Antimicrobial peptides

Nutraceutical Proteins and Peptides in Health and Disease

Volumn , Issue , 2005, Pages 99-136

  Chan, Judy C K ^a   Li Chan, Eunice C Y ^a  

^a UNIVERSITY OF BRITISH COLUMBIA   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

EID: 85122907090     PISSN: None     EISSN: None     Source Type: Book    
DOI: None     Document Type: Chapter

References (253)

1. M. Zasloff. Antimicrobial peptides of multicellular organisms. Nature, 415: 389-395, 2002.
2. H.I. Zeya, J.K. Spitznagel. Cationic proteins of polymorphonuclear leukocyte lysosomes. II. Composition, properties, and mechanism of antibacterial action. J. Bacteriol., 91: 755-762, 1966.
3. H.I. Zeya, J.K. Spitznagel. Cationic proteins of polymorphonuclear leukocyte lysosomes. I. Resolution of antibacterial and enzymatic activities. J. Bacteriol., 91: 750-754, 1966.
4. R.I. Lehrer, T. Ganz. Defensins of vertebrate animals. Curr. Opin. Immunol., 14: 96-102, 2002.
5. A.J. Ouellette, C.L. Bevins. Paneth cell defensins and innate immunity of the small bowel. Inflamm. Bowel Dis., 7: 43-50, 2001.
6. M.V. Sawai, H.P. Jia, L. Liu, V. Aseyev, J.M. Wiencek, P.B.J. McCray, T. Ganz, W.R. Kearney, B.F. Tack. The NMR structure of human beta-defensin-2 reveals a novel alpha-helical 14 segment. Biochemistry, 40: 3810-3816, 2001.
7. C. Hill, J. Yee, M.E. Selsted, D. Eisenberg. Crystal structure of defensin HNP-3, an amphiphilic dimer: mechanisms of membrane permeabilization. Science, 251: 5000, 1991.
8. Y.-Q. Tang, J. Yuan, G. Ösapay, K. Ösapay, D. Tran, C.J. Miller, A.J. Ouellette, M.E. Selsted. A cyclic antimicrobial peptide produced in primate leukocytes by the ligation of two 19 truncated alpha-defensin. Science, 286: 498-502, 1999.
9. M. Trabi, H.J. Schirra, D.J. Craik. Three-dimensional structure of RTD-1, a cyclic antimicrobial defensin from Rhesus macaque leukocytes. Biochemistry, 40: 4211-4221, 2001.
10. W. Wang, A.M. Cole, T. Hong, A.J. Waring, R.I. Lehrer. Retrocyclin, an antiretroviral theta-defensin, is a lectin. J. Immunol., 170: 4708-1716, 2003.
11. M. Zanetti, R. Gennaro, D. Romeo. Cathelicidins: a novel protein family with a common proregion and a variable C-terminal antimicrobial domain. FEBS Lett., 374: 1-5, 1995.
12. A. Tossi, L. Sandri, A. Giangaspero. Amphipathic, alpha-helical antimicrobial peptides. Biopolymers, 55: 4-30, 2000.
13. B. Ramanathan, E.G. Davis, C.R. Ross, F. Blecha. Cathelicidins: microbicidal activity, mechanisms of actions, and roles in innate immunity. Microb. Infect., 4: 361-372, 2002.
14. P. Storici, M. Scocchi, A. Tossi, R. Gennaro, M. Zanetti. Chemical synthesis and biological activity of a novel antibacterial peptide deduced from a pig myeloid cDNA. FEBS Lett., 337: 303-307, 1994.
15. H. Wu, G. Zhang, C.R. Ross, F. Blecha. Cathelicidin gene expression in porcine tissues: roles in ontogeny and tissue specificity. Infect. Immun., 67: 439-442, 1999.
16. G. Zhang, C.R. Ross, F. Blecha. Porcine antimicrobial peptides: new prospects for ancient molecules of host defense. Vet. Res., 31: 277-296, 2000.
17. M.M. Mahoney, A.Y. Lee, D.J. Brezinski-Caliguri, K.M. Huttner. Molecular analysis of the 16 sheep cathelin family reveals a novel antimicrobial peptide. FEBS Lett., 377: 519-522, 1995.
18. B. Skerlavaj, M. Benincasa, A. Risso, M. Zanetti, R. Gennaro. SMAP-29: a potent antibacterial and antifungal peptide from sheep leukocytes. FEBS Lett., 463: 58-62, 1999.
19. J. Larrick, M. Hirata, Y. Shimomoura, M. Yoshida, H. Zheng, J. Zhong, S. Wright. Antimicrobial activity of rabbit CAP18-derived peptides. Antimicrob. Agents Chemother., 37: 2534-2539, 1993.
20. K.A. Zarember, S.S. Katz, B.F. Tack, L. Doukhan, J. Weiss, P.H. Elsbach. Host defense 1 functions of proteolytically processed and parent (unprocessed) cathelicidins of rabbit granulocytes. Infect. Immun., 70: 569-576, 2002.
21. R. Gennaro, M. Scocchi, L. Merluzzi, M. Zanetti. Biological characterization of a novel mammalian antimicrobial peptide. Biochim. Biophys. Acta, 1425: 361-368, 1998.
22. J.W. Larrick, M. Hirata, R.F. Balint, J. Lee, J. Zhong, S.C. Wright. Human CAP18: a novel antimicrobial lipopolysaccharide-binding protein. Infect. Immun., 63: 1291-1297, 1995.
23. J.B. Cowland, A.H. Johnsen, N. Borregaard. hCAP-18, a cathelin/pro-bactenecin-like protein of human neutrophil specific granules. FEBS Lett., 368: 173-176, 1995.
24. A.E. Popsueva, M.V. Zinovjeva, J.W. Visser, J.M. Zijlmans, W.E. Fibbe, A.V. Belyavsky. A novel murine cathelin-like protein expressed in bone marrow. FEBS Lett., 391: 5-8, 1996.
25. R.L. Gallo, K.J. Kim, M. Bernfield, C.A. Kozak, M. Zanetti, L. Merluzzi, R. Gennaro. Identification of CRAMP, a cathelin-related antimicrobial peptide expressed in the embryonic and adult mouse. J. Biol. Chem., 272: 13088-13093, 1997.
26. R.W. Frank, R. Gennaro, K. Schneider, M. Przybylski, D. Romeo. Amino acid sequences of two proline-rich bactenecins. Antimicrobial peptides of bovine neutrophils. J. Biol. Chem., 265: 18871-18874, 1990.
27. B. Agerberth, J.Y. Lee, T. Bergman, M. Carlquist, H.G. Boman, V. Mutt, H. Jornvall. Amino acid sequence of PR-39. Isolation from pig intestine of a new member of the family of proline-arginine-rich antibacterial peptides. Eur. J. Biochem., 202: 849-854, 1991.
28. D. Romeo, B. Skerlavaj, M. Bolognesi, R. Gennaro. Structure and bactericidal activity of an antibiotic dodecapeptide purified from bovine neutrophils. J. Biol. Chem., 263: 9573-9575, 1988.
29. V.N. Kokryakov, S.S.L. Harwig, E.A. Panyutich, A.A. Schevchenko, G.M. Aleshina, O.V. Shamova, H.A. Korneva, R.I. Lehrer. Protegrins: leukocyte antimicrobial peptides that combine features of corticostatic defensins and tachyplesins. FEBS Lett., 327: 231-236, 1993.
30. M.E. Selsted, M.J. Novotny, W.L. Morris, Y.-Q. Tang, W. Smith, J.S. Cullor. Indolicidin, a novel bactericidal tredecapeptide amide from neutrophils. J. Biol. Chem., 267, 1992.
31. S.M. Travis, N.N. Anderson, W.R. Forsyth, C. Espiritu, B.-A.D. Conway, E.P. Greenberg, P.B.J. McCray, R.I. Lehrer, M.J. Welsh, B.F. Tack. Bactericidal activity of mammalian cathelicidin-derived peptides. Infect. Immun., 68: 2748-2755, 2000.
