Antimicrobial peptides (AMPs): Ancient compounds that represent novel weapons in the fight against bacteria

Biochemical Pharmacology

Volumn 133, Issue , 2017, Pages 117-138

  Ageitos, J M ^a   Sanchez Perez A ^b   Calo Mata, P ^a   Villa, T G ^a  

^a UNIVERSITY OF SANTIAGO DE COMPOSTELA   (Spain)

^b UNIVERSITY OF SYDNEY   (Australia)

Author keywords

Antimicrobial peptides; Cathelicidins; Defensins; Gram negative; Gram positive

Indexed keywords

BETA DEFENSIN; CATHELICIDIN; FUNGAL PROTEIN; HEPCIDIN; PISCIDIN DERIVATIVE; PLANT PROTEIN; POLYPEPTIDE ANTIBIOTIC AGENT; SYNTHETIC PEPTIDE; THETA DEFENSIN; UNCLASSIFIED DRUG; ANTIMICROBIAL CATIONIC PEPTIDE; BIOLOGICAL PRODUCT;

ALTERNATIVE MEDICINE; AMPHIBIA; ANTIBACTERIAL ACTIVITY; ARTHROPOD; BACTERICIDAL ACTIVITY; BIRD; CNIDARIA; ECCRINE GLAND; FISH; HUMAN; LIVER; MAMMAL; MOLLUSC; NONHUMAN; PRIORITY JOURNAL; REPTILE; REVIEW; SPONGE (PORIFERA); AMINO ACID SEQUENCE; ANIMAL; CELL WALL; CHEMISTRY; DRUG EFFECTS; GENETICS; METHICILLIN RESISTANT STAPHYLOCOCCUS AUREUS; MICROBIAL SENSITIVITY TEST; MULTIDRUG RESISTANCE; PHYSIOLOGY; PROCEDURES; PROTEIN SECONDARY STRUCTURE;

AMINO ACID SEQUENCE; ANIMALS; ANTIMICROBIAL CATIONIC PEPTIDES; BIOLOGICAL PRODUCTS; CELL WALL; DRUG RESISTANCE, MULTIPLE, BACTERIAL; HUMANS; METHICILLIN-RESISTANT STAPHYLOCOCCUS AUREUS; MICROBIAL SENSITIVITY TESTS; PROTEIN STRUCTURE, SECONDARY;

EID: 84995766783     PISSN: 00062952     EISSN: 18732968     Source Type: Journal    
DOI: 10.1016/j.bcp.2016.09.018     Document Type: Review

References (301)

1. [1] Wang, G., Li, X., Wang, Z., APD3: the antimicrobial peptide database as a tool for research and education. Nucleic Acids Res. 44 (2015), D1087–D1093, 10.1093/nar/gkv1278.
2. [2] Waghu, F.H., Barai, R.S., Gurung, P., Idicula-Thomas, S., CAMP R3: a database on sequences, structures and signatures of antimicrobial peptides. Nucleic Acids Res., 44, 2015, gkv1051, 10.1093/nar/gkv1051.
3. [3] Zhao, X., Wu, H., Lu, H., Li, G., Huang, Q., LAMP: a database linking antimicrobial peptides. PLoS One, 8, 2013, e66557, 10.1371/journal.pone.0066557.
4. [4] Boman, H.G., Peptide antibiotics and their role in innate immunity. Annu. Rev. Immunol. 13 (1995), 61–92, 10.1146/annurev.iy.13.040195.000425.
5. [5] Epand, R.M., Vogel, H.J., Diversity of antimicrobial peptides and their mechanisms of action. Biochim. Biophys. Acta 1462 (1999), 11–28, 10.1016/S0005-2736(99)00198-4.
6. [6] Hancock, R.E., Cationic peptides: effectors in innate immunity and novel antimicrobials. Lancet Infect. Dis. 1 (2001), 156–164, 10.1016/S1473-3099(01)00092-5.
7. [7] Lai, Y., Villaruz, A.E., Li, M., Cha, D.J., Sturdevant, D.E., Otto, M., The human anionic antimicrobial peptide dermcidin induces proteolytic defence mechanisms in staphylococci. Mol. Microbiol. 63 (2007), 497–506, 10.1111/j.1365-2958.2006.05540.x.
8. [8] Cherkasov, A., Hilpert, K., Jenssen, H., Fjell, C.D., Waldbrook, M., Mullaly, S.C., et al. Use of artificial intelligence in the design of small peptide antibiotics effective against a broad spectrum of highly antibiotic-resistant superbugs. ACS Chem. Biol. 4 (2009), 65–74, 10.1021/cb800240j.
9. [9] Wade, D., Boman, A., Wåhlin, B., Drain, C.M., Andreu, D., Boman, H.G., et al. All-D amino acid-containing channel-forming antibiotic peptides. Proc. Natl. Acad. Sci. U.S.A. 87 (1990), 4761–4765, 10.1073/pnas.87.12.4761.
10. [10] Kamysz, W., Okrój, M., Łukasiak, J., Novel properties of antimicrobial peptides. Acta Biochim. Pol. 50 (2003), 461–469 035002461.
11. [11] Dubos, R.J., Studies on a bactericidal agent extracted from a soil bacillus: I. Preparation of the agent. Its activity in vitro. J. Exp. Med. 70 (1939), 1–10.
12. [12] Stauss-Grabo, M., Atiye, S., Le, T., Kretschmar, M., Decade-long use of the antimicrobial peptide combination tyrothricin does not pose a major risk of acquired resistance with gram-positive bacteria and Candida spp. Pharmazie 69 (2014), 838–841, 10.1691/ph.2014.4686.
13. [13] Izadpanah, A., Gallo, R.L., Antimicrobial peptides. J. Am. Acad. Dermatol. 52 (2005), 381–390, 10.1016/j.jaad.2004.08.026 quiz 391–392.
14. [14] Knutson, M.D., Oukka, M., Koss, L.M., Aydemir, F., Wessling-Resnick, M., Iron release from macrophages after erythrophagocytosis is up-regulated by ferroportin 1 overexpression and down-regulated by hepcidin. Proc. Natl. Acad. Sci. U.S.A. 102 (2005), 1324–1328, 10.1073/pnas.0409409102.
15. [15] Thomsen, L.E., Gottlieb, C.T., Gottschalk, S., Wodskou, T.T., Kristensen, H.-H., Gram, L., et al. The heme sensing response regulator HssR in Staphylococcus aureus but not the homologous RR23 in Listeria monocytogenes modulates susceptibility to the antimicrobial peptide plectasin. BMC Microbiol., 10, 2010, 307, 10.1186/1471-2180-10-307.
16. [16] Hotchkiss, R.D., Dubos, R.J., Beam, D.O.N.T., Up, M.E., Toshach, J.C., Fractionation of the bactericidal agent from cultures of a soil Bacillus. J. Biol. Chem. 132 (1940), 791–792, 10.1111/j.1365-2125.2007.02971.x.
17. [17] Townsley, L.E., Tucker, W.A., Sham, S., Hinton, J.F., Structures of gramicidins A, B, and C incorporated into sodium dodecyl sulfate micelles. Biochemistry 40 (2001), 11676–11686, 10.1021/bi010942w.
18. [18] Kelkar, D.A., Chattopadhyay, A., The gramicidin ion channel: a model membrane protein. Biochim. Biophys. Acta 1768 (2007), 2011–2025, 10.1016/j.bbamem.2007.05.011.
19. [19] Ruckdeschel, G., Beaufort, F., Nahler, G., Belzer, O., In vitro antibacterial activity of gramicidin and tyrothricin. Arzneimittelforschung 33 (1983), 1620–1622.
20. [20] Tamaki, M., Akabori, S., Muramatsu, I., Properties of synthetic analogs of gramicidin S containing L-serine or L-glutamic acid residue in place of L-ornithine residue. Int. J. Pept. Protein Res. 47 (2009), 369–375, 10.1111/j.1399-3011.1996.tb01086.x.
