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Volumn 9, Issue 10, 2014, Pages

A thermostable salmonella phage endolysin, Lys68, with broad bactericidal properties against gram-negative pathogens in presence of weak acids

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ENZYME; BACTERICIDE; CITRIC ACID; EDETIC ACID; MALIC ACID; SALMONELLA PHAGE ENDOLYSIN; UNCLASSIFIED DRUG; ANTIINFECTIVE AGENT; ENDOLYSIN; MALIC ACID DERIVATIVE; PROTEINASE;

EID: 84907855839     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0108376     Document Type: Article
Times cited : (151)

References (37)
  • 2
    • 38349170156 scopus 로고    scopus 로고
    • Treatment of health-care-associated infections caused by Gram-negative bacteria: A consensus statement
    • Chopra I, Schofield C, Everett M, O'Neill A, Miller K, et al. (2008) Treatment of health-care-associated infections caused by Gram-negative bacteria: A consensus statement. Lancet Infect Dis 8: 133-139.
    • (2008) Lancet Infect Dis , vol.8 , pp. 133-139
    • Chopra, I.1    Schofield, C.2    Everett, M.3    O'Neill, A.4    Miller, K.5
  • 3
    • 84875774723 scopus 로고    scopus 로고
    • Molecular aspects and comparative genomics of bacteriophage endolysins
    • Oliveira H, Melo LD, Santos SB, Nobrega FL, Ferreira EC, et al. (2013) Molecular aspects and comparative genomics of bacteriophage endolysins. J Virol 87: 4558-4570.
    • (2013) J Virol , vol.87 , pp. 4558-4570
    • Oliveira, H.1    Melo, L.D.2    Santos, S.B.3    Nobrega, F.L.4    Ferreira, E.C.5
  • 4
    • 77955557492 scopus 로고    scopus 로고
    • Bacteriophage endolysins: A novel anti-infective to control Gram-positive pathogens
    • Fischetti VA (2010) Bacteriophage endolysins: A novel anti-infective to control Gram-positive pathogens. Int J Med Microbiol 300: 357-362.
    • (2010) Int J Med Microbiol , vol.300 , pp. 357-362
    • Fischetti, V.A.1
  • 5
    • 0347479229 scopus 로고    scopus 로고
    • Molecular basis of bacterial outer membrane permeability revisited
    • Nikaido H (2003) Molecular basis of bacterial outer membrane permeability revisited. Microbiol Mol Biol Rev 67: 593-656.
    • (2003) Microbiol Mol Biol Rev , vol.67 , pp. 593-656
    • Nikaido, H.1
  • 6
    • 77953890564 scopus 로고    scopus 로고
    • Use of lysozyme, nisin, and EDTA combined treatments for maintaining quality of packed ostrich patties
    • Mastromatteo M, Lucera A, Sinigaglia M, Corbo MR (2010) Use of lysozyme, nisin, and EDTA combined treatments for maintaining quality of packed ostrich patties. J Food Sci 75: M178-M186.
    • (2010) J Food Sci , vol.75 , pp. M178-M186
    • Mastromatteo, M.1    Lucera, A.2    Sinigaglia, M.3    Corbo, M.R.4
  • 7
    • 79551681153 scopus 로고    scopus 로고
    • Use of bacteriophage endolysin EL188 and outer membrane permeabilizers against Pseudomonas aeruginosa
    • Briers Y, Walmagh M, Lavigne R (2011) Use of bacteriophage endolysin EL188 and outer membrane permeabilizers against Pseudomonas aeruginosa. J Appl Microbiol 110: 778-785.
    • (2011) J Appl Microbiol , vol.110 , pp. 778-785
    • Briers, Y.1    Walmagh, M.2    Lavigne, R.3
  • 8
    • 84870749535 scopus 로고    scopus 로고
    • Characterization of modular bacteriophage endolysins from Myoviridae phages OBP, 201phi2-1 and PVP-SE1
    • Walmagh M, Briers Y, dos Santos SB, Azeredo J, Lavigne R (2012) Characterization of modular bacteriophage endolysins from Myoviridae phages OBP, 201phi2-1 and PVP-SE1. PLoS One 7: e36991.
