메뉴 건너뛰기




Volumn 63, Issue 28, 2015, Pages 6402-6409

Alanine-Scanning Mutational Analysis of Durancin GL Reveals Residues Important for Its Antimicrobial Activity

Author keywords

alanine scanning mutation; antilisteria; durancin GL; Enterococcus

Indexed keywords

AMINO ACIDS; LISTERIA; SCANNING; SPECTRUM ANALYSIS;

EID: 84937691045     PISSN: 00218561     EISSN: 15205118     Source Type: Journal    
DOI: 10.1021/acs.jafc.5b02114     Document Type: Article
Times cited : (9)

References (28)
  • 2
    • 0027199706 scopus 로고
    • Genetics of bacteriocins produced by lactic acid bacteria
    • Klaenhammer, T. R. Genetics of bacteriocins produced by lactic acid bacteria FEMS Microbiol. Rev. 1993, 12, 39-85 10.1016/0168-6445(93)90057-G
    • (1993) FEMS Microbiol. Rev. , vol.12 , pp. 39-85
    • Klaenhammer, T.R.1
  • 3
    • 28044472548 scopus 로고    scopus 로고
    • Pediocin-like antimicrobial peptides (class IIa bacteriocins) and their immunity proteins: Biosynthesis, structure, and mode of action
    • Fimland, G.; Johnsen, L.; Dalhus, B.; Nissen-Meyer, J. Pediocin-like antimicrobial peptides (class IIa bacteriocins) and their immunity proteins: biosynthesis, structure, and mode of action J. Pept. Sci. 2005, 11, 688-696 10.1002/psc.699
    • (2005) J. Pept. Sci. , vol.11 , pp. 688-696
    • Fimland, G.1    Johnsen, L.2    Dalhus, B.3    Nissen-Meyer, J.4
  • 4
    • 0035807737 scopus 로고    scopus 로고
    • Bacteriocins: Safe, natural antimicrobials for food preservation
    • Cleveland, J.; Montville, T. J.; Nes, I. F.; Chikindas, M. L. Bacteriocins: safe, natural antimicrobials for food preservation Int. J. Food Microbiol. 2001, 71, 1-20 10.1016/S0168-1605(01)00560-8
    • (2001) Int. J. Food Microbiol. , vol.71 , pp. 1-20
    • Cleveland, J.1    Montville, T.J.2    Nes, I.F.3    Chikindas, M.L.4
  • 5
    • 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 10.1038/nrmicro1273
    • (2005) Nat. Rev. Microbiol. , vol.3 , pp. 777-788
    • Cotter, P.D.1    Hill, C.2    Ross, R.P.3
  • 6
    • 34250622074 scopus 로고    scopus 로고
    • Bacteriocin production as a mechanism for the antiinfective activity of Lactobacillus salivarius UCC118
    • Corr, S. C.; Li, Y.; Riedel, C. U.; O'Toole, P. W.; Hill, C.; Gahan, C. G. Bacteriocin production as a mechanism for the antiinfective activity of Lactobacillus salivarius UCC118 Proc. Natl. Acad. Sci. U. S. A. 2007, 104, 7617-7621 10.1073/pnas.0700440104
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 7617-7621
    • Corr, S.C.1    Li, Y.2    Riedel, C.U.3    O'Toole, P.W.4    Hill, C.5    Gahan, C.G.6
  • 7
    • 84855577092 scopus 로고    scopus 로고
    • Development of class IIa bacteriocins as therapeutic agents
    • Lohans, C. T.; Vederas, J. C. Development of class IIa bacteriocins as therapeutic agents Int. J. Microbiol. 2012, 2012, 1-13 10.1155/2012/386410
    • (2012) Int. J. Microbiol. , vol.2012 , pp. 1-13
    • Lohans, C.T.1    Vederas, J.C.2
  • 9
    • 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, O. 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, O.R.2    Sletten, K.3    Jung, G.4    Nes, I.F.5    Nissen-Meyer, J.6
  • 10
    • 0031745937 scopus 로고    scopus 로고
    • Isolation and characterization of pediocin AcH chimeric protein mutants with altered bactericidal activity
    • Miller, K. W.; Schamber, R.; Osmanagaoglu, O.; Ray, B. Isolation and characterization of pediocin AcH chimeric protein mutants with altered bactericidal activity Appl. Environ. Microbiol. 1998, 64, 1997-2005
    • (1998) Appl. Environ. Microbiol. , vol.64 , pp. 1997-2005
    • Miller, K.W.1    Schamber, R.2    Osmanagaoglu, O.3    Ray, B.4
  • 11
    • 0037199421 scopus 로고    scopus 로고