32. L. Saiman, S. Tabibi, T.D. Starner, P. San Gabriel, P.L. Winokur, H.P. Jia, P.B. McCray, Jr., B.F. Tack. Cathelicidin peptides inhibit multiply antibiotic-resistant pathogens from patients with cystic fibrosis. Antimicrob. Agents Chemother., 45: 2838-2844, 2001.
33. F. García-Olmedo, A. Molina, J.M. Alamillo, P. Rodríguez-Palenzuéla. Plant defense peptides. Biopolymers (Pept. Sci.), 47: 479-491, 1998.
34. F. García-Olmedo, P. Rodríguez-Palenzuela, A. Molina, J.M. Alamill, E. López-Solanilla, M. Berrocal-Lobo, C. Poza-Carrión. Antibiotic activities of peptide, hydrogen peroxide and peroxynitrite in plant defence. FEBS Lett., 498: 219-222, 2001.
35. W.F. Broekaert, F.R.G. Terras, B.P.A. Cammue, R.W. Osborn. Plant defensins: novel antimicrobial peptides as components of the host defense system. Plant Physiol., 108: 1353-1358, 1995.
36. F.J. Colilla, A. Rocher, E. Mendez. Gamma-purothionins: amino acid sequence of two polypeptides of a new family of thionins from wheat endosperm. FEBS Lett., 270: 191-194, 1990.
37. E. Mendez, A. Moreno, F. Colilla, F. Pelaez, G.G. Limas, R. Mendez, F. Soriano, M. Salinas, C. De Haro. Primary structure and inhibition of protein synthesis in eukaryotic cell-free system of a novel thionin, 7-hordothionin, from barley endosperm. Eur. J. Biochem., 194: 533-539, 1990.
38. Y. Zhang, K. Lewis. Fabatins: new antimicrobial plant peptides. FEMS Microbiol. Lett., 149: 59-64, 1997.
39. F.R.G. Terras, H.M.E. Schoofs, M.F.C. De Bolle, F. Van Leuven, S.B. Rees, J. Vanderleyden, B.P.A. Cammue, W.F. Broekaert. Analysis of two novel classes of plant antifungal proteins from radish (Raphanus sativus L.) seeds. J. Biol. Chem., 267: 15301-15309, 1992.
40. A.L. Vilas Alves, G.W. Samblanx, F.R.G. Terras, B.P.A. Cammue, W. Broekaert. Expression of functional Raphanus sativus antifungal protein in yeast. FEBS Lett., 348: 228-232, 1994.
41. A. Segura, M. Moreno, A. Molina, F. García-Olmedo. Novel defensin subfamily from spinach (Spinacia oleracea). FEBS Lett., 435: 159-162, 1998.
42. M.S. Almeida, K.M.S. Cabral, R.B. Zingali, E. Kurtenbach. Characterization of two novel defense peptides from pea (Pisum sativum) seeds. Arch. Biochem. Biophys., 378: 278-286, 2000.
43. M.S. Almeida, K.M.S. Cabral, E. Kurtenbach, F.C.L. Almeida, A.P. Valente. Solution structure of Pisum sativum defensin 1 by high resolution NMR: plant defensins, identical backbone with different mechanisms of action. J. Mol. Biol., 315: 749-757, 2002.
44. M. Moreno, A. Segura, F. García-Olmedo. Pseudothionin-St1, a potato peptide active against potato pathogen. Eur. J. Biochem., 223: 135-139, 1994.
45. W.J. Stiekema, F. Heidekamp, W.G. Dirkse, J. van Beckum, P. de Haan, C. ten Bosch, J.D. Louwerse. Molecular cloning and analysis of four potato tuber mRNAs. Plant Mol. Biol., 11: 255-269, 1988.
46. B. Meyer, G. Houlne, J. Pozueta-Romero, M.L. Schantz, R. Schantz. Fruit-specific expression of a defensin-type gene family in bell pepper. Plant Physiol., 112: 615-622, 1996.
47. M. Aluru, J. Curry, M.A. O'Connell. Nucleotide sequence of a defensin of gramma-thionin-like gene from habanera chili. Plant Physiol., 120: 633, 1999.
48. Q. Gu, E.E. Kawata, M.-J. Morse, H.-M. Wu, A.Y. Cheung. A flower-specific cDNA encoding a novel thionin in tobacco. Mol. Gen. Genet., 234: 89-96, 1992.
49. F.T. Lay, F. Brugliera, M.A. Anderson. Isolation and properties of floral defensins from ornamental tobacco and petunia. Plant Physiol., 131: 1283-1293, 2003.
50. B. Karunanandaa, A. Singh, T.-H. Kao. Characterization of a predominantly pistil-expressed gene encoding a gamma-thionin-like protein of Petunia inflata. Plant Mol. Biol., 26, 1994.
51. J.-P. Douliez, T. Michon, K. Elmorjani, D. Marion. Structure, biological and technological functions of lipid fransfer proteins and indolines, the major lipid binding proteins from cereal kernels. J. Cereal Sci., 32: 1-20, 2000.
52. K.K. Nielsen, J.E. Nielsen, S.M. Madrid, J.D. Mikkelsen. New antifungal proteins from sugar beet (Beta vulgaris L.) showing homology to non-specific lipid transfer proteins. Plant Mol. Biol., 31: 539-552, 1996.
53. J.-C. Kader. Lipid-transfer proteins in plants. Annu. Rev. Plant Physiol. Plant Mol. Biol., 47: 627-654, 1996.
54. M.S. Castro, I.R. Gerhardt, S. Orrù, P. Pucci, C. Bloch Jr. Purification and characterization of a small (7.3 kDa) putative lipid transfer protein from maize seeds. J. Chromatrogr., B 794: 109-114, 2003.
55. A. Molina, A. Segura, F. García-Olmedo. Lipid transfer protein (nsLTPs) from barley and maize leaves are potent inhibitors of bacterial and fungal plant pathogens. FEBS Lett., 316: 119-122, 1993.
56. A. Segura, M. Moreno, F. García-Olmedo. Purification and antipathogenic activity of lipid transfer proteins from the leaves of Arabidopsis and spinach. FEBS Lett., 3: 243-246, 1993.
57. J. Pyee, H. Yu, P.E. Kolattukudy. Identification of a lipid transfer protein as the major protein in the surface wax of broccoli (Brassica oleracea) leaves. Arch. Biochem. Biophys., 311: 460-468, 1994.
58. B.L. Archer. The proteins of Hevea brasiliensis latex. Isolation and characterization of crystalline hevein. Biochemistry, J 75: 236-240, 1960.
59. J.C. Koo, S.Y. Lee, H.J. Chun, Y.H. Cheong, J.S. Choi, S. Kawabata, M. Miyagi, S. Tsunasawa, K.S. Ha, D.W. Bae, C.-D. Han, B.L. Lee, M.J. Cho. Two hevein homologs isolated from the seed of Pharbitis nil L. exhibit potent antifungal activity. Biochim. Biophys. Acta, 1382: 80-90, 1998.
60. X. Huang, W.-J. Xie, Z.-Z. Gong. Characteristics and antifungal activity of a chitin binding protein from Ginkgo biloba. FEBS Lett., 478: 123-126, 2000.
61. S.-S. Li, P. Claeson. Cys/Gly-rich proteins with a putative single chitin-binding domain from oat (Avena sativa) seeds. Phytochemistry, 63: 249-255, 2003.
62. K.P.B. Van den Bergh, P. Proost, J. Van Damme, J. Coosemans, E.J.M.V. Damme, W.J. Peumans. Five disulfide bridges stabilize a hevein-type antimicrobial peptide from the bark of spindle tree (Euonymus europaeus L.). FEBS Lett., 530: 181-185, 2002.
