Three-dimensional structure in lipid micelles of the pediocin-like antimicrobial peptide curvacin A

Biochemistry

Volumn 44, Issue 49, 2005, Pages 16149-16157

  Haugen, Helen Sophie ^a   Fimland, Gunnar ^a   Nissen Meyer, Jon ^a   Kristiansen, Per Eugen ^a  

^a UNIVERSITY OF OSLO   (Norway)

Author keywords

[No Author keywords available]

Indexed keywords

HYDROPHILICITY; HYDROPHOBICITY; LIPIDS; MICROBIOLOGY; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; THREE DIMENSIONAL;

ANTIMICROBIAL; LIPID MICELLES; PEPTIDES;

MICELLES;

CARNOBACTERIOCIN BM1; CURVACIN A; DISULFIDE; ENTEROCIN P; PEDIOCIN; POLYPEPTIDE ANTIBIOTIC AGENT; UNCLASSIFIED DRUG;

ALPHA HELIX; AMINO TERMINAL SEQUENCE; ARTICLE; BETA SHEET; CARBOXY TERMINAL SEQUENCE; DRUG STRUCTURE; HYDROGEN BOND; HYDROPHILICITY; HYDROPHOBICITY; LACTIC ACID BACTERIUM; MICELLE; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN DOMAIN; STRUCTURE ANALYSIS;

AMINO ACID SEQUENCE; ANTIMICROBIAL CATIONIC PEPTIDES; BACTERIOCINS; LACTOBACILLUS; LIPIDS; MICELLES; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; SEQUENCE ALIGNMENT;

BACTERIA (MICROORGANISMS);

EID: 28944447119     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi051215u     Document Type: Article

References (75)