21. [21] Kondejewski, L.H., Farmer, S.W., Wishart, D.S., Kay, C.M., Hancock, R.E.W., Hodges, R.S., Modulation of structure and antibacterial and hemolytic activity by ring size in cyclic gramicidin S analogs. J. Biol. Chem. 271 (1996), 25261–25268, 10.1074/jbc.271.41.25261.
22. [22] Mogi, T., Ui, H., Shiomi, K., Omura, S., Kita, K., Gramicidin S identified as a potent inhibitor for cytochrome bd-type quinol oxidase. FEBS Lett. 582 (2008), 2299–2302, 10.1016/j.febslet.2008.05.031.
23. [23] Tang, X.J., Thibault, P., Boyd, R.K., Characterisation of the tyrocidine and gramicidin fractions of the tyrothricin complex from Bacillus brevis using liquid chromatography and mass spectrometry. Int. J. Mass Spectrom. Ion Process. 122 (1992), 153–179, 10.1016/0168-1176(92)87015-7.
24. [24] Bahar, A.A., Ren, D., Antimicrobial peptides. Pharmaceuticals (Basel) 6 (2013), 1543–1575, 10.3390/ph6121543.
25. [25] Dubos, R.J., Hotchkiss, R.D., The production of bactericidal substances by aerobic sporulating Bacilli. J. Exp. Med., 629–640, 1941.
26. [26] Tareq, F.S., Lee, M.A., Lee, H., Lee, Y., Lee, J.S., Hasan, C.M., et al. Gageotetrins A−C, noncytotoxic antimicrobial linear lipopeptides from a marine bacterium Bacillus subtilis. Org. Lett. 16 (2014), 13–16.
27. [27] Hilpert, K., McLeod, B., Yu, J., Elliott, M.R., Rautenbach, M., Ruden, S., et al. Short cationic antimicrobial peptides interact with ATP. Antimicrob. Agents Chemother. 54 (2010), 4480–4483 http://aac.asm.org/content/54/10/4480.short.
28. [28] Orwa, J.A., Govaerts, C., Busson, R., Roets, E., Van Schepdael, A., Hoogmartens, J., Isolation and structural characterization of polymyxin B components. J. Chromatogr. A 912 (2001), 369–373, 10.1016/S0021-9673(01)00585-4.
29. [29] Koyama, Y., Kurosawa, A., Tsuchiya, A., Takakuta, K., A new antibiotic, colistin, produced by spore-forming soil bacteria. J. Antibiot. (Tokyo) 3 (1950), 457–458.
30. [30] Falagas, M.E., Kasiakou, S.K., Saravolatz, L.D., Colistin: the revival of polymyxins for the management of multidrug-resistant Gram-negative bacterial infections. Clin. Infect. Dis. 40 (2005), 1333–1341, 10.1086/429323.
31. [31] Roberts, K.D., Azad, M.A.K., Wang, J., Horne, A.S., Thompson, P.E., Nation, R.L., et al. Antimicrobial activity and toxicity of the major lipopeptide components of polymyxin B and colistin: last-line antibiotics against multidrug-resistant Gram-negative bacteria. ACS Infect. Dis. 1 (2015), 568–575, 10.1021/acsinfecdis.5b00085.
32. [32] Johnson, B.A., Anker, H., Meleney, F.L., Bacitracin: a new antibiotic produced by a member of the B. subtilis group. Science 102 (1945), 376–377, 10.1126/science.102.2650.376.
33. [33] Ming, L., Epperson, J.D., Metal binding and structure–activity relationship of the metalloantibiotic peptide bacitracin. J. Inorg. Biochem. 91 (2002), 46–58.
34. [34] Ikai, Y., Oka, H., Hayakawa, J., Matsumoto, M., Saito, M., Harada, K.-I., et al. Total structures and antimicrobial activity of bacitracin minor components. J. Antibiot. (Tokyo) 48 (1995), 233–242, 10.7164/antibiotics.48.233.
35. [35] Shiba, T., Wakamiya, T., Fukase, K., Ueki, Y., Teshima, T., Nishikawa, M., Structure of the lanthionine peptides nisin, ancovenin and lanthipeptin. Jung, G., Sahl, H.-G., (eds.) Nisin Nov. Lantibiotics, 1991, ESCOM Science Publisher B.V., Leiden, 113–122.
36. [36] Bierbaum, G., Sahl, H.-G., Lantibiotics: mode of action, biosynthesis and bioengineering. Curr. Pharm. Biotechnol. 10 (2009), 2–18, 10.2174/138920109787048616.
37. [37] Rogers, L.A., The inhibiting effect of Streptococcus lactis on Lactobacillus bulgaricus. J. Bacteriol. 16 (1928), 321–325.
38. [38] Hansen, J.N., Sandine, W.E., Nisin as a model food preservative. Crit. Rev. Food Sci. Nutr. 34 (1994), 69–93, 10.1080/10408399409527650.
39. [39] Rodriguez, J.M., Review: antimicrobial spectrum, structure, properties and mode of action of nisin, a bacteriocin produced by Lactococcus lactis. Food Sci. Technol. Int. 2 (1996), 61–68.
40. [40] Chatterjee, C., Paul, M., Xie, L., van der Donk, W.A., Biosynthesis and mode of action of lantibiotics. Chem. Rev. 105 (2005), 633–683, 10.1021/cr030105v.
41. [41] Duquesne, S., Destoumieux-Garzón, D., Microcins, gene-encoded antibacterial peptides from enterobacteria. Nat. Prod. Rep., 24, 2007, 75005, 10.1039/b516237h.
42. [42] Duquesne, S., Petit, V., Peduzzi, J., Rebuffat, S., Structural and functional diversity of microcins, gene-encoded antibacterial peptides from enterobacteria. J. Mol. Microbiol. Biotechnol. 13 (2007), 200–209, 10.1159/000104748.
43. [43] Salomón, R.A., Farías, R.N., Microcin 25, a novel antimicrobial peptide produced by Escherichia coli. J. Bacteriol. 174 (1992), 7428–7435.
44. [44] Bellomio, A., Vincent, P.A., De Arcuri, B.F., Farias, R.N., Morero, R.D., Microcin J25 has dual and independent mechanisms of action in Escherichia coli: RNA polymerase inhibition and increased superoxide production. J. Bacteriol. 189 (2007), 4180–4186, 10.1128/JB.00206-07.
45. [45] Novikova, M., Metlitskaya, A., Datsenko, K., Kazakov, T., Kazakov, A., Wanner, B., et al. The Escherichia coli Yej transporter is required for the uptake of translation inhibitor microcin C. J. Bacteriol. 189 (2007), 8361–8365, 10.1128/JB.01028-07.
46. [46] Metlitskaya, A., Kazakov, T., Kommer, A., Pavlova, O., Praetorius-Ibba, M., Ibba, M., et al. Aspartyl-tRNA synthetase is the target of peptide nucleotide antibiotic microcin C. J. Biol. Chem. 281 (2006), 18033–18042, 10.1074/jbc.M513174200.
47. [47] Roush, R.F., Nolan, E.M., Löhr, F., Walsh, C.T., Maturation of an Escherichia coli ribosomal peptide antibiotic by ATP-consuming N-P bond formation in microcin C7. J. Am. Chem. Soc. 130 (2008), 3603–3609, 10.1021/ja7101949.
48. [48] Vizán, J.L., Hernández-Chico, C., del Castillo, I., Moreno, F., The peptide antibiotic microcin B17 induces double-strand cleavage of DNA mediated by E. coli DNA gyrase. EMBO J. 10 (1991), 467–476.
49. [49] Herrero, M., Moreno, F., Microcin B17 blocks DNA replication and induces the SOS system in Escherichia coli. J. Gen. Microbiol. 132 (1986), 393–402, 10.1099/00221287-132-2-393.
