메뉴 건너뛰기




Volumn 77, Issue 6, 2011, Pages 1966-1972

Mutational analysis of residues in the helical region of the class IIa bacteriocin pediocin PA-1

Author keywords

[No Author keywords available]

Indexed keywords

AMIDE GROUPS; BACTERIOCINS; HYDROPHILIC CHARGED; HYDROPHOBIC RESIDUES; MUTATIONAL ANALYSIS; PEDIOCIN; POSITIVE CHARGES; SEQUENCE-DEPENDENT; TARGET CELLS; WILD TYPES;

EID: 79953227398     PISSN: 00992240     EISSN: 10985336     Source Type: Journal    
DOI: 10.1128/AEM.02488-10     Document Type: Article
Times cited : (17)

References (36)
  • 1
    • 0029198457 scopus 로고
    • Transformation of Lactobacillus by electroporation
    • Aukrust, T. W., M. B. Brurberg, and I. F. Nes. 1995. Transformation of Lactobacillus by electroporation. Methods Mol. Biol. 47:201-208.
    • (1995) Methods Mol. Biol. , vol.47 , pp. 201-208
    • Aukrust, T.W.1    Brurberg, M.B.2    Nes, I.F.3
  • 3
    • 0030012762 scopus 로고    scopus 로고
    • Biochemical and genetic characterization of enterocin A from Enterococcus faecium, a new antilisterial bacteriocin in the pediocin family of bacteriocins
    • Aymerich, T., et al. 1996. Biochemical and genetic characterization of enterocin A from Enterococcus faecium, a new antilisterial bacteriocin in the pediocin family of bacteriocins. Appl. Environ. Microbiol. 62:1676-1682.
    • (1996) Appl. Environ. Microbiol. , vol.62 , pp. 1676-1682
    • Aymerich, T.1
  • 5
    • 34250622074 scopus 로고    scopus 로고
    • Bacteriocin production as a mechanism for the antiinfective activity of Lactobacillus salivarius UCC118
    • Corr, S. C., et al. 2007. Bacteriocin production as a mechanism for the antiinfective activity of Lactobacillus salivarius UCC118. Proc. Natl. Acad. Sci. U. S. A. 104:7617-7621.
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 7617-7621
    • Corr, S.C.1
  • 6
    • 27244436751 scopus 로고    scopus 로고
    • Bacteriocins: developing innate immunity for food
    • Cotter, P. D., C. Hill, and R. P. Ross. 2005. Bacteriocins: developing innate immunity for food. Nat. Rev. Microbiol. 3:777-788.
    • (2005) Nat. Rev. Microbiol. , vol.3 , pp. 777-788
    • Cotter, P.D.1    Hill, C.2    Ross, R.P.3
  • 7
    • 33847796246 scopus 로고    scopus 로고
    • Common mechanisms of target cell recognition and immunity for class II bacteriocins
    • Diep, D. B., M. Skaugen, Z. Salehian, H. Holo, and I. F. Nes. 2007. Common mechanisms of target cell recognition and immunity for class II bacteriocins. Proc. Natl. Acad. Sci. U. S. A. 104:2384-2389.
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 2384-2389
    • Diep, D.B.1    Skaugen, M.2    Salehian, Z.3    Holo, H.4    Nes, I.F.5
  • 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., et al. 1996. 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. 62:3313-3318.
    • (1996) Appl. Environ. Microbiol. , vol.62 , pp. 3313-3318
    • Fimland, G.1
  • 10
    • 0037199421 scopus 로고    scopus 로고
    • Mutational analysis of the role of tryptophan residues in an antimicrobial peptide
    • Fimland, G., V. Eijsink, and J. Nissen-Meyer. 2002. Mutational analysis of the role of tryptophan residues in an antimicrobial peptide. Biochemistry 41:9508-9515.
    • (2002) Biochemistry , vol.41 , pp. 9508-9515
    • Fimland, G.1    Eijsink, V.2    Nissen-Meyer, J.3
  • 11
    • 0031793223 scopus 로고    scopus 로고
    • The bactericidal activity of pediocin PA-1 is specifically inhibited by a 15-mer fragment that spans the bacteriocin from the center toward the C terminus
    • Fimland, G., R. Jack, G. Jung, I. F. Nes, and J. Nissen-Meyer. 1998. The bactericidal activity of pediocin PA-1 is specifically inhibited by a 15-mer fragment that spans the bacteriocin from the center toward the C terminus. Appl. Environ. Microbiol. 64:5057-5060.
    • (1998) Appl. Environ. Microbiol. , vol.64 , pp. 5057-5060
    • Fimland, G.1    Jack, R.2    Jung, G.3    Nes, I.F.4    Nissen-Meyer, J.5