1. Nissen-Meyer, J., and Nes, I. F. (1997) Ribosomally synthesized antimicrobial peptides: their function, structure, Arch. Microbiol. 167, 67-77.
2. Nes, I. F., Holo, H., Fimland, G., Hauge, H. H., and Nissen-Meyer, J. (2001) in Peptide antibiotics, discovery, modes of action and application (Dutton, H., McArthur, and Max, Eds.) Marcel Decker, New York.
3. Cleveland, J., Montville, T. J., Nes, I. F., and Chikindas, M. L. (2001) Bacteriocins: safe, natural antimicrobials for food preservation, Int. J. Food Microbiol. 71, 1-20.
4. Nissen-Meyer, J., Hauge, H. H., Fimland, G., Eijsink, V. G. H., and Nes, I. F. (1997) Ribosomally syntesized antimicrobial peptides produced by lactic acid bacteria: Their function, structure, biogenisis, and their mechanism of action. Recent Res. Dev. Microbiol. 1, 141-154.
5. Morisset, D., Berjeaud, J. M., Marion, D., Lacombe, C., and Frere, J. (2004) 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. 70, 4672-4680.
6. Aymerich, T., Holo, H., Havarstein, L. S., Hugas, M., Garriga, M., and Nes, I. F. (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.
7. Metivier, A., Pilet, M. F., Dousset, X., Sorokine, O., Anglade, P., Zagorec, M., Piard, J. C., Marion, D., Cenatiempo, Y., and Fremaux, C. (1998) Divercin V41, a new bacteriocin with two disulphide bonds produced by Carnobacterium divergens V41: primary structure and genomic organization, Microbiology 144, 2837-2844.
8. Tahiri, I., Desbiens, M., Benech, R., Kheadr, E., Lacroix, C., Thibault, S., Quellet, D., and Fliss, I. (2004) Purification, characterization and amino acid sequencing of divergicin M35: a novel class IIa bacteriocin produced by Carnobacterium divergens M35, Int. J. Food Microbiol. 97, 123-136.
9. Le Marrec, C., Hyronimus, B., Bressollier, P., Verneuil, B., and Urdaci, M. C. (2000) Biochemical and genetic characterization of coagulin, a new antilisterial bacteriocin in the pediocin family of bacteriocins, produced by Bacillus coagulans I-4, Appl. Environ. Microbiol. 66, 5213-5220.
10. Marugg, J. D., Gonzalez, C. F., Kunka, B. S., Ledeboer, A. M., Pucci, M. J., Toonen, M. Y., Walker, S. A., Zoetmulder, L. C. M., and Vandenbergh, P. A. (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.
11. Yamazaki, K., Suzuki, M., Kawai, Y., Inoue, N., and Montville, T. J. (2005) Purification and characterization of a novel class IIa bacteriocin, piscicocin CS526, from surimi-associated Carnobacterium piscicola CS526, Appl. Environ. Microbiol. 71, 554-557.
12. Tichaczek, P. S., Vogel, R. F., and Hammes, W. P. (1994) Cloning and sequencing of Sakp encoding sakacin-P, the bacteriocin produced by Lactobacillus sake Lth-673, Microbiology 140, 361-367.
13. Kalmokoff, M. L., Banerjee, S. K., Cyr, T., Hefford, M. A., and Gleeson, T. (2001) Identification of a new plasmid-encoded sec-dependent bacteriocin produced by Listeria innocua 743, Appl. Environ. Microbiol. 67, 4041-4047.
14. Bennik, M. H. J., Vanloo, B., Brasseur, R., Gorris, L. G. M., and Smid, E. J. (1998) A novel bacteriocin with a YGNGV motif from vegetable-associated Enterococcus mundtii: full characterization and interaction with target organisms, Biochim. Biophys. Acta 1373, 47-58.
15. Kawamoto, S., Shima, J., Sato, R., Eguchi, T., Ohmomo, S., Shibato, J., Horikoshi, N., Takeshita, K., and Sameshima, T. (2002) Biochemical and genetic characterization of mundticin KS, an antilisterial peptide produced by Enterococcus mundtii NFRI 7393, Appl. Environ. Microbiol. 68, 3830-3840.
16. Jack, R. W., Wan, J., Gordon, J., Harmark, K., Davidson, B. E., Hillier, A. J., Wettenhall, R. E. H., Hickey, M. W., and Coventry, M. J. (1996) Characterization of the chemical and antimicrobial properties of piscicolin 126, a bacteriocin produced by Carnobacterium piscicola JG126, Appl. Environ. Microbiol. 62, 2897-2903.
17. Vaughan, A., Eijsink, V. G. H., O'Sullivan, T. F., O'Hanlon, K., and van Sinderen, D. (2001) An analysis of bacteriocins produced by lactic acid bacteria isolated from malted barley, J. Appl. Microbiol. 91, 131-138.