50. [50] Leitgeb, B., Szekeres, A., Manczinger, L., Vágvölgyi, C., Kredics, L., The history of alamethicin: a review of the most extensively studied peptaibol. Chem. Biodivers. 4 (2007), 1027–1051, 10.1002/cbdv.200790095.
51. [51] Meyer, C.E., Reusser, F., A polypeptide antibacterial agent isolated from Trichoderma viride. Experientia 23 (1967), 85–86, 10.1007/BF02135929.
52. [52] De Zotti, M., Biondi, B., Formaggio, F., Toniolo, C., Stella, L., Park, Y., et al. Trichogin GA IV: an antibacterial and protease-resistant peptide. J. Pept. Sci. 15 (2009), 615–619, 10.1002/psc.1135.
53. [53] Rebuffat, S., Prigent, Y., Auvin-Guette, C., Bodo, B., Tricholongins BI and BII, 19 residue peptaibols from Trichoderma longibrachiatum solution structure from two-dimensional NMR spectroscopy. Eur. J. Biochem. 201 (1991), 661–674.
54. [54] Rebuffat, S., Conraux, L., Massias, M., Auvinguette, C., Bodo, B., Sequence and solution conformation of the 20-residue peptaibols, saturnisporins Sa-Ii and Sa-Iv. Int. J. Pept. Protein Res. 41 (1993), 74–84.
55. [55] Bradley, W.A., Somkuti, G.A., The primary structure of sillucin and antimicrobial peptide from Mucor pusillus. FEBS Lett. 97 (1979), 81–83, 10.1016/0014-5793(79)80057-5.
56. [56] Zhu, S., Gao, B., Harvey, P.J., Craik, D.J., Dermatophytic defensin with antiinfective potential. Proc. Natl. Acad. Sci. U.S.A. 109 (2012), 8495–8500, 10.1073/pnas.1201263109.
57. [57] Schneider, T., Kruse, T., Wimmer, R., Wiedemann, I., Sass, V., Pag, U., et al. Plectasin, a fungal defensin, targets the bacterial cell wall precursor lipid II. Science 80:328 (2010), 1168–1172, 10.1126/science.1185723.
58. [58] Mygind, P.H., Fischer, R.L., Schnorr, K.M., Hansen, M.T., Sönksen, C.P., Ludvigsen, S., et al. Plectasin is a peptide antibiotic with therapeutic potential from a saprophytic fungus. Nature 437 (2005), 975–980, 10.1038/nature04051.
59. [59] Essig, A., Hofmann, D., Münch, D., Gayathri, S., Künzler, M., Kallio, P.T., et al. Copsin, a novel peptide-based fungal antibiotic interfering with the peptidoglycan synthesis. J. Biol. Chem. 289 (2014), 34953–34964, 10.1074/jbc.M114.599878.
60. [60] Fernandez de Caleya, R., Gonzalez-Pascual, B., García-Olmedo, F., Carbonero, P., Susceptibility of phytopathogenic bacteria to wheat purothionins in vitro. Appl. Microbiol. 23 (1972), 998–1000.
61. [61] Nawrot, R., Barylski, J., Nowicki, G., Broniarczyk, J., Buchwald, W., Goździcka-Józefiak, A., Plant antimicrobial peptides. Folia Microbiol. (Praha) 59 (2014), 181–196, 10.1007/s12223-013-0280-4.
62. [62] López-Solanilla, E., González-Zorn, B., Novella, S., Vázquez-Boland, J.A., Rodríguez-Palenzuela, P., Susceptibility of Listeria monocytogenes to antimicrobial peptides. FEMS Microbiol. Lett. 226 (2003), 101–105, 10.1016/S0378-1097(03)00579-2.
63. [63] Day, L., Bhandari, D.G., Greenwell, P., Leonard, S.A., Schofield, J.D., Characterization of wheat puroindoline proteins. FEBS J. 273 (2006), 5358–5373, 10.1111/j.1742-4658.2006.05528.x.
64. [64] Dhatwalia, V.K., Sati, O.P., Tripathi, M.K., Kumar, A., Isolation, characterization and antimicrobial activity at diverse dilution of wheat puroindoline protein. World J. Agric. Sci. 5 (2009), 297–300.
65. [65] Vriens, K., Cammue, B., Thevissen, K., Antifungal plant defensins: mechanisms of action and production. Molecules 19 (2014), 12280–12303, 10.3390/molecules190812280.
66. [66] Osborn, R.W., De Samblanx, G.W., Thevissen, K., Goderis, I., Torrekens, S., Van Leuven, F., et al. Isolation and characterisation of plant defensins from seeds of Asteraceae, Fabaceae, Hippocastanaceae and Saxifragaceae. FEBS Lett. 368 (1995), 257–262, 10.1016/0014-5793(95)00666-W.
67. [67] Segura, A., Moreno, M., Madueño, F., Molina, A., García-Olmedo, F., Snakin-1, a peptide from potato that is active against plant pathogens. Mol. Plant Microbe Interact. 12 (1999), 16–23, 10.1094/MPMI.1999.12.1.16.
68. [68] Craik, D.J., Daly, N.L., Bond, T., Waine, C., Plant cyclotides: a unique family of cyclic and knotted proteins that defines the cyclic cystine knot structural motif. J. Mol. Biol. 294 (1999), 1327–1336, 10.1006/jmbi.1999.3383.
69. [69] Craik, D.D.J., Cemazar, M., Wang, C.C.K.L., Daly, N.N.L., The cyclotide family of circular miniproteins: nature's combinatorial peptide template. Biopolymers 84 (2006), 250–266, 10.1002/bip.
70. [70] Craik, D.J., Host-defense activities of cyclotides. Toxins (Basel) 4 (2012), 139–156, 10.3390/toxins4020139.
71. [71] Nawae, W., Hannongbua, S., Ruengjitchatchawalya, M., Defining the membrane disruption mechanism of kalata B1 via coarse-grained molecular dynamics simulations. Sci. Rep., 4, 2014, 3933, 10.1038/srep03933.
72. [72] Tam, J.P., Lu, Y.A., Yang, J.L., Chiu, K.W., An unusual structural motif of antimicrobial peptides containing end-to-end macrocycle and cystine-knot disulfides. Proc. Natl. Acad. Sci. U.S.A. 96 (1999), 8913–8918, 10.1073/pnas.96.16.8913.
73. [73] Witherup, K.M., Bogusky, M.J., Anderson, P.S., Ramjit, H., Ransom, R.W., Wood, T., et al. Cyclopsychotride-a, a biologically-active, 31-residue cyclic peptide isolated from Psychotria longipes. J. Nat. Prod. 57 (1994), 1619–1625, 10.1021/Np50114a002.
74. [74] Berlinck, R.G.S., Kossuga, M.H., Guanidine alkaloids from marine invertebrates. Fattorusso, E., Taglialatela-Scafati, O., (eds.) Mod. Alkaloids Struct. Isol. Synth. Biol, 2007, Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim, Germany, 305–337, 10.1002/9783527621071.ch11.
75. [75] Matsunaga, S., Fusetani, N., Konosu, S., Bioactive marine metabolites VI. Structure elucidation of discodermin a, an antimicrobial peptide from the marine sponge Discodermia kiiensis. Tetrahedron Lett. 25 (1984), 5165–5168, 10.1016/S0040-4039(01)81553-7.
76. [76] Fusetani, N., Antifungal peptides in marine invertebrates. Invert. Surviv. J. 7 (2010), 53–66 http://www.isj.unimo.it/articoli/ISJ199.pdf.
77. [77] Matsunaga, S., Fusetani, N., Konosu, S., Amino acid composition of discodermin A, an antimicrobial peptide, from the marine sponge Discodermia kiiensis. J. Nat. Prod. 48 (1985), 236–241.
78. [78] Gulavita, N.K., Gunasekera, S.P., Pomponi, S.A., Robinson, E.V., Polydiscamide A: a new bioactive depsipeptide from the marine sponge Discodermia sp. J. Org. Chem. 57 (1992), 1767–1772, 10.1021/jo00032a031.