63. A. Kiba, H. Saitoh, M. Nishihara, K. Omiya, S. Yamamura. C-Terminal domain of a hevein- like protein from Wasabia japonica has potent antimicrobial activity. Plant Cell. Physiol., 44: 296-303, 2003.
64. B.P.A. Cammue, M.F.C. De Bolle, F.R.G. Terras, P. Proost, J. Van Damme, S.B. Rees, J. Vanderleyden, W.F. Broekaert. Isolation and characterization of a novel class of plant antimicrobial peptides from Mirabilis jalapa L. seeds. J. Biol. Chem., 267: 2228-2233, 1992.
65. M.F. De Bolle, K. Eggermont, R.E. Duncan, R.W. Osborn, F.R. Terras, W.F. Broekaert. Cloning and characterization of two cDNA clones encoding seed-specific antimicrobial peptides from Mirabilis jalapa L. Plant Mol. Biol., 28: 713-721, 1995.
66. F. Shao, Z. Hu, Y.-M. Xiong, Q.-Z. Huang, C.-G. Wang, R.-H. Zhu, D.-C. Wang. A new antifungal peptide from the seeds of Phytolacca americana: characterization, amino acid sequence and cDNA cloning. Biochim. Biophys. Acta, 1430: 262-268, 1999.
67. G.-H. Gao, W. Liu, J.-X. Dai, J.-F. Wang, Z. Hu, Y. Zhang, D.-C. Wang. Solution structure of PAFP-s: a new knottin-type antifungal peptide from the seeds of Phytolacca americana. Biochemistry, 40: 10973-10978, 2001.
68. R.H. Tailor, D.P. Acland, S. Attenborough, B.P.A. Cammue, I.J. Evans, R.W. Osborn, J.A. Ray, S.B. Rees, W.F. Broekaert. A novel family of small cysteine-rich antimicrobial peptides from seed of Impatiens balsamina is derived from a single precursor protein. J. Biol. Chem., 272: 24480-24487, 1997.
69. S.U. Patel, R.W. Osborn, S. Rees, J.M. Thornton. Structural studies of Impatiens balsamina antimicrobial protein (Ib-AMP1). Biochemistry, 37: 983-990, 1998.
70. A. Segura, M. Moreno, F. Madueno, A. Molina, F. García-Olmedo. Snakin-1, a peptide from potato that is active against plant pathogens. Mol. Plant-Microb. Interact., 12: 16-23, 1999.
71. M. Berrocal-Lobo, A. Segura, M. Moreno, G. López, F. García-Olmedo, A. Molina. Snakin-2, an antimicrobial peptide from potato whose gene is locally induced by wounding and responds to pathogen infection. Plant Physiol., 128: 951-961, 2002.
72. T. Ando, S. Ishii, M. Yamasaki, K. Iwai, C. Hashimoto, F. Sawada. Protamines. I. Amino acid composition and homogeneity of clupeine, salmine, and iridine. J. Biochem. (Tokyo), 44: 275-288, 1957.
73. K. Iwai, C. Nakahara, T. Ando. Protamines. XV. Complete amino acid sequence of the Z component of clupeine. Application of N-O acyl rearrangement and selective hydrolysis in sequence determination. J. Biochem. (Tokyo), 69: 493-509, 1971.
74. K. Suzuki, T. Ando. Protamines. XVI. Complete amino acid sequence of clupeine YII. J. Biochem. (Tokyo), 72: 1419-1432, 1972.
75. K. Suzuki, T. Ando. Protamines. XVII. Complete amino acid sequence of clupeine YI. J. Biochem. (Tokyo), 72: 1433-1446, 1972.
76. N.M.D. Islam, T. Itakura, T. Motohiro. Antibacterial spectra and minimum inhibition concentration of clupeine and salmine. Bull. Jpn. Soc. Sci. Fish., 50: 1705-1708, 1984.
77. M. Uyttendaele, J. Debevere. Evaluation of the antimicrobial activity of prota-mine. Food Microbiol., 11: 417-427, 1994.
78. L. Truelstrup Hansen, T.A. Gill. Solubility and antimicrobial efficacy of protamine on Listeria monocytogenes and Escherichia coli as influenced by pH. J. Appl. Microbiol., 88: 1049-1055, 2000.
79. L. Truelstrup Hansen, J.W. Austin, T.A. Gill. Antibacterial effect of protamine in combination with EDTA and refrigeration. Int. J. Food Microbiol., 66: 149-161, 2001.
80. C. Johansen, T.A. Gill, L. Gram. Changes in cell morphology of Listeria mono-cytogenes and Shewanella putrefaciens resulting from the action of protamine. Appl. Environ. Microbiol., 62: 1058-1064, 1996.
81. C. Johansen, A. Verheul, L. Gram, T.A. Gill, T. Abee. Protamine-induced perme-abilization of cell envelopes of Gram-positive and Gram-negative bacteria. Appl. Environ. Microbiol., 63: 1155-1159, 1997.
82. S.A. Thompson, K. Tachibana, K. Nakanishi, I. Kubota. Melittin-like peptides from the shark-repelling defense secretion of the sole Pardachirus pavoninus. Science, 233: 341-343, 1986.
83. R. Pal, Y. Barenholz, R.R. Wagner. Pardaxin, a hydrophobic toxin of the Red Sea flatfish, disassembles the intact membrane of vesicular stomatitis virus. J. Biol. Chem., 256: 10209-10212, 1981.
84. Y. Shai, J. Fox, C. Caratsch, Y.-L. Shih, C. Edwards, P. Lazarovici. Sequencing and synthesis of pardaxin, a polypeptide from the Red Sea Moses sole with ionophore activity. FEBS Lett., 242: 161-166, 1988.
85. P. Lazarovici. The structure and function of pardaxin. J. Toxicol. Toxin Rev., 21: 391-421, 2002.
86. Z. Oren, Y. Shai. A class of potent antibacterial peptides derived from pardaxin, a pore forming peptide isolated from Moses sole, Paradachirus marmoratus. Eur. J. Biochem., 237: 303-310, 1996.
87. A.M. Cole, P. Weis, G. Diamond. Isolation and characterization of pleurocidin, an antimicrobial peptide in the skin secretions of winter flounder. J. Biol. Chem., 272: 12008-12103, 1997.
88. S.E. Douglas, J.W. Gallant, Z.-Z. Gong, C. Hew. Cloning and developmental expression of a family of pleurocidin-like antimicrobial peptides from winter flounder, Pleuronectes americanus (Walbaum). Dev. Comp. Immunol., 25: 137-147, 2001.
89. A.M. Cole, R.O. Darouiche, D. Legarda, N. Connell, G. Diamond. Characterization of a fish antimicrobial peptide: gene expression, subcellular localization, and spectrum of activity. Antimicrob. Agents. Chemother., 44: 2039-2045, 2000.
90. N. Saint, H. Cadiou, Y. Bessin, G. Molle. Antibacterial peptide pleurocidin forms ion channels in planar lipid bilayers. Biochim. Biophys. Acta, 1564: 359-364, 2002.
91. K. Yoshida, Y. Mukai, T. Niidome, T. Hatakeyama, H. Aoyagi. Property and activity of amphiphilic antibacterial peptide pleurocidin. Pept. Sci., 35, 1999.
92. S. Inoue, B.-H. Nam, I. Hirono, T. Aoki. A survey of expressed genes in Japanese flounder (Paralichthys olivaceus) liver and spleen. Mol. Mar. Biol. Biotechnol., 6: 376-380, 1997.
93. S.E. Douglas, J.W. Gallant, C.E. Bullerwell, C. Wolff, J. Munholland, M.E. Reith. Winter flounder expressed sequence tags: establishment of an EST database and identification of novel fish genes. Mar. Biotechnol., 1: 458-464, 1999.
94. S.E. Douglas, J.W. Gallant, R.S. Liebscher, A. Dacanay, S.C.M. Tsoi. Identification and expression analysis of hepcidin-like antimicrobial peptides in bony fish. Dev. Comp. Immunol., 27: 589-601, 2003.