18. Fimland, G., Sletten, K., and Nissen-Meyer, J. (2002) The complete amino acid sequence of the pediocin-like antimicrobial peptide leucocin C, Biochem. Biophys. Res. Commun. 295, 826-827.
19. Hastings, J. W., Sailer, M., Johnson, K., Roy, K. L., Vederas, J. C., and Stiles, M. E. (1991) Characterization of leucocin-A-Ual-187 and cloning of the bacteriocin gene from Leuconostoc gelidum, J. Bacteriol. 173, 7491-7500.
20. Ferchichi, M., Frere, J., Mabrouk, K., and Manai, M. (2001) Lactococcin MMFII, a novel class IIa bacteriocin produced by Lactococcus lactis MMFII, isolated from a Tunisian dairy product, FEMS Microbiol. Lett. 205, 49-55.
21. Simon, L., Fremaux, C., Cenatiempo, Y., and Berjeaud, J. M. (2002) Sakacin G, a new type of antilisterial bacteriocin, Appl. Environ. Microbiol. 68, 6416-6420.
22. Van Reenen, C. A., Chikindas, M. L., Van Zyl, W. H., and Dicks, L. M. T. (2003) Characterization and heterologous expression of a class IIa bacteriocin, plantaricin 423 from Lactobacillus plantarum 423, in Saccharomyces cerevisiae, Int. J. Food Microbiol. 81, 29-40.
23. Atrih, A., Rekhif, N., Moir, A. J. G., Lebrihi, A., and Lefebvre, G. (2001) Mode of action, purification and amino acid sequence of plantaricin C19, an anti-Listeria bacteriocin produced by Lactobacillus plantarum C19, Int. J. Food Microbiol. 68, 93-104.
24. Tichaczek, P. S., Nissen-Meyer, J., Nes, I. F., Vogel, R. F., and Hammes, W. P. (1992) Characterization of the bacteriocins curvacin A from Lactobacillus curvatus Lth1174 and Sakacin-P from L. sake Lth673, Syst. Appl. Microbiol. 15, 460-468.
25. Quadri, L. E. N., Sailer, M., Roy, K. L., Vederas, J. C., and Stiles, M. E. (1994) Chemical and genetic characterization of bacteriocins produced by Carnobacterium piscicola Lvl7b, J. Biol. Chem. 269, 12204-12211.
26. Cintas, L. M., Casaus, P., Havarstein, L., Hernandez, P. E., and Nes, I. F. (1997) Biochemical and genetic characterization of enterocin P, a novel sec-dependent bacteriocin from Enterococcus faecium P13 with a broad antimicrobial spectrum, Appl. Environ. Microbiol. 63, 4321-4330.
27. Tomita, H., Fujimoto, S., Tanimoto, K., and Ike, Y. (1996) Cloning and genetic organization of the bacteriocin 31 determinant encoded on the Enterococcus faecalis pheromone responsive conjugative plasmid pYI17, J. Bacteriol. 178, 3585-3593.
28. Henderson, J. T., Chopko, A. L., and Vanwassenaar, P. D. (1992) Purification and primary structure of pediocin PA-1 produced by Pediococcus acidilactici Pac-10, Arch. Biochem. Biophys. 295, 5-12.
29. Holck, A., Axelsson, L., Birkeland, S. E., Aukrust, T., and Blom, H. (1992) Purification and amino acid sequence of sakacin A, a bacteriocin from Lactobacillus sake Lb706, J. Gen. Microbiol. 138, 2715-2720.
30. BhugalooVial, P., Dousset, X., Metivier, A., Sorokine, O., Anglade, P., Boyaval, P., and Marion, D. (1996) Purification and amino acid sequences of piscicocins V1a and V1b, two class IIa bacteriocins secreted by Carnobacterium piscicola V1 that display significantly different levels of specific inhibitory activity, Appl. Environ. Microbiol. 62, 4410-4416.
31. Moll, G. N., Konings, W. N., and Driessen, A. J. M. (1999) Bacteriocins: mechanism of membrane insertion and pore formation, Antonie van Leeuwenhoek 76, 185-198.
32. Chikindas, M. L., Garciagarcera, M. J., Driessen, A. J. M., Ledeboer, A. M., Nissen-Meyer, J., Nes, I. F., Abee, T., Konings, W. N., and Venema, G. (1993) Pediocin Pa-1, a bacteriocin from Pediococcus acidilactici Pac1.0, forms hydrophilic pores in the cytoplasmic membrane of target-cells, Appl. Environ. Microbiol. 59, 3577-3584.
33. Fimland, G., Eijsink, V. G. H., and Nissen-Meyer, J. (2002) Mutational analysis of the role of tryptophan residues in an antimicrobial peptide, Biochemistry 41, 9508-9515.
34. Gallagher, N. L. F., Sailer, M., Niemczura, W. P., Nakashima, T. T., Stiles, M. E., and Vederas, J. C. (1997) Three-dimensional structure of leucocin A in trifluoroethanol and dodecylphophocholine micelles: Spatial location of residues critical for biological activity in type IIa bacteriocins from lactic acid bacteria, Biochemistry 36, 15062-15072.
