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Volumn 215, Issue , 2015, Pages 79-85

Characterisation of the antibacterial properties of a bacterial derived peptidoglycan hydrolase (LysCs4), active against C. sakazakii and other Gram-negative food-related pathogens

Author keywords

Bacterial derived peptidoglycan hydrolase; Cronobacter sakazakii; Gram negative peptidoglycan degradation

Indexed keywords

GLYCOSIDASE; HYDROLASE; LYSOZYME; PEPTIDOGLYCAN; PEPTIDOGLYCAN HYDROLASE; UNCLASSIFIED DRUG; ANTIINFECTIVE AGENT; BIOLOGICAL CONTROL AGENT; N ACETYLMURAMOYLALANINE AMIDASE;

EID: 84940651529     PISSN: 01681605     EISSN: 18793460     Source Type: Journal    
DOI: 10.1016/j.ijfoodmicro.2015.08.007     Document Type: Article
Times cited : (9)

References (54)
  • 6
    • 67650704883 scopus 로고    scopus 로고
    • A lytic enzyme cocktail from Streptomyces sp. B578 for the control of lactic and acetic acid bacteria in wine
    • Blättel V., Wirth K., Claus H., Schlott B., Pfeiffer P., König H. A lytic enzyme cocktail from Streptomyces sp. B578 for the control of lactic and acetic acid bacteria in wine. Appl. Microbiol. Biotechnol. 2009, 83:839-848.
    • (2009) Appl. Microbiol. Biotechnol. , vol.83 , pp. 839-848
    • Blättel, V.1    Wirth, K.2    Claus, H.3    Schlott, B.4    Pfeiffer, P.5    König, H.6
  • 8
    • 0025182708 scopus 로고
    • Effects of lysostaphin on Staphylococcus aureus infections of the mouse mammary gland
    • Bramley A., Foster R. Effects of lysostaphin on Staphylococcus aureus infections of the mouse mammary gland. Res. Vet. Sci. 1990, 49:120-121.
    • (1990) Res. Vet. Sci. , vol.49 , pp. 120-121
    • Bramley, A.1    Foster, R.2
  • 11
    • 0032055947 scopus 로고    scopus 로고
    • Application of lysostaphin-producing lactobacilli to control staphylococcal food poisoning in meat products
    • Cavadini C., Hertel C., Hammes W.P. Application of lysostaphin-producing lactobacilli to control staphylococcal food poisoning in meat products. J. Food Prot. 1998, 61:419-424.
    • (1998) J. Food Prot. , vol.61 , pp. 419-424
    • Cavadini, C.1    Hertel, C.2    Hammes, W.P.3
  • 12
    • 85015560155 scopus 로고    scopus 로고
    • CDC http://www.cdc.gov/cronobacter/technical.html.
  • 13
    • 0028899291 scopus 로고
    • Lytic infection of Escherichia coli biofilms by bacteriophage T4
    • Doolittle M., Cooney J., Caldwell D. Lytic infection of Escherichia coli biofilms by bacteriophage T4. Can. J. Microbiol. 1995, 41:12-18.
    • (1995) Can. J. Microbiol. , vol.41 , pp. 12-18
    • Doolittle, M.1    Cooney, J.2    Caldwell, D.3
  • 14
    • 64749083080 scopus 로고    scopus 로고
    • Application of a group II Campylobacter bacteriophage to reduce strains of Campylobacter jejuni and Campylobacter coli colonizing broiler chickens
    • El-Shibiny A., Scott A., Timms A., Metawea Y., Connerton P., Connerton I. Application of a group II Campylobacter bacteriophage to reduce strains of Campylobacter jejuni and Campylobacter coli colonizing broiler chickens. J. Food Prot. 2009, 72:733-740.
    • (2009) J. Food Prot. , vol.72 , pp. 733-740
    • El-Shibiny, A.1    Scott, A.2    Timms, A.3    Metawea, Y.4    Connerton, P.5    Connerton, I.6
  • 15
    • 0019311549 scopus 로고
    • Enterobacter sakazakii: a new species of "Enterobacteriaceae" isolated from clinical specimens