95. A.Y. Gracey, J.V. Troll, G.N. Somero. Hypoxia-induced gene expression profiling in the euryoxic fish Gillichthys mirabilis. Proc. Natl. Acad. Sci. USA, 98: 1993-1998, 2001.
96. H. Shike, X. Lauth, M.E. Westerman, V.E. Ostland, J.M. Carlberg, J.C. Van Olst, C. Shimizu, P. Bulet, J.C. Burns. Bass hepcidin is a novel antimicrobial peptide induced by bacterial challenge. Eur. J. Biochem., 269: 2232-2237, 2002.
97. C.B. Park, J.M. Lee, I.Y. Park, M.S. Kim, S.C. Kim. A novel antimicrobial peptide from the loach, Misgurnus anguillicaudatus. FEBS Lett., 411: 173-178, 1997.
98. I.Y. Park, C.B. Park, M.S. Kim, S.C. Kim. Parasin I, an antimicrobial peptide derived from histone H2A in the catfish, Parasilurus asotus. FEBS Lett., 437: 258-262, 1998.
99. G. Basañez, A.E. Shinnar, J. Zimmerberg. Interaction of hagfish cathelicidin antimicrobial peptides with model lipid membranes. FEBS Lett., 532: 115-120, 2002.
100. X. Lauth, H. Shike, J.C. Burns, M.E. Westerman, V.E. Ostland, J.M. Carlberg, J.C.V. Olst, V. Nizet, S.W. Taylor, C. Shimizu, P. Bulet. Discovery and characterization of two isoforms of moronecidin, a novel antimicrobial peptide from hybrid striped bass. J. Biol. Chem., 277: 5030-5039, 2002.
101. E.J. Noga, T.A. Arroll, R.A. Bullis, L. Khoo. Antibacterial activity in hemolymph of white shrimp Penaeus setiferus. J. Mar. Biotechnol., 4: 181-184, 1996.
102. J. Pan, A. Kurosky, B. Xu, A.K. Chopra, D.H. Coppenhaver, I.P. Singh, S. Baron. Broad antiviral activity in tissue of crustaceans. Antivir. Res., 48: 39-47, 2000.
103. J.R.S. Chisholm, V.J. Smith. Camparison of antibacterial activity in the hemocytes of different crustacean species. Comp. Biochem. Physiol., A110: 39-45, 1995.
104. E.J. Noga, T.A. Arroll, Z. Fan. Specificity and some physiochemical characteristics of the antibacterial activity from the blue crab Callinectes sapidus. Fish Shellfish Immunol., 6, 1996.
105. T. Haug, A.K. Kjuul, K. Stensvåga, E. Sandsdalen, O.B. Styrvold. Antibacterial activity in four marine crustacean decapods. Fish Shellfish Immunol., 12: 371-385, 2002.
106. D. Schnapp, G.D. Kemp, V.J. Smith. Purification and characterization of a proline-rich antibacterial peptide with sequence similarity to bactenecin-7, from the haemocytes of the shore crab, Carcinus maenas. Eur. J. Biochem., 240: 532-539, 1996.
107. J.M. Relf, J.R.S. Chisholm, G.D. Kemp, V.J. Smith. Purification and characterization of a cysteine-rich 5-kDa antibacterial protein from the granular haemocytes of the shore crab, Carcinus maenas. Eur. J. Biochem., 264: 350-357, 1999.
108. L. Khoo, D.W. Robinette, E.J. Noga. Callinectin an antibacterial peptide from the blue crab, Callinectes sapidus, hemocytes. Mar. Biotechnol., 1: 44-51, 1999.
109. T. Nakamura, H. Furunaka, T. Miyata, F. Tokunaga, T. Muta, S. Iwanaga, M. Niwa, T. Takao, Y. Shimonishi. Tachyplesin, a class of antimicrobial peptide from the hemocytes of the horseshoe crab (Tachypleus tridentatus). Isolation and chemical structure. J. Biol. Chem., 263: 16709-16713, 1988.
110. T. Saito, S. Kawabata, T. Shigenaga, Y. Takayenoki, J. Cho, H. Nakajima, M. Hirata, S. Iwanaga. A novel big defensin identified in horseshoe crab hemocytes: isolation, amino acid sequence, and antibacterial activity. J. Biochem., 117: 1131-1137, 1995.
111. S. Kawabata, R. Nagayama, M. Hirata, T. Shigenaga, K.L. Agarwala, T. Saito, J. Cho, H. Nakajima, T. Takagi, S. Iwanaga. Tachycitin, a small granular component in horseshoe crab hemocytes, is an antimicrobial protein with chitin-binding activity. J. Biochem., 120: 1253-1260, 1996.
112. T. Osaki, M. Omotezako, R. Nagayama, M. Hirata, S. Iwanaga, J. Kasahara, J. Hattori, I. Ito, H. Sugiyama, S. Kawabata. Horseshoe crab hemocyte-derived antimicrobial polypeptides, tachystatins, with sequence similarity to spider neurotoxins. J. Biol. Chem., 274: 26172-26178, 1999.
113. N. Fujitani, S.-I. Kawabata, T. Osaki, Y. Kumaki, M. Demura, K. Nitta, K. Kawano. Structure of the antimicrobial peptide tachystatin A. J. Biol. Chem., 277: 23651-23657, 2002.
114. D. Destoumieux, P. Bulet, D. Loew, A. Van Dorsselaer, J. Rodriguez, E. Bachère. Penaeidins, a new family of antimicrobial peptides isolated from the shrimp Penaeus vannamei (Decapoda). J. Biol. Chem., 272: 28398-28406, 1997.
115. M. Muñoz, F. Vandenbulcke, Y. Gueguen, E. Bachère. Expression of penaeidin antimicrobial peptides in early larval stages of the shrimp Penaeus vannamei. Dev. Comp. Immunol., 27: 283-289, 2003.
116. E. Bachère, D. Destoumieux, P. Bulet. Penaeidins, antimicrobial peptides of shrimp: a comparison with other effectors of innate immunity. Aquaculture, 191: 71-88, 2000.
117. D. Destoumieux, P. Bulet, J.-M. Strub, A. van Dorsselaer, E. Bachèr. Recombinant expression and range of activity of penaeidins, antimicrobial peptides from penaeid shrimp. Eur. J. Biochem., 266: 335-346, 1999.
118. T.C. Bartlett, B.J. Cuthbertson, E.F. Shepard, R.W. Chapman, P.S. Gross, G.W. Warr. Crustins, homologues of an 11.5-kDa antibacterial peptide, from two species of penaeid shrimp, Litopenaeus vannamei and Litopenaeus setiferus. Mar. Biotechnol., 4: 278-293, 2002.
119. G. Mitta, F. Hubert, E.A. Dyrynda, P. Boudry, P. Roch. Mytilin B and MGD2, two antimicrobial peptides of marine mussels: gene structure and expression analysis. Dev. Comp. Immunol., 24: 381-393, 2000.
120. G. Mitta, F. Vandenbulcke, P. Roch. Original involvement of antimicrobial peptides in mussel innate immunity. FEBS Lett., 486: 185-190, 2000.
121. M. Charlet, S. Chernysh, H. Philippe, C. Hetru, J.A. Hoffmann, P. Bulet. Isolation of several cysteine-rich antimicrobial peptides from the blood of a mollusc, Myitlus edulis. Innate. Immun., 271: 21808-21813, 1996.
122. F. Hubert, T. Noël, P. Roch. A member of the arthropod defensin family from edible Mediterranean mussels (Mytilus galloprovincialis). Eur. J. Biochem., 240: 302-306, 1996.
123. G. Mitta, F. Hubert, T. Noël, P. Roch. Myticin, a novel cysteine-rich antimicrobial peptide isolated from haemocytes and plasma of the mussel Mytilus galloprovincialis. Eur. J. Biochem., 265: 71-78, 1999.