79. [79] Ovchinnikova, T.V., Balandin, S.V., Aleshina, G.M., Tagaev, A.A., Leonova, Y.F., Krasnodembsky, E.D., et al. Aurelin, a novel antimicrobial peptide from jellyfish Aurelia aurita with structural features of defensins and channel-blocking toxins. Biochem. Biophys. Res. Commun. 348 (2006), 514–523, 10.1016/j.bbrc.2006.07.078.
80. [80] Shenkarev, Z.O., Panteleev, P.V., Balandin, S.V., Gizatullina, A.K., Altukhov, D.A., Finkina, E.I., et al. Recombinant expression and solution structure of antimicrobial peptide aurelin from jellyfish Aurelia aurita. Biochem. Biophys. Res. Commun. 429 (2012), 63–69, 10.1016/j.bbrc.2012.10.092.
81. [81] Vidal-Dupiol, J., Ladrière, O., Destoumieux-Garzón, D., Sautière, P.-E., Meistertzheim, A.-L., Tambutté, E., et al. Innate immune responses of a scleractinian coral to vibriosis. J. Biol. Chem. 286 (2011), 22688–22698, 10.1074/jbc.M110.216358.
82. [82] Charlet, M., Chernysh, S., Philippe, H., Hetru, C., Hoffmann, J.A., Bulet, P., Innate Immunity. Isolation of several cysteine-rich antimicrobial peptides from the blood of a mollusc, Mytilus edulis. J. Biol. Chem. 271 (1996), 21808–21813, 10.1074/jbc.271.36.21808.
83. [83] Mitta, G., Vandenbulcke, F., Roch, P., Original involvement of antimicrobial peptides in mussel innate immunity. FEBS Lett. 486 (2000), 185–190, 10.1016/S0014-5793(00)02192-X.
84. [84] Miyata, T., Tokunaga, F., Yoneya, T., Yoshikawa, K., Iwanaga, S., Niwa, M., et al. Antimicrobial peptides, isolated from horseshoe crab hemocytes tachyplesin II, and polyphemusins I and II: chemical structures and biological activity. J. Biochem. 106 (1989), 663–668.
85. [85] Jain, A., Yadav, B.K., Chugh, A., Marine antimicrobial peptide tachyplesin as an efficient nanocarrier for macromolecule delivery in plant and mammalian cells. FEBS J. 282 (2014), 732–745, 10.1111/febs.13178.
86. [86] Bulet, P., Stöcklin, R., Menin, L., Anti-microbial peptides: from invertebrates to vertebrates. Immunol. Rev. 198 (2004), 169–184.
87. [87] Yonezawa, A., Kuwahara, J., Fujii, N., Sugiura, Y., Binding of tachyplesin I to DNA revealed by footprinting analysis: significant contribution of secondary structure to DNA binding and implication for biological action. Biochemistry 31 (1992), 2998–3004, 10.1021/bi00126a022.
88. [88] Yonezawa, A., Sugiura, Y., Tachyplesin I-induced inhibition of sequence-specific protein binding to DNA. Bull. Inst. Chem. Res. Kyoto Univ. 71 (1993), 245–251.
89. [89] Steiner, H., Hultmark, D., Engström, A., Bennich, H., Boman, H.G., Sequence and specificity of two antibacterial proteins involved in insect immunity. Nature 292 (1981), 246–248, 10.1038/292246a0.
90. [90] Moore, A.J., Beazley, W.D., Bibby, M.C., Devine, D.A., Antimicrobial activity of cecropins. J. Antimicrob. Chemother. 37 (1996), 1077–1089.
91. [91] Flyg, C., Dalhammar, G., Rasmuson, B., Boman, H.G., Insect immunity. Isolation from the lepidopteran Heliothis virescens of a novel insect defensin with potent antifungal activity. Insect Biochem. 17 (1987), 153–160, 10.1016/0020-1790(87)90155-7.
92. [92] De Lucca, A.J., Walsh, T.J., Antifungal peptides: novel therapeutic compounds against emerging pathogens. Antimicrob. Agents Chemother. 43 (1999), 1–11.
93. [93] Fehlbaum, P., Bulet, P., Chernysh, S., Briand, J.P., Roussel, J.P., Letellier, L., et al. Structure-activity analysis of thanatin, a 21-residue inducible insect defense peptide with sequence homology to frog skin antimicrobial peptides. Proc. Natl. Acad. Sci. U.S.A. 93 (1996), 1221–1225, 10.1073/pnas.93.3.1221.
94. [94] Fennell, J.F., Shipman, W.H., Cole, L.J., Antibacterial action of melittin, a polypeptide from bee venom. Exp. Biol. Med. 127 (1968), 707–710, 10.3181/00379727-127-32779.
95. [95] Park, S.-C., Kim, J.-Y., Jeong, C., Yoo, S., Hahm, K.-S., Park, Y., A plausible mode of action of pseudin-2, an antimicrobial peptide from Pseudis paradoxa. Biochim. Biophys. Acta 2011 (1808), 171–182, 10.1016/j.bbamem.2010.08.023.
96. [96] Casteels, P., Ampe, C., Jacobs, F., Vaeck, M., Tempst, P., Apidaecins: antibacterial peptides from honeybees. EMBO J. 8 (1989), 2387–2391.
97. [97] Casteels, P., Tempst, P., Apidaecin-type peptide antibiotics function through a non-poreforming mechanism involving stereospecificity. Biochem. Biophys. Res. Commun. 199 (1994), 339–345, 10.1006/bbrc.1994.1234.
98. [98] Otvos, L., Rogers, I.O.M.E., Consolvo, P.J., Condie, B.A., Lovas, S., et al. Interaction between heat shock proteins and antimicrobial peptides. Biochemistry 39 (2000), 14150–14159, 10.1021/bi0012843.
99. [99] Casteels, P., Ampe, C., Riviere, L., Van Damme, J., Elicone, C., Fleming, M., et al. Isolation and characterization of abaecin, a major antibacterial response peptide in the honeybee (Apis mellifera). Eur. J. Biochem. 187 (1990), 381–386, 10.1111/j.1432-1033.1990.tb15315.x.
100. [100] Casteels, P., Ampe, C., Jacobs, F., Tempst, P., Functional and chemical characterization of Hymenoptaecin, an antibacterial polypeptide that is infection-inducible in the honeybee (Apis mellifera). J. Biol. Chem. 268 (1993), 7044–7054.
101. [101] Rahnamaeian, M., Cytryńska, M., Zdybicka-Barabas, A., Dobslaff, K., Wiesner, J., Twyman, R.M., et al. Insect antimicrobial peptides show potentiating functional interactions against Gram-negative bacteria. Proc. Biol. Sci., 282, 2015, 20150293, 10.1098/rspb.2015.0293.
102. [102] Cociancich, S., Dupont, A., Hegy, G., Lanot, R., Holder, F., Hetru, C., et al. Novel inducible antibacterial peptides from a hemipteran insect, the sap-sucking bug Pyrrhocoris apterus. Biochem. J. 300:Pt 2 (1994), 567–575.
103. [103] Bulet, P., Dimarcq, J.L., Hetru, C., Lagueux, M., Charlet, M., Hegy, G., et al. A novel inducible antibacterial peptide of Drosophila carries an O-glycosylated substitution. J. Biol. Chem. 268 (1993), 14893–14897.
104. [104] Marcos, J.F., Gandía, M., Antimicrobial peptides: to membranes and beyond. Expert Opin. Drug Discov., 2009, 10.1517/17460440902992888.
105. [105] Kragol, G., Lovas, S., Varadi, G., Condie, B.A., Hoffmann, R., Otvos, L., The antibacterial peptide pyrrhocoricin inhibits the ATPase actions of DnaK and prevents chaperone-assisted protein folding. Biochemistry 40 (2001), 3016–3026, 10.1021/bi002656a.
106. [106] Lele, D.S., Talat, S., Kumari, S., Srivastava, N., Kaur, K.J., Understanding the importance of glycosylated threonine and stereospecific action of Drosocin, a proline rich antimicrobial peptide. Eur. J. Med. Chem. 92 (2015), 637–647, 10.1016/j.ejmech.2015.01.032.