    • (2012) PLoS One , vol.7 , pp. e36991
    • Walmagh, M.1    Briers, Y.2    Dos Santos, S.B.3    Azeredo, J.4    Lavigne, R.5
  • 9
    • 84859443661 scopus 로고    scopus 로고
    • Characterization of endolysin from a Salmonella Typhimurium-infecting bacteriophage SPN1S
    • Lim JA, Shin H, Kang DH, Ryu S (2012) Characterization of endolysin from a Salmonella Typhimurium-infecting bacteriophage SPN1S. Res Microbiol 163: 233-241.
    • (2012) Res Microbiol , vol.163 , pp. 233-241
    • Lim, J.A.1    Shin, H.2    Kang, D.H.3    Ryu, S.4
  • 10
    • 0002285254 scopus 로고
    • Organic acids
    • Davidson PMB, A.L. editor. 2 ed. New York: Marcel Dekker Ltd
    • Doores S (1993) Organic acids. In: Davidson PMB, A.L., editor. Antimicrobials in Food. 2 ed. New York: Marcel Dekker Ltd. pp.95-136.
    • (1993) Antimicrobials in Food , pp. 95-136
    • Doores, S.1
  • 11
    • 79954417616 scopus 로고    scopus 로고
    • Mechanisms of microbial inhibition
    • Theron MM LJ, editor.: CRC Press
    • Theron MM LJ (2011) Mechanisms of microbial inhibition. In: Theron MM LJ, editor. Organic Acids and Food Preservation: CRC Press. pp.117-150.
    • (2011) Organic Acids and Food Preservation , pp. 117-150
    • Theron, M.M.L.J.1
  • 13
  • 14
    • 33847633917 scopus 로고    scopus 로고
    • A standardized approach for accurate quantification of murein hydrolase activity in high-throughput assays
    • Briers Y, Lavigne R, Volckaert G, Hertveldt K (2007) A standardized approach for accurate quantification of murein hydrolase activity in high-throughput assays. J Biochem Biophys Methods 70: 531-533.
    • (2007) J Biochem Biophys Methods , vol.70 , pp. 531-533
    • Briers, Y.1    Lavigne, R.2    Volckaert, G.3    Hertveldt, K.4
  • 15
    • 62449307950 scopus 로고    scopus 로고
    • A genetic screen to identify bacteriophage lysins
    • Martha R.J. Clokie AMK, editor
    • Raymond Schuch VAF, Daniel C. Nelson (2009) A Genetic Screen to Identify Bacteriophage Lysins. In: Martha R.J. Clokie AMK, editor. Bacteriophages - Methods in Molecular Biology. pp.307-319.
    • (2009) Bacteriophages - Methods in Molecular Biology , pp. 307-319
    • Raymond, S.V.A.F.1    Nelson, D.C.2
  • 16
    • 0022474744 scopus 로고
    • Analysis of protein circular dichroism spectra for secondary structure using a simple matrix multiplication
    • Compton LA, Johnson WC Jr (1986) Analysis of protein circular dichroism spectra for secondary structure using a simple matrix multiplication. Anal Biochem 155: 155-167.
    • (1986) Anal Biochem , vol.155 , pp. 155-167
    • Compton, L.A.1    Johnson, W.C.2
  • 18
    • 0019873820 scopus 로고
    • Estimation of globular protein secondary structure from circular dichroism
    • Provencher SW, Glockner J (1981) Estimation of globular protein secondary structure from circular dichroism. Biochemistry 20: 33-37.
    • (1981) Biochemistry , vol.20 , pp. 33-37
    • Provencher, S.W.1    Glockner, J.2
  • 19
    • 3242877618 scopus 로고    scopus 로고
    • DICHROWEB, An online server for protein secondary structure analyses from circular dichroism spectroscopic data
    • Whitmore L, Wallace BA (2004) DICHROWEB, an online server for protein secondary structure analyses from circular dichroism spectroscopic data. Nucleic Acids Res 32: W668-W673.