  • 12
    • 0034005323 scopus 로고    scopus 로고
    • A C-terminal disulfide bridge in pediocin-like bacteriocins renders bacteriocin activity less temperature dependent and is a major determinant of the antimicrobial spectrum
    • Fimland, G., et al. 2000. A C-terminal disulfide bridge in pediocin-like bacteriocins renders bacteriocin activity less temperature dependent and is a major determinant of the antimicrobial spectrum. J. Bacteriol. 182:2643- 2648.
    • (2000) J. Bacteriol. , vol.182 , pp. 2643-2648
    • Fimland, G.1
  • 13
    • 28044472548 scopus 로고    scopus 로고
    • Pediocinlike antimicrobial peptides (class IIa bacteriocins) and their immunity proteins: biosynthesis, structure, and mode of action
    • Fimland, G., L. Johnsen, B. Dalhus, and J. Nissen-Meyer. 2005. Pediocinlike antimicrobial peptides (class IIa bacteriocins) and their immunity proteins: biosynthesis, structure, and mode of action. J. Pept. Sci. 11:688-696.
    • (2005) J. Pept. Sci. , vol.11 , pp. 688-696
    • Fimland, G.1    Johnsen, L.2    Dalhus, B.3    Nissen-Meyer, J.4
  • 14
    • 0000870269 scopus 로고    scopus 로고
    • Three-dimensional structure of leucocin A in trifluoroethanol and dodecylphosphocholine micelles: spatial location of residues critical for biological activity in type IIa bacteriocins from lactic acid bacteria
    • Gallagher, N. L. F., et al. 1997. Three-dimensional structure of leucocin A in trifluoroethanol and dodecylphosphocholine micelles: spatial location of residues critical for biological activity in type IIa bacteriocins from lactic acid bacteria. Biochemistry 36:15062-15072.
    • (1997) Biochemistry , vol.36 , pp. 15062-15072
    • Gallagher, N.L.F.1
  • 15
    • 0025719296 scopus 로고
    • Characterization of leucocin A-UAL 187 and cloning of the bacteriocin gene from Leuconostoc gelidum
    • Hastings, J. W., et al. 1991. Characterization of leucocin A-UAL 187 and cloning of the bacteriocin gene from Leuconostoc gelidum. J. Bacteriol. 173:7491-7500.
    • (1991) J. Bacteriol. , vol.173 , pp. 7491-7500
    • Hastings, J.W.1
  • 16
    • 28944447119 scopus 로고    scopus 로고
    • Three-dimensional structure in lipid micelles of the pediocin-like antimicrobial peptide curvacin A
    • Haugen, H. S., G. Fimland, J. Nissen-Meyer, and P. E. Kristiansen. 2005. Three-dimensional structure in lipid micelles of the pediocin-like antimicrobial peptide curvacin A. Biochemistry 44:16149-16157.
    • (2005) Biochemistry , vol.44 , pp. 16149-16157
    • Haugen, H.S.1    Fimland, G.2    Nissen-Meyer, J.3    Kristiansen, P.E.4
  • 17
    • 55049088136 scopus 로고    scopus 로고
    • Mutational analysis of the class IIa bacteriocin curvacin A and its orientation in target cell membranes
    • Haugen, H. S., P. E. Kristiansen, G. Fimland, and J. Nissen-Meyer. 2008. Mutational analysis of the class IIa bacteriocin curvacin A and its orientation in target cell membranes. Appl. Environ. Microbiol. 74:6766-6773.
    • (2008) Appl. Environ. Microbiol. , vol.74 , pp. 6766-6773
    • Haugen, H.S.1    Kristiansen, P.E.2    Fimland, G.3    Nissen-Meyer, J.4
  • 18
    • 0026724915 scopus 로고
    • Purification and primary structure of pediocin PA-1 produced by Pediococcus acidilactici PAC-1.0
    • Henderson, J. T., A. L. Chopko, and P. D. van Wassenaar. 1992. Purification and primary structure of pediocin PA-1 produced by Pediococcus acidilactici PAC-1.0. Arch. Biochem. Biophys. 295:5-12.
    • (1992) Arch. Biochem. Biophys. , vol.295 , pp. 5-12
    • Henderson, J.T.1    Chopko, A.L.2    van Wassenaar, P.D.3
  • 19
    • 0027077825 scopus 로고
    • Purification and amino acid sequence of sakacin A, a bacteriocin from Lactobacillus sake Lb706
    • Holck, A., L. Axelsson, S. E. Birkeland, T. Aukrust, and H. Blom. 1992. Purification and amino acid sequence of sakacin A, a bacteriocin from Lactobacillus sake Lb706. J. Gen. Microbiol. 138:2715-2720.