107. [107] Talat, S., Thiruvikraman, M., Kumari, S., Kaur, K.J., Glycosylated analogs of formaecin I and drosocin exhibit differential pattern of antibacterial activity. Glycoconj. J. 28 (2011), 537–555, 10.1007/s10719-011-9353-2.
108. [108] Bikker, F.J., Kaman-van Zanten, W.E., De Vries-van De Ruit, A.M.B.C., Voskamp-Visser, I., Van Hooft, P.A.V., Mars-Groenendijk, R.H., et al. Evaluation of the antibacterial spectrum of drosocin analogues. Chem. Biol. Drug Des. 68 (2006), 148–153, 10.1111/j.1747-0285.2006.00424.x.
109. [109] Marchini, D., Giordano, P.C., Amons, R., Bernini, L.F., Dallai, R., Purification and primary structure of ceratotoxin A and B, two antibacterial peptides from the female reproductive accessory glands of the medfly Ceratitis capitata (insecta: Diptera). Insect Biochem. Mol. Biol. 23 (1993), 591–598, 10.1016/0965-1748(93)90032-N.
110. [110] Rosetto, M., Manetti, A.G.O., Giordano, P.C., Marri, L., Amons, R., Baldari, C.T., et al. Molecular characterization of ceratotoxin C, a novel antibacterial female-specific peptide of the ceratotoxin family from the medfly Ceratitis capitata. Eur. J. Biochem. 241 (1996), 330–337, 10.1111/j.1432-1033.1996.00330.x.
111. [111] Manetti, A.G.O., CDNA sequence and expression of the ceratotoxin gene encoding an antibacterial sex-specific peptide from the medfly Ceratitis capitata (diptera). J. Biol. Chem. 270 (1995), 6199–6204, 10.1074/jbc.270.11.6199.
112. [112] Marri, L., Dallai, R., Marchini, D., The novel antibacterial peptide ceratotoxin A alters permeability of the inner and outer membrane of Escherichia coli K-12. Curr. Microbiol. 33 (1996), 40–43, 10.1007/s002849900071.
113. [113] Masso-Silva, J.A., Diamond, G., Antimicrobial peptides from fish. Pharmaceuticals 7 (2014), 265–310, 10.3390/ph7030265.
114. [114] van Hoek, M.L., Antimicrobial peptides in reptiles. Pharmaceuticals 7 (2014), 723–753, 10.3390/ph7060723.
115. [115] Zhang, G., Sunkara, L.T., Avian antimicrobial host defense peptides: from biology to therapeutic applications. Pharmaceuticals 7 (2014), 220–247, 10.3390/ph7030220.
116. [116] Kościuczuk, E.M., Lisowski, P., Jarczak, J., Strzałkowska, N., Jóźwik, A., Horbańczuk, J., et al. Cathelicidins: family of antimicrobial peptides. A review. Mol. Biol. Rep., 2012, 1–14, 10.1007/s11033-012-1997-x.
117. [117] Tomasinsig, L., Zanetti, M., The cathelicidins-structure, function and evolution. Curr. Protein Pept. Sci. 6 (2005), 23–34, 10.2174/1389203053027520.
118. [118] Shinnar, A., Uzzell, T., Rao, M., Spooner, E., Lane, W., Zasloff, M., New family of linear antimicrobial peptides from hagfish intestine contains bromo-tryptophan as novel amino acid. Kaumaya, P., Hodges, R., (eds.) Pept. Chem. Biol. Proc. 14th Am. Pept. Symp. Columbus, Ohio, U.S.A., 1996, Mayflower Scientific Ltd, 189–191.
119. [119] Uzzell, T., Stolzenberg, E.D., Shinnar, A.E., Zasloff, M., Hagfish intestinal antimicrobial peptides are ancient cathelicidins. Peptides 24 (2003), 1655–1667, 10.1016/j.peptides.2003.08.024.
120. [120] Broekman, D.C., Zenz, A., Gudmundsdottir, B.K., Lohner, K., Maier, V.H., Gudmundsson, G.H., Functional characterization of codCath, the mature cathelicidin antimicrobial peptide from Atlantic cod (Gadus morhua). Peptides 32 (2011), 2044–2051, 10.1016/j.peptides.2011.09.012.
121. [121] Broekman, D.C., Frei, D.M., Gylfason, G.A., Steinarsson, A., Jörnvall, H., Agerberth, B., et al. Cod cathelicidin: isolation of the mature peptide, cleavage site characterisation and developmental expression. Dev. Comp. Immunol. 35 (2011), 296–303, 10.1016/j.dci.2010.10.002.
122. [122] Chang, C., Zhang, Y., Zou, J., Nie, P., Secombes, C.J., Two cathelicidin genes are present in both rainbow trout (Oncorhynchus mykiss) and Atlantic salmon (Salmo salar). Society 50 (2006), 185–195, 10.1128/AAC.50.1.185.
123. [123] Chang, C.-I., Pleguezuelos, O., Zhang, Y.-A., Zou, J., Secombes, C.J., Identification of a novel cathelicidin gene in the rainbow trout, Oncorhynchus mykiss. Infect. Immun. 73 (2005), 5053–5064, 10.1128/IAI.73.8.5053.
124. [124] Maier, V.H., Dorn, K.V., Gudmundsdottir, B.K., Gudmundsson, G.H., Characterisation of cathelicidin gene family members in divergent fish species. Mol. Immunol. 45 (2008), 3723–3730, 10.1016/j.molimm.2008.06.002.
125. [125] Ruangsri, J., Kitani, Y., Kiron, V., Lokesh, J., Brinchmann, M.F., Karlsen, B.O., et al. A novel beta-defensin antimicrobial peptide in atlantic cod with stimulatory effect on phagocytic activity. PLoS One, 8, 2013, 10.1371/journal.pone.0062302.
126. [126] Cai, L., Cai, J.J., Liu, H.P., Fan, D.Q., Peng, H., Wang, K.J., Recombinant medaka (Oryzias melastigmus) pro-hepcidin: multifunctional characterization. Comp. Biochem. Physiol. B Biochem. Mol. Biol. 161 (2012), 140–147, 10.1016/j.cbpb.2011.10.006.
127. [127] Cole, A.M., Weis, P., Diamond, G., Isolation and characterization of pleurocidin, an antimicrobial peptide in the skin secretions of winter flounder. J. Biol. Chem. 272 (1997), 12008–12013, 10.1074/jbc.272.18.12008.
128. [128] Patrzykat, A., Friedrich, C.L., Zhang, L., Mendoza, V., Hancock, R.E.W., Sublethal concentrations of pleurocidin-derived antimicrobial peptides inhibit macromolecular synthesis in Escherichia coli. Antimicrob. Agents Chemother. 46 (2002), 605–614, 10.1128/AAC.46.3.605.
129. [129] Silphaduang, U., Noga, E.J., Peptide antibiotics in mast cells of fish. Nature 414 (2001), 268–269, 10.1038/35104690.
130. [130] Simmaco, M., Mignogna, G., Barra, D., Antimicrobial peptides from amphibian skin: What do they tell us?. Biopolym. Pept. Sci. Sect. 47 (1998), 435–450, 10.1002/(SICI)1097-0282(1998)47:6<435::AID-BIP3>3.0.CO;2-8.
131. [131] Mor, A., Nguyen, V.H., Delfour, A., Migliore-Samour, D., Nicolas, P., Isolation, amino acid sequence, and synthesis of dermaseptin, a novel antimicrobial peptide of amphibian skin. Biochemistry 30 (1991), 8824–8830, 10.1021/bi00100a014.
132. [132] Xiao, Y., Liu, C., Lai, R., Antimicrobial peptides from amphibians. Biomol. Concepts 2 (2011), 27–38, 10.1515/bmc.2011.006.