    • Mutational analysis of the role of tryptophan residues in an antimicrobial peptide
    • Fimland, G.; Eijsink, V. G.; Nissen-Meyer, J. Mutational analysis of the role of tryptophan residues in an antimicrobial peptide Biochemistry 2002, 41, 9508-9515 10.1021/bi025856q
    • (2002) Biochemistry , vol.41 , pp. 9508-9515
    • Fimland, G.1    Eijsink, V.G.2    Nissen-Meyer, J.3
  • 12
    • 0036063421 scopus 로고    scopus 로고
    • Mutational analysis of the role of charged residues in target-cell binding, potency and specificity of the pediocin-like bacteriocin sakacin P
    • Kazazic, M.; Nissen-Meyer, J.; Fimland, G. Mutational analysis of the role of charged residues in target-cell binding, potency and specificity of the pediocin-like bacteriocin sakacin P Microbiology 2002, 148, 2019-2027
    • (2002) Microbiology , vol.148 , pp. 2019-2027
    • Kazazic, M.1    Nissen-Meyer, J.2    Fimland, G.3
  • 13
    • 4143107127 scopus 로고    scopus 로고
    • Mutational analysis of mesentericin Y105, an anti-Listeria bacteriocin, for determination of impact on bactericidal activity, in vitro secondary structure, and membrane interaction
    • Morisset, D.; Berjeaud, J. M.; Marion, D.; Lacombe, C.; Frère, J. Mutational analysis of mesentericin Y105, an anti-Listeria bacteriocin, for determination of impact on bactericidal activity, in vitro secondary structure, and membrane interaction Appl. Environ. Microbiol. 2004, 70, 4672-4680 10.1128/AEM.70.8.4672-4680.2004
    • (2004) Appl. Environ. Microbiol. , vol.70 , pp. 4672-4680
    • Morisset, D.1    Berjeaud, J.M.2    Marion, D.3    Lacombe, C.4    Frère, J.5
  • 14
    • 0031030583 scopus 로고    scopus 로고
    • Effect of amino acid substitutions on the activity of carnobacteriocin B2 Overproduction of the antimicrobial peptide, its engineered variants, and its precursor in Escherichia coli
    • Quadri, L. E.; Yan, L. Z.; Stiles, M. E.; Vederas, J. C. Effect of amino acid substitutions on the activity of carnobacteriocin B2 Overproduction of the antimicrobial peptide, its engineered variants, and its precursor in Escherichia coli J. Biol. Chem. 1997, 272, 3384-3388 10.1074/jbc.272.6.3384
    • (1997) J. Biol. Chem. , vol.272 , pp. 3384-3388
    • Quadri, L.E.1    Yan, L.Z.2    Stiles, M.E.3    Vederas, J.C.4
  • 15
    • 33144455595 scopus 로고    scopus 로고
    • Determination of essential and variable residues in pediocin PA-1 by NNK scanning
    • Tominaga, T.; Hatakeyama, Y. Determination of essential and variable residues in pediocin PA-1 by NNK scanning Appl. Environ. Microbiol. 2006, 72, 1141-1147 10.1128/AEM.72.2.1141-1147.2006
    • (2006) Appl. Environ. Microbiol. , vol.72 , pp. 1141-1147
    • Tominaga, T.1    Hatakeyama, Y.2
  • 16
    • 84861896861 scopus 로고    scopus 로고
    • Molecular analysis of the bacteriocin-encoding plasmid pDGL1 from Enterococcus durans and genetic characterization of the Durancin GL locus
    • Du, L.; Somkuti, G. A.; Renye, J. A., Jr. Molecular analysis of the bacteriocin-encoding plasmid pDGL1 from Enterococcus durans and genetic characterization of the Durancin GL locus Microbiology 2012, 158, 1523-1532 10.1099/mic.0.055624-0
    • (2012) Microbiology , vol.158 , pp. 1523-1532
    • Du, L.1    Somkuti, G.A.2    Renye, J.A.3
  • 17
    • 84856515412 scopus 로고    scopus 로고
    • Properties of Durancin GL, a new antilisterial bacteriocin produced by Enterococcus durans 41D
    • Du, L.; Somkuti, G. A.; Renye, J. A., Jr.; Huo, G. Properties of Durancin GL, a new antilisterial bacteriocin produced by Enterococcus durans 41D J. Food Saf. 2012, 32, 74-83 10.1111/j.1745-4565.2011.00346.x
    • (2012) J. Food Saf. , vol.32 , pp. 74-83
    • Du, L.1    Somkuti, G.A.2    Renye, J.A.3    Huo, G.4
  • 20