    • Farmer J.J., Asbury M., Hickman F., Brenner D.J. Enterobacter sakazakii: a new species of "Enterobacteriaceae" isolated from clinical specimens. Int. J. Syst. Bacteriol. 1980, 30:569-584.
    • (1980) Int. J. Syst. Bacteriol. , vol.30 , pp. 569-584
    • Farmer, J.J.1    Asbury, M.2    Hickman, F.3    Brenner, D.J.4
  • 16
    • 28244478427 scopus 로고    scopus 로고
    • Enterobacter sakazakii and other bacteria in powdered infant milk formula
    • Forsythe S.J. Enterobacter sakazakii and other bacteria in powdered infant milk formula. Matern. Child Nutr. 2005, 1:44-50.
    • (2005) Matern. Child Nutr. , vol.1 , pp. 44-50
    • Forsythe, S.J.1
  • 17
    • 70449524449 scopus 로고    scopus 로고
    • Epidemiology of invasive neonatal Cronobacter (Enterobacter sakazakii) infections
    • Friedemann M. Epidemiology of invasive neonatal Cronobacter (Enterobacter sakazakii) infections. Eur. J. Clin. Microbiol. Infect. Dis. 2009, 28:1297-1304.
    • (2009) Eur. J. Clin. Microbiol. Infect. Dis. , vol.28 , pp. 1297-1304
    • Friedemann, M.1
  • 19
    • 0036570034 scopus 로고    scopus 로고
    • Enterobacter sakazakii infections associated with the use of powdered infant formula-Tennessee, 2001
    • Himelright I. Enterobacter sakazakii infections associated with the use of powdered infant formula-Tennessee, 2001. J. Am. Med. Assoc. 2002, 287:2204-2205.
    • (2002) J. Am. Med. Assoc. , vol.287 , pp. 2204-2205
    • Himelright, I.1
  • 20
    • 0024556150 scopus 로고
    • Engineering hybrid genes without the use of restriction enzymes: gene splicing by overlap extension
    • Horton R.M., Hunt H.D., Ho S.N., Pullen J.K., Pease L.R. Engineering hybrid genes without the use of restriction enzymes: gene splicing by overlap extension. Gene 1989, 77:61-68.
    • (1989) Gene , vol.77 , pp. 61-68
    • Horton, R.M.1    Hunt, H.D.2    Ho, S.N.3    Pullen, J.K.4    Pease, L.R.5
  • 22
    • 4143061597 scopus 로고    scopus 로고
    • Isolation of Enterobacter sakazakii and other Enterobacteriaceae from powdered infant formula milk and related products
    • Iversen C., Forsythe S. Isolation of Enterobacter sakazakii and other Enterobacteriaceae from powdered infant formula milk and related products. Food Microbiol. 2004, 21:771-777.
    • (2004) Food Microbiol. , vol.21 , pp. 771-777
    • Iversen, C.1    Forsythe, S.2
  • 23
    • 84862336939 scopus 로고    scopus 로고
    • Genome sequence of the phage clP1, which infects the beer spoilage bacterium Pediococcus damnosus
    • Kelly D., O'Sullivan O., Mills S., McAuliffe O., Ross R.P., Neve H., Coffey A. Genome sequence of the phage clP1, which infects the beer spoilage bacterium Pediococcus damnosus. Gene 2012, 504:53-63.
    • (2012) Gene , vol.504 , pp. 53-63
    • Kelly, D.1    O'Sullivan, O.2    Mills, S.3    McAuliffe, O.4    Ross, R.P.5    Neve, H.6    Coffey, A.7
  • 25
    • 79954652277 scopus 로고    scopus 로고
    • Antibacterial activity of Acinetobacter baumannii phage ϕAB2 endolysin (LysAB2) against both Gram-positive and Gram-negative bacteria
    • Lai M.-J., Lin N.-T., Hu A., Soo P.-C., Chen L.-K., Chen L.-H., Chang K.-C. Antibacterial activity of Acinetobacter baumannii phage ϕAB2 endolysin (LysAB2) against both Gram-positive and Gram-negative bacteria. Appl. Microbiol. Biotechnol. 2011, 90:529-539.
    • (2011) Appl. Microbiol. Biotechnol. , vol.90 , pp. 529-539