133. [133] Simmaco, M., Kreil, G., Barra, D., Bombinins, antimicrobial peptides from Bombina species. Biochim. Biophys. Acta 1788 (2009), 1551–1555, 10.1016/j.bbamem.2009.01.004.
134. [134] Kiss, G., Michl, H., Uber das Giftsekret der Gelbbauchunke, Bombina variegata L. Toxicon 1 (1962), 33–34, 10.1016/0041-0101(62)90006-5.
135. [135] Csordás, A., Michl, H., Isolation and structure elucidation of an hemolytic polypeptide from the defensive secretion European Bombina species (in German). Monatsh. Chem. 101 (1970), 182–189, 10.1007/BF00907538.
136. [136] Simmaco, M., Barra, D., Chiarini, F., Noviello, L., Melchiorri, P., Kreil, G., et al. A family of bombinin-related peptides from the skin of Bombina variegata. Eur. J. Biochem. 199 (1991), 217–222, 10.1111/j.1432-1033.1991.tb16112.x.
137. [137] Gibson, B.W., Tang, D., Mandrell, R., Kelly, M., Spindel, E.R., Bombinin-like peptides with antimicrobial activity from skin secretions of the Asian toad, Bombina orientalis. J. Biol. Chem. 266 (1991), 23103–23111.
138. [138] Mignogna, G., Simmaco, M., Kreil, G., Barra, D., Antibacterial and haemolytic peptides containing D-alloisoleucine from the skin of Bombina variegata. EMBO J. 12 (1993), 4829–4832.
139. [139] Mangoni, M.L., Maisetta, G., Di Luca, M., Gaddi, L.M.H., Esin, S., Florio, W., et al. Comparative analysis of the bactericidal activities of amphibian peptide analogues against multidrug-resistant nosocomial bacterial strains. Antimicrob. Agents Chemother. 52 (2008), 85–91, 10.1128/AAC.00796-07.
140. [140] Lai, R., Liu, H., Hui Lee, W., Zhang, Y., An anionic antimicrobial peptide from toad Bombina maxima. Biochem. Biophys. Res. Commun. 295 (2002), 796–799, 10.1016/S0006-291X(02)00762-3.
141. [141] Lai, R., Zheng, Y.T., Shen, J.H., Liu, G.J., Liu, H., Lee, W.H., et al. Antimicrobial peptides from skin secretions of Chinese red belly toad Bombina maxima. Peptides 23 (2002), 427–435, 10.1016/S0196-9781(01)00641-6.
142. [142] Lee, W.H., Li, Y., Lai, R., Li, S., Zhang, Y., Wang, W., Variety of antimicrobial peptides in the Bombina maxima toad and evidence of their rapid diversification. Eur. J. Immunol. 35 (2005), 1220–1229, 10.1002/eji.200425615.
143. [143] Wang, T., Zhang, J., Shen, J.H., Jin, Y., Lee, W.H., Zhang, Y., Maximins S, a novel group of antimicrobial peptides from toad Bombina maxima. Biochem. Biophys. Res. Commun. 327 (2005), 945–951, 10.1016/j.bbrc.2004.12.094.
144. [144] Liu, R., Liu, H., Ma, Y., Wu, J., Yang, H., Ye, H., et al. There are abundant antimicrobial peptides in brains of two kinds of Bombina toads. J. Proteome Res. 10 (2011), 1806–1815, 10.1021/pr101285n.
145. [145] Park, C.B.C., Kim, M.M.S., Kim, S.C.S., A novel antimicrobial peptide from Bufo bufo gargarizans. Biochem. Biophys. Res Commun. 218 (1996), 408–413, 10.1006/bbrc.1996.0071.
146. [146] Hale, J.D.F., Hancock, R.E.W., Alternative mechanisms of action of cationic antimicrobial peptides on bacteria. Expert Rev. Anti Infect. Ther. 5 (2007), 951–959, 10.1586/14787210.5.6.951.
147. [147] Hao, X., Yang, H., Wei, L., Yang, S., Zhu, W., Ma, D., et al. Amphibian cathelicidin fills the evolutionary gap of cathelicidin in vertebrate. Amino Acids 43 (2012), 677–685, 10.1007/s00726-011-1116-7.
148. [148] Wei, L., Yang, J., He, X., Mo, G., Hong, J., Yan, X., et al. Structure and function of a potent lipopolysaccharide-binding antimicrobial and anti-inflammatory peptide. J. Med. Chem. 56 (2013), 3546–3556, 10.1021/jm4004158.
149. [149] Yu, H., Cai, S., Gao, J., Zhang, S., Lu, Y., Qiao, X., et al. Identification and polymorphism discovery of the cathelicidins, Lf-CATHs in ranid amphibian (Limnonectes fragilis). FEBS J. 280 (2013), 6022–6032, 10.1111/febs.12521.
150. [150] Ling, G., Gao, J., Zhang, S., Xie, Z., Wei, L., Yu, H., et al. Cathelicidins from the bullfrog Rana catesbeiana provides novel template for peptide antibiotic design. PLoS One, 9, 2014, 10.1371/journal.pone.0093216.
151. [151] Simmaco, M., Mignognas, G., Barra, D., Bossas, F., Antimicrobial peptides from skin secretions of Rana esculenta. J. Biol. Chem. 269 (1994), 11956–11961.
152. [152] Mor, A., Nicolas, P., Isolation and structure of novel defensive peptides from frog skin. Eur. J. Biochem. 219 (1994), 145–154.
153. [153] Mor, A., Hani, K., Nicolas, P., The vertebrate peptide antibiotics dermaseptins have overlapping structural features but target specific microorganisms. J. Biol. Chem. 269 (1994), 31635–31641.
154. [154] Amiche, M., Ladram, A., Nicolas, P., A consistent nomenclature of antimicrobial peptides isolated from frogs of the subfamily Phyllomedusinae. Peptides 29 (2008), 2074–2082, 10.1016/j.peptides.2008.06.017.
155. [155] Nicolas, P., El Amri, C., The dermaseptin superfamily: a gene-based combinatorial library of antimicrobial peptides. Biochim. Biophys. Acta 1788 (2009), 1537–1550, 10.1016/j.bbamem.2008.09.006.
156. [156] Vanhoye, D., Bruston, F., El Amri, S., Ladram, A., Amiche, M., Nicolas, P., Membrane association, electrostatic sequestration, and cytotoxicity of Gly-Leu-rich peptide orthologs with differing functions. Biochemistry 43 (2004), 8391–8409, 10.1021/bi0493158.
157. [157] Amiche, M., Seon, A.A., Wroblewski, H., Nicolas, P., Isolation of dermatoxin from frog skin, an antibacterial peptide encoded by a novel member of the dermaseptin genes family. Eur. J. Biochem. 267 (2000), 4583–4592, 10.1046/j.1432-1327.2000.01514.x.
158. [158] El Amri, C., Lacombe, C., Zimmerman, K., Ladram, A., Amiche, M., Nicolas, P., et al. The plasticins: membrane adsorption, lipid disorders, and biological activity. Biochemistry 45 (2006), 14285–14297, 10.1021/bi060999o.
159. [159] Wu, M., Maier, E., Benz, R., Hancock, R.E.W., Mechanism of interaction of different classes of cationic antimicrobial peptides with planar bilayers and with the cytoplasmic membrane of Escherichia coli. Biochemistry 38 (1999), 7235–7242, 10.1021/bi9826299.
160. [160] Pierre, T.N., Seon, A.A., Amiche, M., Nicolas, P., Phylloxin, a novel peptide antibiotic of the dermaseptin family of antimicrobial/opioid peptide precursors. Eur. J. Biochem. 267 (2000), 370–378, 10.1046/j.1432-1327.2000.01012.x.
161. [161] Leite, J.R.S.A., Silva, L.P., Rodrigues, M.I.S., Prates, M.V., Brand, G.D., Lacava, B.M., et al. Phylloseptins: a novel class of anti-bacterial and anti-protozoan peptides from the Phyllomedusa genus. Peptides 26 (2005), 565–573, 10.1016/j.peptides.2004.11.002.
