    • Lanigan RS, Yamarik TA. Final report on the safety assessment of EDTA, calcium disodium EDTA, diammonium EDTA, dipotassium EDTA, disodium EDTA, TEA-EDTA, tetrasodium EDTA, tripotassium EDTA, trisodium EDTA, HEDTA, and trisodium HEDTA. Int. J. Toxicol. 21(Suppl. 2), 95-142 (2002).
    • (2002) Int. J. Toxicol. , vol.21 , pp. 95-142
    • Lanigan, R.S.1    Yamarik, T.A.2
  • 67
    • 84896993913 scopus 로고    scopus 로고
    • Preclinical safety evaluation of intravenously administered SAL200 containing the recombinant phage endolysin SAL-1 as a pharmaceutical ingredient
    • Jun SY, Jung GM, Yoon SJ et al. Preclinical safety evaluation of intravenously administered SAL200 containing the recombinant phage endolysin SAL-1 as a pharmaceutical ingredient. Antimicrob. Agents Chemother. 58(4), 2084-2088 (2014).
    • (2014) Antimicrob. Agents Chemother. , vol.58 , Issue.4 , pp. 2084-2088
    • Jun, S.Y.1    Jung, G.M.2    Yoon, S.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.