124. Y.-S. Yang, G. Mitta, A. Chavanieu, B. Calas, J.F. Sanchez, P. Roch, A. Aumelas. Solution 17 structure and activity of the synthetic four-disulfide bond Mediterranean mussel defensin (MGD-1). Biochemistry, 39: 14436-14447, 2000.
125. R.S. Anderson, A.E. Beaven. Antibacterial activities of oyster (Crassostrea virginica) and mussel (Mytilus edulis and Geukensia demissa) plasma. Aquat. Living Resour., 14: 343-349, 2001.
126. H. Meisel. Biochemical properties of bioactive peptides derived from milk proteins: potential nutraceuticals for food and pharmaceutical applications. Livestock Prod. Sci., 50: 125-138, 1997.
127. E. Lahov, W. Regelson. Antibacterial and immunostimulating casein-derived substances from milk: casecidin, isracidin peptides. Food Chem. Toxicol., 34: 131-145, 1996.
128. A. Pellegrini. Antimicrobial peptides from food proteins. Curr. Pharm. Des., 9: 1225-1238, 2003.
129. R.D. Hill, E. Lahav, D. Givol. A rennin-sensitive bond in alpha-s1 beta-casein. J. Dairy Res., 41: 147-153, 1974.
130. H.-D. Zucht, M. Raida, K. Adermann, H.-J. Mägert, W.-G. Forssmann. Casocidin-I: a casein-αs2 derived peptide exhibits antibacterial activity. FEBS Lett., 372: 185-188, 1995.
131. I. Recio, S. Visser. Identification of two distinct antibacterial domains within the sequence of bovine αs2-casein. Biochim. Biophys. Acta, 1428: 314-326, 1999.
132. M. Malkoski, S.G. Dashper, N.M. O'Brien-Simpson, G.H. Talbo, M. Macris, K.J. Cross, E.C. Reynolds. Kappacin, a novel antibacterial peptide from bovine milk. Antimicrob. Agents. Chemother., 45: 2309-2315, 2001.
133. G.H. Talbo, D. Suckau, M. Malkoski, E.C. Reynolds. MALDI-PSD-MS analysis of the phosphorylation sites of caseinomacropeptide. Peptides, 22: 1093-1098, 2001.
134. A. Pellegrini, C. Dettling, U. Thomas, P. Hunziker. Isolation and characterization of four bactericidal domains in the bovine β-lactoglobulin. Biochim. Biophys. Acta, 1526: 131-140, 2001.
135. A. Pellegrini, U. Thomas, N. Bramaz, P. Hunziker, R. von Fellenberg. Isolation and identification of three bactericidal domains in the bovine alpha-lactalbumin molecule. Biochim. Biophys. Acta, 1426: 439-448, 1999.
136. H. Wakabayashi, M. Takase, M. Tomita. Lactoferricin derived from milk protein lactoferrin. Curr. Pharm. Des., 9: 1277-1287, 2003.
137. M. Tomita, W. Bellamy, M. Takase, K. Yamauchi, H. Wakabayashi, K. Kawase. Potent antibacterial peptides generated by pepsin digestion of bovine lactoferrin. J. Dairy Sci., 74: 4137-4142, 1991.
138. P.M. Hwang, N. Zhou, X. Shan, C.H. Arrowsmith, H.J. Vogel. Three-dimensional solution structure of lactoferricin B, an antimicrobial peptide derived from bovine lactoferrin. Biochemistry, 37: 4288-4298, 1998.
139. R.T. Ellison, T.J. Giehl, F.M. LaForce. Damage of the outer membrane of enteric gram-negative bacteria by lactoferrin and transferrin. Infect. Immun., 56: 2774-2781, 1988.
140. K. Yamauchi, M. Tomita, T.J. Giehl, R.T. Ellison. Antibacterial activity of lactoferrin and a pepsin-derived lactoferrin peptide fragment. Infect. Immun., 61: 719-728, 1993.
141. W. Bellamy, M. Takase, H. Wakabayashi, K. Kawase, M. Tomita. Antibacterial spectrum of lacteferricin B, a potent bactericidal peptide derived from the N-terminal region of bovine lactoferrin. J. Appl. Bacteriol., 73: 472-479, 1992.
142. W. Bellamy, H. Wakabayashi, M. Takase, K. Kawase, S. Shimamura, M. Tomita. Killing of Candida albicans by lactoferricin B, a potent antimicrobial peptide derived from the N-terminal region of bovine lactoferrin. Med. Microbiol. Immunol., 182: 97-105, 1993. 21
143. H. Wakabayashi, S. Abe, S. Teraguchi, H. Hayasawa, H. Yamaguchi. Inhibition of hyphal growth of azole-resistant strains of Candida albicans by triazole antifun-gal agents in the presence of lactoferrin-related compounds. Antimicrob. Agents Chemother., 42: 1587-1591, 1998.
144. Y. Omata, M. Satake, R. Maeda, A. Saito, K. Shimazaki, K. Yamaguchi, Y. Uzuka, S. Tanabe, T. Sarashina, T. Mikami. Reduction of the infectivity of Toxoplasma gondii and Eimeria stiedae sporozoites by treatment with bovine lactoferricin. J. Vet. Med. Sci., 63: 187-190, 2001.
145. H.R. Ibrahim, S. Higashiguchi, L.R. Juneja, M. Kim, T. Yamamoto. A structural phase of heat-denatured lysozyme with novel antimicrobial action. J. Agric. Food Chem., 44: 1416-1423, 1996.
146. K. Düring, P. Porsch, A. Mahn, O. Brinkmann, W. Gieffers. The non-enzymatic microbicidal activity of lysozymes. FEBS Lett., 449: 93-100, 1999.
147. H.R. Ibrahim, T. Matsuzaki, T. Aoki. Genetic evidence that antibacterial activity of lysozyme is independent of its catalytic function. FEBS Lett., 506: 27-32, 2001.
148. H.R. Ibrahim, U. Thomas, A. Pellegrini. A helix-loop-helix peptide at the upper lip of the active site cleft of lysozyme confers potent antimicrobial activity with membrane permeabilization action. J. Biol. Chem., 276: 43767-43774, 2001.
149. A. Pellegrini, U. Thomas, N. Bramaz, P. Hunziker, R. von Fellenberg. Identification and isolation of a bactericidal domain in chicken egg white lysozyme. J. Appl. Microbiol., 82: 372-378, 1997.
150. A. Pellegrini, S. Schumacher, R. Stephan. In-vitro activity of various antimicrobial peptides developed from the bactericidal domains of lysozyme and beta-lactoglob-ulin with respect to Listeria monocytogenes, Escherichia coli O157, Salmonella spp. and Staphylococcus aureus. Arch. Lebensmittelhyg., 54: 34-36, 2003.
151. P. Valenti, G. Antonini, C. Von Hunolstein, P. Visca, N. Orsi, E. Antonini. Studies on the antimicrobial activity of ovotransferrin. Int. J. Tissue Reac., 5: 97-105, 1983.
152. H.R. Ibrahim, E. Iwamori, Y. Sugimoto, T. Aoki. Identification of a distinct antibacterial domain within the N-lobe of ovotransferrin. Biochim. Biophys. Acta, 1401: 289-303, 1998.
153. H.R. Ibrahim, Y. Sugimoto, T. Aoki. Ovotransferrin antimicrobial peptide (OTAP-92) kills bacteria through a membrane damage mechanism. Biochim. Biophys. Acta, 1523: 196-205, 2000.
154. O. McAuliffe, R.P. Ross, C. Hill. Lantibiotics: structure, biosynthesis and mode of action. FEMS Microbiol. Rev., 25: 285-308, 2001.
155. S. Garneau, N.I. Martin, J.C. Vederas. Two-peptide bacteriocins produced by lactic acid bacteria. Biochimie, 84: 577-592, 2002.