162. [162] Raja, Z., André, S., Piesse, C., Sereno, D., Nicolas, P., Foulon, T., et al. Structure, antimicrobial activities and mode of interaction with membranes of novel Phylloseptins from the painted-belly leaf frog, Phyllomedusa sauvagii. PLoS One, 8, 2013, 10.1371/journal.pone.0070782.
163. [163] Rollins-Smith, L.A., King, J.D., Nielsen, P.F., Sonnevend, A., Conlon, J.M., An antimicrobial peptide from the skin secretions of the mountain chicken frog Leptodactylus fallax (Anura: Leptodactylidae). Regul. Pept. 124 (2005), 173–178, 10.1016/j.regpep.2004.07.013.
164. [164] Basir, Y.J., Knoop, F.C., Dulka, J., Conlon, J.M., Multiple antimicrobial peptides and peptides related to bradykinin and neuromedin N isolated from skin secretions of the pickerel frog, Rana palustris. Biochim. Biophys. Acta 1543 (2000), 95–105, 10.1016/S0167-4838(00)00191-6.
165. [165] Zasloff, M., Magainins, a class of antimicrobial peptides from Xenopus skin: isolation, characterization of two active forms, and partial cDNA sequence of a precursor. Proc. Natl. Acad. Sci. U.S.A. 84 (1987), 5449–5453, 10.1097/00043764-198806000-00004.
166. [166] Matsuzaki, K., Why and how are peptide–lipid interactions utilized for self-defense? Magainins and tachyplesins as archetypes. Biochim. Biophys. Acta 1462 (1999), 1–10, 10.1016/S0005-2736(99)00197-2.
167. [167] Mechkarska, M., Ahmed, E., Coquet, L., Leprince, J., Jouenne, T., Vaudry, H., et al. Peptidomic analysis of skin secretions demonstrates that the allopatric populations of Xenopus muelleri (Pipidae) are not conspecific. Peptides 32 (2011), 1502–1508, 10.1016/j.peptides.2011.05.025.
168. [168] Conlon, J.M., Al-Ghaferi, N., Ahmed, E., Meetani, M.A., Leprince, J., Nielsen, P.F., Orthologs of magainin, PGLa, procaerulein-derived, and proxenopsin-derived peptides from skin secretions of the octoploid frog Xenopus amieti (Pipidae). Peptides 31 (2010), 989–994, 10.1016/j.peptides.2010.03.002.
169. [169] Conlon, J.M., Mechkarska, M., Kolodziejek, J., Nowotny, N., Coquet, L., Leprince, J., et al. Host-defense peptides from skin secretions of Fraser's clawed frog Xenopus fraseri (Pipidae): Further insight into the evolutionary history of the Xenopodinae. Comp. Biochem. Physiol. D Genomics Proteomics 12 (2014), 45–52, 10.1016/j.cbd.2014.10.001.
170. [170] Roelants, K., Fry, B.G., Ye, L., Stijlemans, B., Brys, L., Kok, P., et al. Origin and functional diversification of an amphibian defense peptide arsenal. PLoS Genet., 9, 2013, e1003662, 10.1371/journal.pgen.1003662.
171. [171] Soravia, E., Martini, G., Zasloff, M., Antimicrobial properties of peptides from Xenopus granular gland secretions. FEBS Lett. 228 (1988), 337–341.
172. [172] Olson, L., Soto, A.M., Knoop, F.C., Conlon, J.M., Pseudin-2: an antimicrobial peptide with low hemolytic activity from the skin of the paradoxical frog. Biochem. Biophys. Res. Commun. 288 (2001), 1001–1005, 10.1006/bbrc.2001.5884.
173. [173] Goraya, J., Knoop, F.C., Conlon, J.M., Ranatuerins: antimicrobial peptides isolated from the skin of the American bullfrog, Rana catesbeiana. Biochem. Biophys. Res. Commun. 250 (1998), 589–592, 10.1006/bbrc.1998.9362.
174. [174] Sonnevend, A., Knoop, F.C., Patel, M., Pál, T., Soto, A.M., Conlon, J.M., Antimicrobial properties of the frog skin peptide, ranatuerin-1 and its [Lys-8]-substituted analog. Peptides 25 (2004), 29–36, 10.1016/j.peptides.2003.11.011.
175. [175] Clark, D.P., Durell, S., Maloy, W.L., Zaslof, M., Ranalexin. A novel antimicrobial peptide from bullfrog (Rana catesbeiana) skin, structurally related to the bacterial antibiotic, polymyxin. J. Biol. Chem. 269 (1994), 10849–10855.
176. [176] Giacometti, A., Cirioni, O., Greganti, G., Quarta, M., In vitro activities of membrane-active peptides against Gram-positive and Gram-negative aerobic bacteria in vitro activities of membrane-active peptides against Gram-positive and Gram-negative aerobic bacteria. Antimicrob. Agents Chemother. 42 (1998), 3320–3324.
177. [177] Cheng, Y., Prickett, M.D., Gutowska, W., Kuo, R., Belov, K., Burt, D.W., Evolution of the avian β-defensin and cathelicidin genes. BMC Evol. Biol., 15, 2015, 188, 10.1186/s12862-015-0465-3.
178. [178] Semple, C.A., Rolfe, M., Dorin, J.R., Duplication and selection in the evolution of primate beta-defensin genes. Genome Biol., 4, 2003, R31, 10.1186/gb-2003-4-5-r31.
179. [179] Zhao, H., Gan, T.X., Liu, X.D., Jin, Y., Lee, W.H., Shen, J.H., et al. Identification and characterization of novel reptile cathelicidins from elapid snakes. Peptides 29 (2008), 1685–1691, 10.1016/j.peptides.2008.06.008.
180. [180] Wang, Y., Hong, J., Liu, X., Yang, H., Liu, R., Wu, J., et al. Snake cathelicidin from Bungarus fasciatus is a potent peptide antibiotics. PLoS One, 3, 2008, 10.1371/journal.pone.0003217.
181. [181] Nair, D.G., Fry, B.G., Alewood, P., Kumar, P.P., Kini, R.M., Antimicrobial activity of omwaprin, a new member of the waprin family of snake venom proteins. Biochem. J. 402 (2007), 93–104, 10.1042/BJ20060318.
182. [182] Xiao, Y., Cai, Y., Bommineni, Y.R., Fernando, S.C., Prakash, O., Gilliland, S.E., et al. Identification and functional characterization of three chicken cathelicidins with potent antimicrobial activity. J. Biol. Chem. 281 (2006), 2858–2867, 10.1074/jbc.M507180200.
183. [183] Goitsuka, R., Chen, C.-L.H., Benyon, L., Asano, Y., Kitamura, D., Cooper, M.D., Chicken cathelicidin-B1, an antimicrobial guardian at the mucosal M cell gateway. Proc. Natl. Acad. Sci. U.S.A. 104 (2007), 15063–15068, 10.1073/pnas.0707037104.
184. [184] Gao, W., Xing, L., Qu, P., Tan, T., Yang, N., Li, D., et al. Identification of a novel cathelicidin antimicrobial peptide from ducks and determination of its functional activity and antibacterial mechanism. Sci. Rep., 5, 2015, 17260, 10.1038/srep17260.
185. [185] Stegemann, C., Kolobov, A., Leonova, Y.F., Knappe, D., Shamova, O., Ovchinnikova, T.V., et al. Isolation, purification and de novo sequencing of TBD-1, the first beta-defensin from leukocytes of reptiles. Proteomics 9 (2009), 1364–1373, 10.1002/pmic.200800569.
186. [186] Yount, N.Y., Kupferwasser, D., Spisni, A., Dutz, S.M., Ramjan, Z.H., Sharma, S., et al. Selective reciprocity in antimicrobial activity versus cytotoxicity of hBD-2 and crotamine. Proc. Natl. Acad. Sci. U.S.A. 106 (2009), 14972–14977, 10.1073/pnas.0904465106.