    • 0029109787 scopus 로고
    • Evidence for two bacteriocins produced by Carnobacterium piscicola and Carnobacterium divergens isolated from fish and active against Listeria monocytogenes
    • Pilet, M. F.; Dousset, X.; Barré, R.; Novel, G.; Desmazeaud, M.; Piard, J. C. Evidence for two bacteriocins produced by Carnobacterium piscicola and Carnobacterium divergens isolated from fish and active against Listeria monocytogenes J. Food Protect. 1995, 58, 256-262
    • (1995) J. Food Protect. , vol.58 , pp. 256-262
    • Pilet, M.F.1    Dousset, X.2    Barré, R.3    Novel, G.4    Desmazeaud, M.5    Piard, J.C.6
  • 21
    • 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.; Oppegard, C.; Haugen, H.; Kristiansen, P. Structure-function relationships of the non-lanthionine-containing peptide (class II) bacteriocins produced by gram-positive bacteria Curr. Pharm. Biotechnol. 2009, 10, 19-37 10.2174/138920109787048661
    • (2009) Curr. Pharm. Biotechnol. , vol.10 , pp. 19-37
    • Nissen-Meyer, J.1    Rogne, P.2    Oppegard, C.3    Haugen, H.4    Kristiansen, P.5
  • 23
    • 0030999249 scopus 로고    scopus 로고
    • Functional characterization of pediocin PA-1 binding to liposomes in the absence of a protein receptor and its relationship to a predicted tertiary structure
    • Chen, Y.; Shapira, R.; Eisenstein, M.; Montville, T. J. Functional characterization of pediocin PA-1 binding to liposomes in the absence of a protein receptor and its relationship to a predicted tertiary structure Appl. Environ. Microbiol. 1997, 63, 524-531
    • (1997) Appl. Environ. Microbiol. , vol.63 , pp. 524-531
    • Chen, Y.1    Shapira, R.2    Eisenstein, M.3    Montville, T.J.4
  • 25
    • 79953227398 scopus 로고    scopus 로고
    • Mutational analysis of residues in the helical region of the class IIa bacteriocin pediocin PA-1
    • Haugen, H. S.; Fimland, G.; Nissen-Meyer, J. Mutational analysis of residues in the helical region of the class IIa bacteriocin pediocin PA-1 Appl. Environ. Microbiol. 2011, 77 (6) 1966-1972 10.1128/AEM.02488-10
    • (2011) Appl. Environ. Microbiol. , vol.77 , Issue.6 , pp. 1966-1972
    • Haugen, H.S.1    Fimland, G.2    Nissen-Meyer, J.3
  • 26
    • 0028882402 scopus 로고
    • Tryptophan dynamics and structural refinement in a lipid bilayer environment: Solid state NMR of the gramicidin channel
    • Hu, W.; Lazo, N.; Cross, T. Tryptophan dynamics and structural refinement in a lipid bilayer environment: solid state NMR of the gramicidin channel Biochemistry 1995, 34, 14138-14146 10.1021/bi00043a019
    • (1995) Biochemistry , vol.34 , pp. 14138-14146
    • Hu, W.1    Lazo, N.2    Cross, T.3
  • 27
    • 0028787147 scopus 로고
    • Tryptophan hydrogen bonding and electric dipole moments: Functional roles in the gramicidin channel and implications for membrane proteins
    • Hu, W.; Cross, T. Tryptophan hydrogen bonding and electric dipole moments: functional roles in the gramicidin channel and implications for membrane proteins Biochemistry 1995, 34, 14147-14155 10.1021/bi00043a020
    • (1995) Biochemistry , vol.34 , pp. 14147-14155
    • Hu, W.1    Cross, T.2
  • 28
    • 23044477877 scopus 로고    scopus 로고
    • Evidence on correlation between number of disulfide bridge and toxicity of class IIa bacteriocins
    • Richard, C.; Canon, R.; Naghmouchi, K.; Bertrand, D.; Prevost, H.; Drider, D. Evidence on correlation between number of disulfide bridge and toxicity of class IIa bacteriocins Food Microbiol. 2006, 23, 175-183 10.1016/j.fm.2005.02.001
    • (2006) Food Microbiol. , vol.23 , pp. 175-183
    • Richard, C.1    Canon, R.2    Naghmouchi, K.3    Bertrand, D.4    Prevost, H.5    Drider, D.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.