    • Lai, M.-J.1    Lin, N.-T.2    Hu, A.3    Soo, P.-C.4    Chen, L.-K.5    Chen, L.-H.6    Chang, K.-C.7
  • 26
    • 11144252652 scopus 로고    scopus 로고
    • Identification and characterization of a highly thermostable bacteriophage lysozyme
    • Lavigne R., Briers Y., Hertveldt K., Robben J., Volckaert G. Identification and characterization of a highly thermostable bacteriophage lysozyme. Cell. Mol. Life Sci. 2004, 61:2753-2759.
    • (2004) Cell. Mol. Life Sci. , vol.61 , pp. 2753-2759
    • Lavigne, R.1    Briers, Y.2    Hertveldt, K.3    Robben, J.4    Volckaert, G.5
  • 30
    • 0029930408 scopus 로고    scopus 로고
    • Construction of luciferase reporter bacteriophage A511: luxAB for rapid and sensitive detection of viable Listeria cells
    • Loessner M.J., Rees C., Stewart G., Scherer S. Construction of luciferase reporter bacteriophage A511: luxAB for rapid and sensitive detection of viable Listeria cells. Appl. Environ. Microbiol. 1996, 62:1133-1140.
    • (1996) Appl. Environ. Microbiol. , vol.62 , pp. 1133-1140
    • Loessner, M.J.1    Rees, C.2    Stewart, G.3    Scherer, S.4
  • 31
    • 0030993334 scopus 로고    scopus 로고
    • Incidence, survival, and growth of Enterobacter sakazakii in infant formula
    • Nazarowec-White M., Farber J.M. Incidence, survival, and growth of Enterobacter sakazakii in infant formula. J. Food Prot. 1997, 60:226-230.
    • (1997) J. Food Prot. , vol.60 , pp. 226-230
    • Nazarowec-White, M.1    Farber, J.M.2
  • 32
    • 55549119928 scopus 로고    scopus 로고
    • Lytic activity of the recombinant staphylococcal bacteriophage ΦH5 endolysin active against Staphylococcus aureus in milk
    • Obeso J.M., Martínez B., Rodríguez A., García P. Lytic activity of the recombinant staphylococcal bacteriophage ΦH5 endolysin active against Staphylococcus aureus in milk. Int. J. Food Microbiol. 2008, 128:212-218.
    • (2008) Int. J. Food Microbiol. , vol.128 , pp. 212-218
    • Obeso, J.M.1    Martínez, B.2    Rodríguez, A.3    García, P.4
  • 33
    • 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
  • 38
    • 33947374647 scopus 로고    scopus 로고
    • Peptidoglycan recognition proteins: pleiotropic sensors and effectors of antimicrobial defences
    • Royet J., Dziarski R. Peptidoglycan recognition proteins: pleiotropic sensors and effectors of antimicrobial defences. Nat. Rev. Microbiol. 2007, 5:264-277.
    • (2007) Nat. Rev. Microbiol. , vol.5 , pp. 264-277
    • Royet, J.1    Dziarski, R.2
  • 41
    • 0032568655 scopus 로고    scopus 로고
    • SMART, a simple modular architecture research tool: identification of signaling domains
    • Schultz J., Milpetz F., Bork P., Ponting C.P. SMART, a simple modular architecture research tool: identification of signaling domains. Proc. Natl. Acad. Sci. 1998, 95:5857-5864.
    • (1998) Proc. Natl. Acad. Sci. , vol.95 , pp. 5857-5864
    • Schultz, J.1    Milpetz, F.2    Bork, P.3    Ponting, C.P.4
  • 42
    • 77956866741 scopus 로고
    • Microbial peptidoglycan (murein) hydrolases
    • Shockman G., Höltje J.-V. Microbial peptidoglycan (murein) hydrolases. New Compr. Biochem. 1994, 27:131-166.
    • (1994) New Compr. Biochem. , vol.27 , pp. 131-166
    • Shockman, G.1    Höltje, J.-V.2
  • 43
    • 0033950951 scopus 로고    scopus 로고
    • Autolysins of Bacillus subtilis: multiple enzymes with multiple functions