35. Wang, Y. J., Henz, M. E., Gallagher, N. L. F., Chai, S. Y., Gibbs, A. C., Yan, L. Z., Stiles, M. E., Wishart, D. S., and Vederas, J. C. (1999) Solution structure of carnobacteriocin B2 and implications for structure-activity relationships among type IIa bacteriocins from lactic acid bacteria, Biochemistry 38, 15438-15447.
36. Uteng, M., Hauge, H. H., Markwick, P. R. L., Fimland, G., Mantzilas, D., Nissen-Meyer, J., and Muhle-Goll, C. (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 bridges, Biochemistry 42, 11417-11426.
37. Chen, Y., Ludescher, R. D., and Montville, T. J. (1997) Electrostatic interactions, but not the YGNGV consensus motif govern the binding of pediocin PA-1 and its fragments to phospholipid vesicles, Appl. Environ. Microbiol. 63, 4770-4777.
38. Kazazic, M., Nissen-Meyer, J., and Fimland, G. (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.
39. Johnsen, L., Fimland, G., and Nissen-Meyer, J. (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.
40. Fimland, G., Johnsen, L., Axelsson, L., Brurberg, M. B., Nes, I. F., Eijsink, V. G. H., and Nissen-Meyer, J. (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.
41. Johnsen, L., Fimland, G., Mantzilas, D., and Nissen-Meyer, J. (2004) Structure-function analysis of immunity proteins of pediocin-like bacteriocins: C-terminal parts of immunity proteins are involved in specific recognition of cognate bacteriocins, Appl. Environ. Microbiol. 70, 2647-2652.
42. Uteng, M., Hauge, H. H., Brondz, L, Nissen-Meyer, J., and Fimland, G. (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.
43. Eijsink, V. G., Skeie, M., P. H., M., Brurberg, M. B., and Nes, I. F. (1998) Comparative studies of class IIa bacteriocins of lactic acid bacteria, Appl. Environ. Microbiol. 64, 3275-3281.
44. Anderssen, E. L., Diep, D. B., Nes, I. F., Eijsink, V. G., and Nissen-Meyer, J. (1998) Antagonistic activity of Lactobacillus plantarum C11: two new two-peptide, Appl. Environ. Microbiol. 64, 2269-2272.
45. Sreerama, N., and Woody, R. W. (2000) Estimation of protein secondary structure from circular dichroism spectra: Comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set, Anal. Biochem. 287, 252-260.
46. Sklenar, V., Piotto, M., Leppik, R., and Saudek, V. (1993) Gradient tailored water suppression for H-1-N-15 Hsqc experiments optimized to retain full sensitivity, J. Magn. Reson., Ser. A 102, 241-245.
47. Braunschweiler, L., and Ernst, R. R. (1983) Coherence transfer by isotropic mixing: application to proton correlation spectroscopy, J. Magn. Reson. 53, 521.
48. Jeener, J., Meier, B. H., Bachmann, P., and Ernst, R. R. (1979) Investigation of exchange processes by 2-dimensional NMR-spectroscopy, J. Chem. Phys. 71, 4546-4553.
49. Wuthrich, K. (1986) NMR of proteins and nucleic acids, Wiley-Interscience, New York.
50. Delaglio, F., Grzesiek, S., Vuister, G. W., Zhu, G., Pfeifer, J., and Bax, A. (1995) NMRpipe-a multidimensional spectral processing system based on Unix pipes, J. Biomol. NMR 6, 277-293.
51. Wishart, D. S., Bigam, C. G., Yao, J., Abildgaard, F., Dyson, H. J., Oldfield, E., Markley, J. L., and Sykes, B. D. (1995) H-1, C-13 and N-15 chemical-shift referencing in biomolecular NMR, J. Biomol. NMR 6, 135-140.
52. Cornilescu, G., Delaglio, F., and Bax, A. (1999) Protein backbone angle restraints from searching a database for chemical shift and sequence homology, J. Biomol. NMR 13, 289-302.
53. Guntert, P., Mumenthaler, C., and Wuthrich, K. (1997) Torsion angle dynamics for NMR structure calculation with the new program DYANA, J. Mol. Biol. 273, 283-298.
54. Guntert, P. (2004) in Methods in molecular biology, protein NMR techniques (Downing, A. K., Ed.) pp 353-378, Humana Press, Totowa, NJ.
55. Koradi, R., Billeter, M., and Wuthrich, K. (1996) MOLMOL: A program for display and analysis of macromolecular structures, J. Mol. Graphics 14, 51.
56. Sreerama, N., and Woody, R. W. (1994) Protein secondary structure from circular-dichroism spectroscopy-combining variable selection principle and cluster analysis with neural-network, ridge-regression and self-consistent methods, J. Mol. Biol. 242, 497-507.