    • (2004) Nucleic Acids Res , vol.32 , pp. W668-W673
    • Whitmore, L.1    Wallace, B.A.2
  • 20
    • 45849096536 scopus 로고    scopus 로고
    • Protein secondary structure analyses from circular dichroism spectroscopy: Methods and reference databases
    • Whitmore L, Wallace BA (2008) Protein secondary structure analyses from circular dichroism spectroscopy: methods and reference databases. Biopolymers 89: 392-400.
    • (2008) Biopolymers , vol.89 , pp. 392-400
    • Whitmore, L.1    Wallace, B.A.2
  • 22
    • 84891629745 scopus 로고    scopus 로고
    • Accessed 2014 May 12
    • Carbohydrate-Active enZYmes website. Available: Www.cazy.org/Glycoside-Hydrolases. Accessed 2014 May 12.
    • Carbohydrate-Active EnZYmes
  • 23
    • 0033529853 scopus 로고    scopus 로고
    • Structural basis of the conversion of T4 lysozyme into a transglycosidase by reengineering the active site
    • Kuroki R, Weaver LH, Matthews BW (1999) Structural basis of the conversion of T4 lysozyme into a transglycosidase by reengineering the active site. Proc Natl Acad Sci U S A 96: 8949-8954.
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 8949-8954
    • Kuroki, R.1    Weaver, L.H.2    Matthews, B.W.3
  • 24
    • 78649737514 scopus 로고    scopus 로고
    • Structural relationships in the lysozyme superfamily: Significant evidence for glycoside hydrolase signature motifs
    • Wohlkonig A, Huet J, Looze Y, Wintjens R (2010) Structural relationships in the lysozyme superfamily: Significant evidence for glycoside hydrolase signature motifs. PLoS One 5: e15388.
    • (2010) PLoS One , vol.5 , pp. e15388
    • Wohlkonig, A.1    Huet, J.2    Looze, Y.3    Wintjens, R.4
  • 25
    • 0015462556 scopus 로고
    • Peptidoglycan types of bacterial cell walls and their taxonomic implications
    • Schleifer KH, Kandler O (1972) Peptidoglycan types of bacterial cell walls and their taxonomic implications. Bacteriol Rev 36: 407-477.
    • (1972) Bacteriol Rev , vol.36 , pp. 407-477
    • Schleifer, K.H.1    Kandler, O.2
  • 26
    • 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, Lagaert S, Michiels CW, et al. (2007) Muralytic activity and modular structure of the endolysins of Pseudomonas aeruginosa bacteriophages phiKZ and EL. Mol Microbiol 65: 1334-1344.
    • (2007) Mol Microbiol , vol.65 , pp. 1334-1344
    • Briers, Y.1    Volckaert, G.2    Cornelissen, A.3    Lagaert, S.4    Michiels, C.W.5
  • 27
    • 0021868497 scopus 로고
    • Isolation and characterization of the bacteriophage T4 tail-associated lysozyme
    • Nakagawa H, Arisaka F, Ishii S (1985) Isolation and characterization of the bacteriophage T4 tail-associated lysozyme. J Virol 54: 460-466.
    • (1985) J Virol , vol.54 , pp. 460-466
    • Nakagawa, H.1    Arisaka, F.2    Ishii, S.3
  • 28
    • 84856294356 scopus 로고    scopus 로고
    • Listeria bacteriophage peptidoglycan hydrolases feature high thermoresistance and reveal increased activity after divalent metal cation substitution
    • Schmelcher M, Waldherr F, Loessner MJ (2012) Listeria bacteriophage peptidoglycan hydrolases feature high thermoresistance and reveal increased activity after divalent metal cation substitution. Appl Microbiol Biotechnol 93: 633-643.