156. M.A. Riley, J.E. Wertz. Bacteriocin diversity: ecological and evolutionary perspectives. Biochimie, 84: 357-364, 2002.
157. J. Cleveland, T.J. Montville, I.F. Nes, M.L. Chikindas. Bacteriocins: safe, natural antimicrobials for food preservation. Int. J. Food Microbiol., 71: 1-20, 2001.
158. J.R. Tagg, A.S. Dajani, L.W. Wannamaker. Bacteriocins of Gram-positive bacteria. Microbiol. Rev., 40: 722-756, 1976.
159. T.R. Klaenhammer. Genetics of bacteriocins produced by lactic acid bacteria. FEMS Microbiol. Rev., 12: 39-86, 1993.
160. C. van Kraaij, W.M. de Vos, R.J. Siezen, O.P. Kuipers. Lantibiotics: biosynthesis, mode of action and applications. Natl. Prod. Rep., 16: 575-587, 1999.
161. J.C. Piard, O.P. Kuipers, H.S. Rollema, M.J. Desmazeuad, W.M. de Vos. Structure, organization and expression of the lct gene for lacticin 481, a novel lantibiotic produced by Lactococcus lactis. J. Biol. Chem., 268: 16361-16368, 1993.
162. M.J. van Belkum, M.E. Stiles. Nonlantibiotic antibacterial peptides from lactic acid bacteria. Natl. Prod. Rep., 17: 323-335, 2000.
163. J.T. Henderson, A.L. Chopko, P.D. van Wassenaar. Purification and primary structure of pediocin PA-1 produced by Pediococcus acidilactici PAC-1.0. Arch. Biochem. Biophys., 295: 5-12, 1992.
164. A.L. Holck, L. Axelsson, S. Birkeland, T. Aukrust, H. Blom. Purification and amino acid sequence of sakacin A, a bacteriocin from Lactobacillus sake Lb706. J. Gen. Microbiol., 138: 2715-2720, 1992.
165. T. Aymerich, H. Holo, L.S. Håvarstein, M. Hugas, M. Garriga, I.F. Nes. Biochemical and genetic characterization of enterocin A from Enterococcus fae-cium, a new antilisterial bacteriocin in the pediocin family of bacteriocins. Appl. Environ. Microbiol., 62: 1676-1682, 1996.
166. J. Nissen-Meyer, H. Holo, L.S. Håvarstein, K. Sletten, I.F. Nes. A novel lactococcal bacteriocin whose activity depends on the complementary action of two pep-tides. J. Bacteriol., 174: 5686-5692, 1992.
167. P.M. Muriana, T.R. Klaenhammer. Purification and partial characterization of lactacin F, a bacteriocin produced by Lactobacillus acidophilus 11088. Appl. Environ. Microbiol., 57: 114-121, 1991.
168. R.J. Leer, J.M.B.M. van der Vossen, M. van Giezen, J.M. van Noort, P.H. Pouwels. Genetic analysis of acidocin B, a novel bacteriocin produced by Lactobacillus acidophilus. Microbiology, 141: 1629-1635, 1995.
169. M.C. Joerger, T.R. Klaenhammer. Characterization and purification of helveticin J and evidence for a chromosomally determined bacteriocin produced by Lactobacillus heleveticus 481. J. Bacteriol., 167: 439-446, 1986.
170. J. Delves-Broughton, P. Blackburn, R.J. Evans, J. Hugenholtz. Applications of bacteriocin, nisin. Int. J. Gen. Mol. Microbiol., 69: 193-202, 1996.
171. E. Breukink, C. van Kraaij, R.A. Demel, R.J. Siezen, O.P. Kuipers, B.D. Kruijff. The C-terminal region of nisin is responsible for the initial interaction of nisin with the target membrane. Biochemistry, 36: 6968-6976, 1997.
172. H. Brötz, M. Josten, I. Wiedemann, U. Schneider, F. Götz, G. Bierbaum, H.-G. Sahl. Role of lipid-bound peptidoglycan precursors in the formation of pores by nisin, epidermin and other lantibiotics. Mol. Microbiol., 30: 317-327, 1998.
173. L. Lins, P. Ducarme, E. Breukink, R. Brasseur. Computational study of nisin interaction with model membrane. Biochim. Biophys. Acta, 1420: 111-120, 1999.
174. M.E.C. Bruno, A. Kaiser, T.J. Montville. Depletion of proton motive force by nisin in Listeria monocytogenes cells. Appl. Environ. Microbiol., 58: 2255-2259, 1992.
175. E. Breukink, B. de Kruijff. The lantibiotic nisin, a special case or not? Biochim. Biophys. Acta, 1462: 223-234, 1999.
176. L. Voland, H. Ulvatne, Ø. Rekdal, J. Svendsen. Initial binding sites of antimicrobial peptides in Staphylococcus aureus and Escherichia coli. Scand. J. Infect. Dis., 31: 467-473, 1999.
177. H. Ulvatne, H. Haukland, Ø. Olsvik, L. Vorland. Lactoferricin B causes depolarization of the cytoplasmic membrane of Escherichia coli ATCC 26922 and fusion of negatively charged liposomes. FEBS Lett., 492: 62-65, 2001.
178. Z. Oren, Y. Shai. Selective lysis of bacteria but not mammalian cells by diastereomers of melittin: structure-function study. Biochemistry, 36: 1826-1835, 1997.
179. Z. Oren, Y. Shai. Cyclization of a cytolytic amphipathic alpha-helical peptide and its diastereomer: effect on structure, interaction with model membranes, and biological function. Biochemistry, 39: 6103-6114, 2000.
180. A. Bera, S. Singh, R. Nagaraj, T. Vaidya. Induction of autophagic cell death in Leishmania donovani by antimicrobial peptides. Mol. Biochem. Parasitol., 127: 23-35, 2003.
181. H.W. Huang. Action of antimicrobial peptide: two-state model. Biochemistry, 39: 8347-8452, 2000.
182. Y. Shai, Z. Oren. From "carpet" mechanism to de-novo design diastereomeric cell-selective antimicrobial peptides. Peptides, 22: 1629-1641, 2001.
183. M. Cudic, L.J. Otvos. Intracellular targets of antibacterial peptides. Curr. Drug Targets, 3: 101-106, 2002.
184. H.G. Boman, B. Agerberth, A. Boman. Mechanisms of action on Escherichia coli of cecropin P1 and PR-39, two antibacterial peptides from pig intestine. Infect. Immun., 61: 2978-2984, 1993.
185. C.L. Friedrich, A. Rozek, A. Patrzykat, R.E. Hancock. Structure and mechanism of action of an indolicidin peptide derivative with improved activity against grampositive bacteria. J. Biol. Chem., 276: 24015-24022, 2001.
186. T.J. Falla, D.N. Karunaratne, R.E.W. Hancock. Mode of action of the antimicrobial peptide indolicidin. J. Biol. Chem., 271: 19298-19303, 1996.
187. C. Subbalakshmi, N. Krishnakumari, R. Nagaraj, N. Sitaram. Requirements for antibacterial and hemolytic activities in the bovine neutrophil derived 13-residue peptide indolicidin. FEBS Lett., 395: 48-52, 1996.
188. C. Subbalakshmi, N. Sitaram. Mechanism of antimicrobial action of indolicidin. FEMS Microbiol. Lett., 160: 91-96, 1998.
189. P.A. Charp, W.G. Rice, R.L. Raynor, E. Reimund, J.M. Kinkade, J.T. Ganz, M.E. Selsted, R.I. Lehrer, J.F. Kuo. Inhibition of protein kinase C by defensins, antibiotic peptides form human neutrophils. Biochem. Pharmacol., 37: 951-956, 1988.