57. Sreerama, N., and Woody, R. W. (1993) A self-consistent method for the analysis of protein secondary structure from circular dichroism, Biophys. J. 64, A170.
58. Johnson, W. C. (1999) Analyzing protein circular dichroism spectra for accurate secondary structures, Proteins, Struct., Fund., Genet. 35, 307-312.
59. Sreerama, N., and Woody, R. W. (2000) Analysis of protein CD spectra: Comparison of CONTIN, SELCON3, and CDSSTR methods in CD Pro software, Biophys. J. 78, 334 A.
60. Wishart, D. S., Sykes, B. D., and Richards, F. M. (1991) Simple techniques for the quantification of protein secondary structure by H-1-NMR spectroscopy, FEBS Lett. 293, 72-80.
61. Wishart, D. S., Sykes, B. D., and Richards, F. M. (1991) Relationship between nuclear-magnetic-resonance chemical shift and protein secondary structure, J. Mol. Biol. 222, 311-333.
62. Laskowski, R. A., MacArthur, M. W., Moss, D. S., and Thornton, J. M. (1993) PROCHECK: a program to check the stereochemcial quality of protein structures, J. Appl. Crystallogr. 26, 283-291.
63. Kaur, K., Andrew, L. C., Wishart, D. S., and Vederas, J. C. (2004) Dynamic relationships among type IIa bacteriocins: temperature effects on antimicrobial activity and on structure of the C-terminal amphipathic alpha helix as a receptor-binding region, Biochemistry 43, 9009-9020.
64. Sprules, T., Kawulka, K. E., and Vederas, J. C. (2004) NMR solution structure of ImB2, a protein conferring immunity to antimicrobial activity of the type IIa bacteriocin, carnobacteriocin B2, Biochemistry 43, 11740-11749.
65. Yan, L. Z., Gibbs, A. C., Stiles, M. E., Wishart, D. S., and Vederas, J. C. (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.
66. Finnland, G., Jack, R., Jung, G., Nes, I. F., and Nissen-Meyer, J. (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.
67. Saavedra, L., Minahk, C., Holgado, A. P. D., and Sesma, F. (2004) Enhancement of the enterocin CRL35 activity by a synthetic peptide derived from the NH2-terminal sequence, Antimicrob, Agents Chemother. 48, 2778-2781.
68. Ramnath, M., Beukes, M., Tamura, K., and Hastings, J. W. (2000) Absence of a putative mannose-specific phosphotransferase system enzyme IIAB component in a leucocin A-resistant strain of Listeria monocytogenes, as shown by two-dimensional sodium dodecyl sulfate-polyacrylamide gel electrophoresis, Appl. Environ. Microbiol. 66, 3098-3101.
69. Hechard, Y., Pelletier, C., Cenatiempo, Y., and Frere, J. (2001) Analysis of sigma(54)-dependent genes in Enterococcus faecalis: a mannose PTS permease (EIIMan) is involved in sensitivity to a bacteriocin, mesentericin Y105, Microbiology 147, 1575-1580.
70. Gravesen, A., Ramnath, M., Rechinger, K. B., Andersen, N., Jansch, L., Hechard, Y., Hastings, J. W., and Knochel, S. (2002) High-level resistance to class IIa bacteriocins is associated with one general mechanism in Listeria monocytogenes, Microbiology 148, 2361-2369.
71. Dalet, K., Cenatiempo, Y., Cossart, P., and Hechard, Y. (2001) A sigma(54)-dependent PTS permease of the mannose family is responsible for sensitivity of Listeria monocytogenes to mesentericin Y105, Microbiology 147, 3263-3269.
72. Ramnath, M., Arous, S., Gravesen, A., Hastings, J. W., and Hechard, Y. (2004) Expression of mptC of Listeria monocytogenes induces sensitivity to class IIa bacteriocins in Lactococcus lactis, Microbiology 150, 2663-2668.
73. Xue, J. F., Hunter, I., Steinmetz, T., Peters, A., Ray, B., and Miller, K. W. (2005) Novel activator of mannose-specific phosphotransferase system permease expression in Listeria innocua, identified by screening for pediocin AcH resistance, Appl. Environ. Microbiol. 71, 1283-1290.
74. Fimland, G., Eijsink, V. G. H., and Nissen-Meyer, J. (2002) Comparative studies of immunity proteins of pediocin-like bacteriocins, Microbiology 148, 3661-3670.
75. Fleury, Y., Dayem, M. A., Montagne, J. J., Chaboisseau, E., LeCaer, J. P., Nicolas, P., and Delfour, A. (1996) Covalent structure, synthesis, and structure-function studies of mesentericin Y 105(37), a defensive peptide from gram-positive bacteria Leuconostoc mesenteroides, J. Biol. Chem. 271, 14421-14429.