    • Smith T.J., Blackman S.A., Foster S.J. Autolysins of Bacillus subtilis: multiple enzymes with multiple functions. Microbiology 2000, 146:249-262.
    • (2000) Microbiology , vol.146 , pp. 249-262
    • Smith, T.J.1    Blackman, S.A.2    Foster, S.J.3
  • 44
    • 34547124551 scopus 로고    scopus 로고
    • Protective effect of lysostaphin from Staphylococcus simulans against growth of Staphylococcus aureus in milk and some other food products
    • Szweda P., Kotłowski R., Łacka I., Synowiecki J. Protective effect of lysostaphin from Staphylococcus simulans against growth of Staphylococcus aureus in milk and some other food products. J. Food Saf. 2007, 27:265-274.
    • (2007) J. Food Saf. , vol.27 , pp. 265-274
    • Szweda, P.1    Kotłowski, R.2    Łacka, I.3    Synowiecki, J.4
  • 45
    • 0034798343 scopus 로고    scopus 로고
    • Veterinary use and antibiotic resistance
    • Teuber M. Veterinary use and antibiotic resistance. Curr. Opin. Microbiol. 2001, 4:493-499.
    • (2001) Curr. Opin. Microbiol. , vol.4 , pp. 493-499
    • Teuber, M.1
  • 46
    • 0002249336 scopus 로고
    • Building and breaking of bonds in the cell wall of bacteria-the role for autolysins
    • Elsevier Science Publishers, Amsterdam
    • Tomasz A. Building and breaking of bonds in the cell wall of bacteria-the role for autolysins. Microbial Cell Wall Synthesis and Autolysis 1984, 3-12. Elsevier Science Publishers, Amsterdam.
    • (1984) Microbial Cell Wall Synthesis and Autolysis , pp. 3-12
    • Tomasz, A.1
  • 47
    • 78149416567 scopus 로고    scopus 로고
    • Reduction of Escherichia coli O157:H7 viability on leafy green vegetables by treatment with a bacteriophage mixture and trans-cinnamaldehyde
    • Viazis S., Akhtar M., Feirtag J., Diez-Gonzalez F. Reduction of Escherichia coli O157:H7 viability on leafy green vegetables by treatment with a bacteriophage mixture and trans-cinnamaldehyde. Food Microbiol. 2011, 28:149-157.
    • (2011) Food Microbiol. , vol.28 , pp. 149-157
    • Viazis, S.1    Akhtar, M.2    Feirtag, J.3    Diez-Gonzalez, F.4
  • 48
    • 39149102149 scopus 로고    scopus 로고
    • Structural variation in the glycan strands of bacterial peptidoglycan
    • Vollmer W. Structural variation in the glycan strands of bacterial peptidoglycan. FEMS Microbiol. Rev. 2008, 32:287-306.
    • (2008) FEMS Microbiol. Rev. , vol.32 , pp. 287-306
    • Vollmer, W.1
  • 52
    • 76149141577 scopus 로고    scopus 로고
    • Phage therapy to reduce preprocessing Salmonella infections in market-weight swine
    • Wall S.K., Zhang J., Rostagno M.H., Ebner P.D. Phage therapy to reduce preprocessing Salmonella infections in market-weight swine. Appl. Environ. Microbiol. 2010, 76:48-53.
    • (2010) Appl. Environ. Microbiol. , vol.76 , pp. 48-53
    • Wall, S.K.1    Zhang, J.2    Rostagno, M.H.3    Ebner, P.D.4
  • 54
    • 0036840423 scopus 로고    scopus 로고
    • The murein hydrolase of the bacteriophage ϕ3626 dual lysis system is active against all tested Clostridium perfringens strains
    • Zimmer M., Vukov N., Scherer S., Loessner M.J. The murein hydrolase of the bacteriophage ϕ3626 dual lysis system is active against all tested Clostridium perfringens strains. Appl. Environ. Microbiol. 2002, 68:5311-5317.
    • (2002) Appl. Environ. Microbiol. , vol.68 , pp. 5311-5317
    • Zimmer, M.1    Vukov, N.2    Scherer, S.3    Loessner, M.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.