190. A. Hobta, I. Lisovskiy, S. Mikhalap, D. Kolybo, S. Romanyuk, M. Soldatkina, N. Markeyeva, L. Garmanchouk, S.P. Sidorenko, P.V. Pogrebnoy. Epidermoid carcinoma-derived antimicrobial peptide (ECAP) inhibits phosphorylation by protein kinases in vitro. Cell Biochem. Funct., 19: 291-298, 2001.
191. A. Risso, M. Zanetti, R. Gennaro. Cytotoxicity and apoptosis mediated by two peptides of innate immunity. Cell Immunol., 189: 107-115, 1998.
192. G.H. Gudmundsson, B. Agerberth. Neutrophil antibacterial peptides, multifunctional effector molecules in the mammalian immune system. J. Immunol. Methods, 232: 45-54, 1999.
193. R.E.W. Hancock, G. Diamond. The role of cationic antimicrobial peptides in innate host defences. Trends Microbiol., 8: 402-410, 2000.
194. R.E. Hancock. Cationic peptides: effectors in innate immunity and novel antimicrobials. Lancet Infect. Dis., 1: 156-164, 2001.
195. M. Salzet. Antimicrobial peptides signaling molecules. Trends Immunol., 23: 283-284, 2002.
196. D. Yang, O. Chertov, J.J. Oppenheim. Participation of mammalian defensins and cathelicidins in anti-microbial immunity: receptors and activities of human defensins and cathelicidin (LL-37). J. Leukocyte Biol., 69: 691-697, 2001.
197. A.D. Befus, C. Mowat, M. Gilchrist, J. Hu, S. Solomon, A. Bateman. Neutrophil defensins induce histamine secretion from mast cells: mechanisms of action. J. Immunol., 163: 947-953, 1999.
198. A. Di Nardo, A. Vitiello, R.L. Gallo. Cutting edge: mast cell antimicrobial activity is mediated by expression of cathelicin antimicrobial peptide. J. Immunol., 170: 2274-2278, 2003.
199. S. Yomogida, I. Nagaoka, T. Yamashita. Comparative studies on the extracellular release and biological activity of guinea pig neutrophil cationic antibacterial polypeptide of 11 kDa (CAP11) and defensin. Comp. Biochem. Physiol. B. Biochem. Mol. Biol., 116: 99-107, 1997.
200. M. Zaiou, V. Nizet, R.L. Gallo. Antimicrobial and protease inhibitory functions of the human cathelicidin (hCAP18/LL-37) prosequence. J. Invest. Dermatol., 120: 810-816, 2003.
201. C.J. Murphy, B.A. Foster, M.J. Mannis, M.E. Selsted, T.W. Reid. Defensins are mitogenic for epithelial cells and fibroblasts. J. Cell Physiol., 155: 408-1-13, 1993.
202. R.L. Gallo, M. Ono, T. Povsic, C. Page, E. Eriksson, M. Klagsbrun, M. Bernfield. Syndecans, cell surface heparan sulfate proteoglycans, are induced by a proline-rich antimicrobial peptide from wounds. Prod. Natl. Acad. Sci. USA, 91: 11035-11039, 1994.
203. M. Frohm, B. Agerberth, G. Ahangari, M. Stahle-Backdahl, S. Liden, H. Wigzell, G.H. Gudmundsson. The expression of the gene coding for the antibacterial peptide LL-37 is induced in human keratinocytes during inflammatory disorders. J. Biol. Chem., 272: 15258-15263, 1997.
204. M. Frohm, H. Gunne, A.C. Bergman, B. Agerberth, T. Bergman, A. Boman, S. Liden, H. Jornvall, H.G. Boman. Biochemical and antibacterial analysis of human wound and blister fluid. Eur. J. Biochem., 237: 86-92, 1996.
205. O.E. Sørensen, J.B. Cowland, K. Theilgaard-Mönch, L. Liu, T. Ganz, N. Borregaard. Wound healing and expression of antimicrobial peptides/polypeptides in human ker-atinocytes, a consequence of common growth factors. J. Immunol., 170: 5583-5589, 2003.
206. A.G. Gao, S.M. Hakim, C.A. Mittanck, Y. Wu, B.M. Woerner, D.M. Stark, D.M. Shah, J. Liang, C.M. Rommens. Fungal pathogen protection in potato by expression of a plant defensin peptide. Nature Biotechnol., 18: 1307-1310, 2000.
207. V.G. Lebedev, S.V. Dolgov, N. Lavrova, V.G. Lunin, B.S. Naroditski. Plant-defensin genes introduction for improvement of pear phytopathogen resistance. Acta Hortic., 596: 167-172, 2002.
208. A. Chakrabarti, T.R. Ganapathi, P.K. Mukherjee, V.A. Bapat. Msl-99, a magainin analogue, impact enhanced disease resistance in transgenic tobacco and banana. Planta, 216: 587-596, 2003.
209. O.S. Lee, B. Lee, N. Park, J.C. Koo, Y.H. Kim, T. Prasad, C. Karigar, H.J. Chun, B.R. Jeong, D.H. Kim, J. Nam, J.-G. Yun, S.-S. Kwak, M.J. Cho, D.-J. Yun. Pn-AMPs, the hevein-like proteins from Pharbitis nil confers disease resistance against phytopathogenic fungi in tomato, Lycopersicum esculentum. Phytochemistry, 62:1073-1079, 2003.
210. N. Banzet, M.-P. Latorse, P. Bulet, E. François, C. Derpierre, M. Dubald. Expression of insect cysteine-rich antifungal peptides in transgenic tobacco enhances resistance to a fungal disease. Plant Sci., 162: 995-1006, 2002.
211. D. Ponti, M. Luisa Mangoni, G. Mignogna, M. Simmaco, D. Barra. An amphibian antimicrobial peptide variant expressed in Nicotiana tabacum confers resistance to phytopathogens. Biochem. J., 370: 121-127, 2003.
212. S. Holtorf, K. Apel, H. Bohlmann. Specific and different expression patterns of two members of the leaf thionin multigene family of barley in transgenic tobacco. Plant Sci., 111: 27-37, 1995.
213. M.J. Carmona, A. Molina, J.A. Fernandez, J.J. Lopez-Fando, F. García-Olmedo. Expression of the alpha-thionin from barley in tobacco confers enhanced resistance to bacterial pathogens. Plant J., 3: 457-462, 1993.
214. M.F.C. De Bolle, R.W. Osborn, I.J. Goderis, L. Noe, D. Acland, C.A. Hart, S. Torrekens, F. Van Leuven, W.F. Broekaert. Antimicrobial peptides from Mirabilis jalapa and Amaranthus caudatus: expression, processing, localization and biological activity in transgenic tobacco. Plant Mol. Biol., 31: 993-1008, 1996.
215. F.-M. Lai, C. DeLong, K. Mei, T. Wignes, P.R. Fobert. Analysis of the DRR230 family of pea defensins: gene expression pattern and evidence of broad host-range antifungal activity. Plant Sci., 163: 855-864, 2002.
216. N.P. Everett. Design of antifungal peptides for agricultural applications. ACS Symp. Ser., 551: 278-291, 1994.
217. L.D. Owens, T.M. Heutte. A single amino acid substitution in the antimicrobial defense protein cecropin B is associated with diminished degradation by leaf intercellular fluid. Mol. Plant-Microbe Interact., 10: 525-528, 1997.
218. J.W. Cary, K. Rajasekaran, J.M. Jaynes, T.E. Cleveland. Transgenic expression of a gene encoding a synthetic antimicrobial peptide result in inhibition of fungal growth in vitro and in planta. Plant Sci., 154: 171-181, 2000.
219. M. Osusky, G. Zhou, L. Osuska, R.E. Hancock, W.W. Kay, S. Misra. Trangenic plants expressing cationic peptide chimeras exhibit broad-spectrum resistance to phytopathogens. Nat. Biotechnol., 18: 1162-1166, 2000.
220. C.N. Cutter, G.R. Siragusa. Population reductions of Gram negative pathogens following treatments with nisin and chelators under various conditions. J. Food Prot., 58: 977-983, 1995.