    • (2012) Appl Microbiol Biotechnol , vol.93 , pp. 633-643
    • Schmelcher, M.1    Waldherr, F.2    Loessner, M.J.3
  • 29
    • 0025896984 scopus 로고
    • A family of clostridial and streptococcal ligand-binding proteins with conserved C-terminal repeat sequences
    • Wren BW (1991) A family of clostridial and streptococcal ligand-binding proteins with conserved C-terminal repeat sequences. Mol Microbiol 5: 797- 803.
    • (1991) Mol Microbiol , vol.5 , pp. 797-803
    • Wren, B.W.1
  • 30
    • 26944440137 scopus 로고    scopus 로고
    • Organic acid toxicity, tolerance, and production in Escherichia coli biorefining applications
    • Warnecke T, Gill RT (2005) Organic acid toxicity, tolerance, and production in Escherichia coli biorefining applications. Microb Cell Fact 4: 25.
    • (2005) Microb Cell Fact , vol.4 , pp. 25
    • Warnecke, T.1    Gill, R.T.2
  • 32
    • 84855928763 scopus 로고    scopus 로고
    • Lag phase is a distinct growth phase that prepares bacteria for exponential growth and involves transient metal accumulation
    • Rolfe MD, Rice CJ, Lucchini S, Pin C, Thompson A, et al. (2012) Lag phase is a distinct growth phase that prepares bacteria for exponential growth and involves transient metal accumulation. J Bacteriol 194: 686-701.
    • (2012) J Bacteriol , vol.194 , pp. 686-701
    • Rolfe, M.D.1    Rice, C.J.2    Lucchini, S.3    Pin, C.4    Thompson, A.5
  • 33
    • 79954417616 scopus 로고    scopus 로고
    • Mechanisms of microbial inhibition
    • Theron MM, Lues JFR, editors. CRC Press
    • Theron MM, Lues JFR (2011) Mechanisms of microbial inhibition. In: Theron MM, Lues JFR, editors. Organic Acids and Food Preservation: CRC Press. pp.117-150.
    • (2011) Organic Acids and Food Preservation , pp. 117-150
    • Theron, M.M.1    Lues, J.F.R.2
  • 35
    • 84886899769 scopus 로고    scopus 로고
    • Marked synergistic bactericidal effects and mode of action of medium-chain fatty acids in combination with organic acids against Escherichia coli O157:H7
    • Kim SA, Rhee MS (2013) Marked synergistic bactericidal effects and mode of action of medium-chain fatty acids in combination with organic acids against Escherichia coli O157:H7. Appl Environ Microbiol 79: 6552-6560.
    • (2013) Appl Environ Microbiol , vol.79 , pp. 6552-6560
    • Kim, S.A.1    Rhee, M.S.2
  • 36
    • 79551502607 scopus 로고    scopus 로고
    • Remeasuring HEWL pK(a) values by NMR spectroscopy: Methods, analysis, accuracy, and implications for theoretical pK(a) calculations
    • Webb H, Tynan-Connolly BM, Lee GM, Farrell D, O'Meara F, et al. (2010) Remeasuring HEWL pK(a) values by NMR spectroscopy: methods, analysis, accuracy, and implications for theoretical pK(a) calculations. Proteins 79: 685- 702.
    • (2010) Proteins , vol.79 , pp. 685-702
    • Webb, H.1    Tynan-Connolly, B.M.2    Lee, G.M.3    Farrell, D.4    O'Meara, F.5
  • 37
    • 0028794520 scopus 로고
    • The refined structures of goose lysozyme and its complex with a bound trisaccharide show that the goose-type lysozymes lack a catalytic aspartate residue
    • Weaver LH, Grutter MG, Matthews BW (1995) The refined structures of goose lysozyme and its complex with a bound trisaccharide show that the goose-type lysozymes lack a catalytic aspartate residue. J Mol Biol 245: 54-68.
    • (1995) J Mol Biol , vol.245 , pp. 54-68
    • Weaver, L.H.1    Grutter, M.G.2    Matthews, B.W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.