    • (1992) J. Gen. Microbiol. , vol.138 , pp. 2715-2720
    • Holck, A.1    Axelsson, L.2    Birkeland, S.E.3    Aukrust, T.4    Blom, H.5
  • 20
    • 15744401646 scopus 로고    scopus 로고
    • The C-terminal domain of pediocin-like antimicrobial peptides (class IIa bacteriocins) is involved in specific recognition of the C-terminal part of cognate immunity proteins and in determining the antimicrobial spectrum
    • Johnsen, L., G. Fimland, and J. Nissen-Meyer. 2005. The C-terminal domain of pediocin-like antimicrobial peptides (class IIa bacteriocins) is involved in specific recognition of the C-terminal part of cognate immunity proteins and in determining the antimicrobial spectrum. J. Biol. Chem. 280:9243-9250.
    • (2005) J. Biol. Chem. , vol.280 , pp. 9243-9250
    • Johnsen, L.1    Fimland, G.2    Nissen-Meyer, J.3
  • 21
    • 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., J. Nissen-Meyer, and G. Fimland. 2002. Mutational analysis of the role of charged residues in target-cell binding, potency and specificity of the pediocin-like bacteriocin sakacin P. Microbiology 148:2019-2027.
    • (2002) Microbiology , vol.148 , pp. 2019-2027
    • Kazazic, M.1    Nissen-Meyer, J.2    Fimland, G.3
  • 22
    • 78049439560 scopus 로고    scopus 로고
    • An extracellular loop of the mannose phosphotransferase system component IIC is responsible for specific targeting by class IIa bacteriocins
    • Kjos, M., Z. Salehian, I. F. Nes, and D. B. Diep. 2010. An extracellular loop of the mannose phosphotransferase system component IIC is responsible for specific targeting by class IIa bacteriocins. J. Bacteriol. 192:5906-5913.
    • (2010) J. Bacteriol. , vol.192 , pp. 5906-5913
    • Kjos, M.1    Salehian, Z.2    Nes, I.F.3    Diep, D.B.4
  • 23
    • 0026681413 scopus 로고
    • Cloning, expression, and nucleotide sequence of genes involved in production of pediocin PA-1, a bacteriocin from Pediococcus acidilactici PAC1.0
    • Marugg, J. D., et al. 1992. Cloning, expression, and nucleotide sequence of genes involved in production of pediocin PA-1, a bacteriocin from Pediococcus acidilactici PAC1.0. Appl. Environ. Microbiol. 58:2360-2367.
    • (1992) Appl. Environ. Microbiol. , vol.58 , pp. 2360-2367
    • Marugg, J.D.1
  • 24
    • 0026759323 scopus 로고
    • Purification and amino acid sequence of a bacteriocin produced by Pediococcus acidilactici
    • Nieto Lozano, J. C., J. Nissen-Meyer, K. Sletten, C. Pelaz, and I. F. Nes. [1992] Purification and amino acid sequence of a bacteriocin produced by Pediococcus acidilactici. J. Gen. Microbiol. 138:1985-1990.
    • (1992) J. Gen. Microbiol. , vol.138 , pp. 1985-1990
    • Nieto Lozano, J.C.1    Nissen-Meyer, J.2    Sletten, K.3    Pelaz, C.4    Nes, I.F.5
  • 25
    • 0026786508 scopus 로고
    • A novel lactococcal bacteriocin whose activity depends on the complementary action of two peptides
    • Nissen-Meyer, J., H. Holo, L. S. Håvarstein, K. Sletten, and I. F. Nes. 1992. A novel lactococcal bacteriocin whose activity depends on the complementary action of two peptides. J. Bacteriol. 174:5686-5692.
    • (1992) J. Bacteriol. , vol.174 , pp. 5686-5692
    • Nissen-Meyer, J.1    Holo, H.2    Håvarstein, L.S.3    Sletten, K.4    Nes, I.F.5
  • 26
    • 77953862178 scopus 로고    scopus 로고
    • Structure and mode-of-action of the two-peptide (class-IIb) bacteriocins. Probiotics Antimicrob
    • Nissen-Meyer, J., C. Oppegård, P. Rogne, H. S. Haugen, and P. E. Kristiansen. [2010] Structure and mode-of-action of the two-peptide (class-IIb) bacteriocins. Probiotics Antimicrob. Proteins 2:52-60.
    • (2010) Proteins , vol.2 , pp. 52-60
    • Nissen-Meyer, J.1    Oppegård, C.2    Rogne, P.3    Haugen, H.S.4    Kristiansen, P.E.5
  • 27
    • 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., P. Rogne, C. Oppegård, H. S. Haugen, and P. E. Kristiansen. [2009] Structure-function relationships of the non-lanthionine-containing peptide (class II) bacteriocins produced by Gram-positive bacteria. Curr. Pharm. Biotechnol. 10:19-37.