221. C.N. Cutter, G.R. Siragusa. Treatments with nisin and chelators to reduce Salmonella and Escherichia coli on beef. J. Food Prot., 58: 1028-1030, 1995.
222. G.A. Dykes, S.M. Moorhead. Combined antimicrobial effect of nisin and a liste-riophage against Listeria monocytogenes in broth but not in buffer or on raw beef. Int. J. Food Microbiol., 73: 71-81, 2002.
223. W. Chung, R.E.W. Hancock. Action of lysozyme and nisin mixtures against lactic acid bacteria. Int. J. Food Microbiol., 60: 25-32, 2000.
224. M.J. Facon, B.J. Skura. Antibacterial activity of lactoferrin, lysozyme and EDTA against Salmonella enteritidis. Int. Dairy J., 6: 303-313, 1996.
225. P. Chantaysakorn, R.L. Richter. Antimicrobial properties of pepsin-digested lactofer-rin added carrot juice and filtrates of carrot juice. J. Food Prot., 63: 376-380, 2000.
226. F.M. Nattress, C.K. Yost, L.P. Baker. Evaluation of the ability of lysozyme and nisin to control meat spoilage bacteria. Int. J. Food Microbiol., 70: 111-119, 2001.
227. T. Ariyapitipun, A. Mustapha, A.D. Clarke. Microbial shelf life determination of vacuum-packaged fresh beef treated with polylactic acid, lactic acid, and nisin solutions. J. Food Prot., 62: 913-920, 1999.
228. T. Ariyapitipun, A. Mustapha, A.D. Clarke. Survival of Listeria monocytogenes Scott A on vacuum-packaged raw beef treated with polylactic acid, lactic acid, and nisin. J. Food Prot., 63: 131-136, 2000.
229. M.L. Cabo, M.A. Murado, M.P. Gonzalez, L. Pastoriza. Dose-response relationships. A model for describing interactions, and its application to the combined effect of nisin and lactic acid on Leuconostoc mesenteroides. J. Appl. Microbiol., 88: 756-763, 2000.
230. S. Zhang, A. Mustapha. Reduction of Listeria monosytogenes and Escherichia coli O157:H7 numbers on vacuum-packaged fresh beef treated with nisin or nisin combined with EDTA. J. Food Prot., 62: 1123-1127, 1999.
231. L. Nilsson, Y. Chen, M.L. Chikindas, H.H. Huss, L. Gram, T.J. Montville. Carbon dioxide and nisin act synergistically on Listeria monocytogenes. Appl. Environ. Microbiol., 66: 769-774, 2000.
232. C.N. Cutter, G.R. Siragusa. Reductions of Listeria innocua and Brochothrix thermosphacta on beef following nisin spray treatments and vacuum packaging. Food Microbiol., 13: 23-33, 1996.
233. C.N. Cutter, G.R. Siragusa. Reduction of Brochothrix rheumosphacta on beef surfaces following immobilization of nisin in calcium alginate gels. Lett. Appl. Microbiol., 23: 9-12, 1996.
234. C.N. Cutter, G.R. Siragusa. Growth of Brochothrix thermosphacta in ground beef following treatment with nisin in calcium alginate gels. Food Microbiol., 14: 425-430, 1997.
235. C.N. Cutter, G.R. Siragusa. Incorporation of nisin into a meat binding system to inhibit bacteria on beef surfaces. Lett. Appl. Microbiol., 27: 19-23, 1998.
236. P.L. Dawson, I.Y. Han, T.R. Padgett. Effect of lauric acid on nisin activity in edible protein packaging films. Poult. Sci., 76 (S): 74, 1997.
237. T. Padgett, I.Y. Han, P.L. Dawson. Incorporation of food-grade antimicrobial compounds into biodegradable packaging films. J. Food Prot., 61: 1330-1335, 1998.
238. G.R. Siragusa, C.N. Cutter, J.L. Willett. Incorporation of bacteriocin in plastic retains activity and inhibits surface growth of bacteria on meat. Food Microbiol., 16: 229-235, 1999.
239. C.N. Cutter, J.L. Willett, G.R. Siragusa. Improved antimicrobial activity of nisin-incorporated polymer films by formulation change and addition of food grade chelator. Lett. Appl. Microbiol., 33: 325-328, 2001.
240. F.M. Nattress, L.P. Baker. Effects of treatment with lysozyme and nisin on the microflora and sensory properties of commercial pork. Int. J. Food Microbiol., 85: 259-267, 2003.
241. R.E.W. Hancock, R.I. Lehrer. Cationic peptides: a new source of antibiotics. Trends Biotechnol., 16: 82-88, 1998.
242. T. Gura. Innate immnunity: ancient system gets new respect. Science, 291: 2068-2070, 2001.
243. A.R. Koczulla, R. Bals. Antimicrobial peptides: current status and therapeutic potential. Drugs, 63: 389-406, 2003.
244. M. Gough, R.E. Hancock, N.M. Kelly. Antiendotoxin activity of cationic peptide antimicrobial agents. Infect. Immun., 64: 4922-4927, 1996.
245. I. Ahmad, W.R. Perkins, D.M. Lupan, M.E. Selsted, A.S. Janoff. Liposomal entrapment of the neutrophil-derived peptide indolicidin endows it with in vivo antifungal activity. Biochim. Biophys. Acta, 1237: 109-114, 1995.
246. D.A. Steinberg, M.A. Hurst, C.A. Fujii, A.H. Kung, J.F. Ho, F.C. Cheng, D.J. Loury, J.C. Fiddes. Protegrin-1: a broad-spectrum, rapidly microbicidal peptide with in vivo activity. Antimicrob. Agents Chemother., 41: 1738-1742, 1997.
247. T. Kirikae, M. Hirata, H. Yamasu, F. Kirikae, H. Tamura, F. Kayama, K. Nakatsuka, T. Yokochi, M. Nakano. Protective effects of a human 18-kilodalton cationic antimicrobial protein (CAP18)-derived peptide against murine endotoxemia. Infect. Immun., 66: 1861-1868, 1998.
248. A. Giacometti, O. Cirioni, R. Ghiselli, F. Mocchegiani, M.S. Del Prete, C. Viticchi, W. Kamysz, E. Lempicka, V. Saba, G. Scalise. Potential therapeutic role of cationic peptides in three experimental models of septic shock. Antimicrob. Agents Chemother., 46: 2132-2136, 2002.
249. D. Loury, J.R. Embree, D.A. Steinberg, S.T. Sonis, J.C. Fiddes. Effect of local application of the antimicrobial peptide IB-367 on the incidence and severity of oral mucositis in hamsters. Oral Surg. Oral Med. Oral Pathol. Oral Radiol. Endod., 87: 544-551, 1999.
250. A. Giacometti, O. Cirioni, R. Ghiselli, F. Mocchegiani, G. D'Amato, M.S. Del Prete, F. Orlando, W. Kamysz, J. Lukasiak, V. Saba, G. Scalise. Adminstration of protegrin peptide IB-367 to prevent endotoxin induced mortality in bile duct ligated rats. Gut, 52: 874-878, 2003.
251. Y. Ge, D.L. MacDonald, K.J. Holroyd, C. Thornsberry, H. Wexler, M. Zasloff. In vitro antibacterial properties of pexiganan, an analog of magainin. Antimicrob. Agents Chemother., 43: 782-788, 1999.
252. M. Cazzola, A. Sanduzzi, M.G. Matera. Novelties in the field of antimicrobial compounds for the treatment of lower respiratory tract infections. Pulm. Pharmacol. Ther., 16: 131-145, 2003.
253. D.A. Mosca, M.A. Hurst, W. So, B.S.C. Viajar, C.A. Fujii, T.J. Falla. IB-367, a protegrin peptide with in vitro and in vivo activities against the microflora associated with oral mucositis. Antimicrob. Agents Chemother., 44: 1803-1808, 2000.