    • (2009) Curr. Pharm. Biotechnol. , vol.10 , pp. 19-37
    • Nissen-Meyer, J.1    Rogne, P.2    Oppegård, C.3    Haugen, H.S.4    Kristiansen, P.E.5
  • 28
    • 34548500384 scopus 로고    scopus 로고
    • The two-peptide class II bacteriocins: structure, production, and mode of action
    • Oppegård, C., et al. 2007. The two-peptide class II bacteriocins: structure, production, and mode of action. J. Mol. Microbiol. Biotechnol. 13:210-219.
    • (2007) J. Mol. Microbiol. Biotechnol. , vol.13 , pp. 210-219
    • Oppegård, C.1
  • 30
    • 0028344604 scopus 로고
    • Cloning and sequencing of sakP encoding sakacin P, the bacteriocin produced by Lactobacillus sake LTH673
    • Tichaczek, P. S., R. F. Vogel, and W. P. Hammes. 1994. Cloning and sequencing of sakP encoding sakacin P, the bacteriocin produced by Lactobacillus sake LTH673. Microbiology 140:361-367.
    • (1994) Microbiology , vol.140 , pp. 361-367
    • Tichaczek, P.S.1    Vogel, R.F.2    Hammes, W.P.3
  • 31
    • 0027326620 scopus 로고
    • Cloning and sequencing of curA encoding curvacin A, the bacteriocin produced by Lactobacillus curvatus LTH1174
    • Tichaczek, P. S., R. F. Vogel, and W. P. Hammes. 1993. Cloning and sequencing of curA encoding curvacin A, the bacteriocin produced by Lactobacillus curvatus LTH1174. Arch. Microbiol. 160:279-283.
    • (1993) Arch. Microbiol. , vol.160 , pp. 279-283
    • Tichaczek, P.S.1    Vogel, R.F.2    Hammes, W.P.3
  • 32
    • 0036154401 scopus 로고    scopus 로고
    • Rapid two-step procedure for large-scale purification of pediocin-like bacteriocins and other cationic antimicrobial peptides from complex culture medium
    • Uteng, M., H. H. Hauge, I. Brondz, J. Nissen-Meyer, and G. Fimland. 2002. Rapid two-step procedure for large-scale purification of pediocin-like bacteriocins and other cationic antimicrobial peptides from complex culture medium. Appl. Environ. Microbiol. 68:952-956.
    • (2002) Appl. Environ. Microbiol. , vol.68 , pp. 952-956
    • Uteng, M.1    Hauge, H.H.2    Brondz, I.3    Nissen-Meyer, J.4    Fimland, G.5
  • 33
    • 0141817944 scopus 로고    scopus 로고
    • Three-dimensional structure in lipid micelles of the pediocin-like antimicrobial peptide sakacin P and a sakacin P variant that is structurally stabilized by an inserted C-terminal disulfide bridge
    • Uteng, M., et al. 2003. Three-dimensional structure in lipid micelles of the pediocin-like antimicrobial peptide sakacin P and a sakacin P variant that is structurally stabilized by an inserted C-terminal disulfide bridge. Biochemistry 42:11417-11426.
    • (2003) Biochemistry , vol.42 , pp. 11417-11426
    • Uteng, M.1
  • 35
    • 0033598699 scopus 로고    scopus 로고
    • Solution structure of carnobacteriocin B2 and implications for structure-activity relationships among type IIa bacteriocins from lactic acid bacteria
    • Wang, Y., et al. 1999. Solution structure of carnobacteriocin B2 and implications for structure-activity relationships among type IIa bacteriocins from lactic acid bacteria. Biochemistry 38:15438-15447.
    • (1999) Biochemistry , vol.38 , pp. 15438-15447
    • Wang, Y.1
  • 36
    • 0034736095 scopus 로고    scopus 로고
    • Analogues of bacteriocins: antimicrobial specificity and interactions of leucocin A with its enantiomer, carnobacteriocin B2, and truncated derivatives
    • Yan, L. Z., A. C. Gibbs, M. E. Stiles, D. S. Wishart, and J. C. Vederas. 2000. Analogues of bacteriocins: antimicrobial specificity and interactions of leucocin A with its enantiomer, carnobacteriocin B2, and truncated derivatives. J. Med. Chem. 43:4579-4581.
    • (2000) J. Med. Chem. , vol.43 , pp. 4579-4581
    • Yan, L.Z.1    Gibbs, A.C.2    Stiles, M.E.3    Wishart, D.S.4    Vederas, J.C.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.