187. [187] Lakshminarayanan, R., Vivekanandan, S., Samy, R.P., Banerjee, Y., Chi-Jin, E.O., Kay, W.T., et al. Structure, self-assembly, and dual role of a β-defensin-like peptide from the Chinese soft-shelled turtle eggshell matrix. J. Am. Chem. Soc. 130 (2008), 4660–4668, 10.1021/ja075659k.
188. [188] Chattopadhyay, S., Sinha, N.K., Banerjee, S., Roy, D., Chattopadhyay, D., Roy, S., Small cationic protein from a marine turtle has β-defensin-like fold and antibacterial and antiviral activity. Proteins Struct. Funct. Bioinf. 64 (2006), 524–531, 10.1002/prot.20963.
189. [189] Sugiarto, H., Yu, P.L., Avian antimicrobial peptides: the defense role of B-defensins. Biochem. Biophys. Res. Commun. 323 (2004), 721–727, 10.1016/j.bbrc.2004.08.162.
190. [190] Evans, E.W., Beach, G.G., Wunderlich, J., Harmon, B.G., Isolation of antimicrobial peptides from avian heterophils. J. Leukoc. Biol. 56 (1994), 661–665.
191. [191] Evans, E.W., Beach, F.G., Moore, K.M., Jackwood, M.W., Glisson, J.R., Harmon, B.G., Antimicrobial activity of chicken and turkey heterophil peptides CHP1, CHP2, THP1, and THP3. Vet. Microbiol. 47 (1995), 295–303, 10.1016/0378-1135(95)00126-3.
192. [192] Harwig, S.S.L., Swiderek, K.M., Kokryakov, V.N., Tan, L., Lee, T.D., Panyutich, E.A., et al. Gallinacins: cystine-rich antimicrobial peptides of chicken leukocytes. FEBS Lett. 342 (1994), 281–285.
193. [193] Derache, C., Labas, V., Aucagne, V., Meudal, H., Landon, C., Delmas, A.F., et al. Primary structure and antibacterial activity of chicken bone marrow-derived β-defensins. Antimicrob. Agents Chemother. 53 (2009), 4647–4655, 10.1128/AAC.00301-09.
194. [194] Zhao, C., Nguyen, T., Liu, L., Sacco, R.E., Brogden, K.A., Lehrer, R.I., Gallinacin-3, an inducible epithelial β-defensin in the chicken. Infect. Immun. 69 (2001), 2684–2691, 10.1128/IAI.69.4.2684-2691.2001.
195. [195] Thouzeau, C., Le Maho, Y., Froget, G., Sabatier, L., Le Bohec, C., Hoffmann, J.A., et al. Spheniscins, avian β-defensins in preserved stomach contents of the King Penguin, Aptenodytes patagonicus. J. Biol. Chem. 278 (2003), 51053–51058, 10.1074/jbc.M306839200.
196. [196] Sugiarto, H., Yu, P.L., Identification of three novel ostricacins: an update on the phylogenetic perspective of β-defensins. Int. J. Antimicrob. Agents 27 (2006), 229–235, 10.1016/j.ijantimicag.2005.10.013.
197. [197] van Dijk, A., Veldhuizen, E.J.A., Haagsman, H.P., Avian defensins. Vet. Immunol. Immunopathol. 124 (2008), 1–18, 10.1016/j.vetimm.2007.12.006.
198. [198] Lynn, D.J., Higgs, R., Lloyd, A.T., O'Farrelly, C., Hervé-Grépinet, V., Nys, Y., et al. Avian beta-defensin nomenclature: a community proposed update. Immunol. Lett. 110 (2007), 86–89, 10.1016/j.imlet.2007.03.007.
199. [199] Yang, D., Biragyn, A., Kwak, L.W., Oppenheim, J.J., Mammalian defensins in immunity: more than just microbicidal. Trends Immunol. 23 (2002), 291–296, 10.1016/S1471-4906(02)02246-9.
200. [200] Dürr, U.H.N., Sudheendra, U.S., Ramamoorthy, A., LL-37, the only human member of the cathelicidin family of antimicrobial peptides. Biochim. Biophys. Acta 1758 (2006), 1408–1425, 10.1016/j.bbamem.2006.03.030.
201. [201] De Smet, K., Contreras, R., Human antimicrobial peptides: defensins, cathelicidins and histatins. Biotechnol. Lett. 27 (2005), 1337–1347, 10.1007/s10529-005-0936-5.
202. [202] Turner, J., Cho, Y., Dinh, N.N., Waring, A.J., Lehrer, R.I., Activities of LL-37, a cathelin-associated antimicrobial peptide of human neutrophils. Antimicrob. Agents Chemother. 42 (1998), 2206–2214, 10.5021/ad.2012.24.2.126.
203. [203] Duplantier, A.J., van Hoek, M.L., The human cathelicidin antimicrobial peptide LL-37 as a potential treatment for polymicrobial infected wounds. Front. Immunol. 4 (2013), 1–14, 10.3389/fimmu.2013.00143.
204. [204] Overhage, J., Campisano, A., Bains, M., Torfs, E.C.W., Rehm, B.H.A., Hancock, R.E.W., Human host defense peptide LL-37 prevents bacterial biofilm formation. Infect. Immun. 76 (2008), 4176–4182, 10.1128/IAI.00318-08.
205. [205] Falla, T.J., Nedra Karunaratne, D., Hancock, R.E.W., Mode of action of the antimicrobial peptide indolicidin. J. Biol. Chem. 271 (1996), 19298–19303, 10.1074/jbc.271.32.19298.
206. [206] Brahma, B., Patra, M.C., Karri, S., Chopra, M., Mishra, P., De, B.C., et al. Diversity, antimicrobial action and structure-activity relationship of buffalo cathelicidins. PLoS One, 10, 2015, e0144741, 10.1371/journal.pone.0144741.
207. [207] Hsu, C.H., Chen, C., Jou, M.L., Lee, A.Y.L., Lin, Y.C., Yu, Y.P., et al. Structural and DNA-binding studies on the bovine antimicrobial peptide, indolicidin: evidence for multiple conformations involved in binding to membranes and DNA. Nucleic Acids Res. 33 (2005), 4053–4064, 10.1093/nar/gki725.
208. [208] Marchand, C., Krajewski, K., Lee, H.-F., Antony, S., Johnson, A.A., Amin, R., et al. Covalent binding of the natural antimicrobial peptide indolicidin to DNA abasic sites. Nucleic Acids Res. 34 (2006), 5157–5165, 10.1093/nar/gkl667.
209. [209] Subbalakshmi, C., Sitaram, N., Mechanism of antimicrobial action of indolicidin. FEMS Microbiol. Lett. 160 (1998), 91–96, 10.1016/S0378-1097(98)00008-1.
210. [210] Kokryakov, V.N., Harwig, S.S.L., Panyutich, E.A., Shevchenko, A.A., Aleshina, G.M., Shamova, O.V., et al. Protegrins: leukocyte antimicrobial peptides that combine features of corticostatic defensins and tachyplesins. FEBS Lett. 327 (1993), 231–236, 10.1016/0014-5793(93)80175-T.
211. [211] Steinberg, D.A., Hurst, M.A., Fujii, C.A., Kung, A.H.C., Ho, J.F., Cheng, F.C., et al. Protegrin-1: a broad-spectrum, rapidly microbicidal peptide with in vivo activity. Antimicrob. Agents Chemother. 41 (1997), 1738–1742.
212. [212] Yan, H., Hancock, R.E.W., Synergistic interactions between mammalian antimicrobial defense peptides. Antimicrob. Agents Chemother. 45 (2001), 1558–1560, 10.1128/AAC.45.5.1558-1560.2001.
213. [213] Brogden, K.A., Ackermann, M., McCray, P.B., Tack, B.F., Antimicrobial peptides in animals and their role in host defences. Int. J. Antimicrob. Agents 22 (2003), 465–478, 10.1016/S0924-8579(03)00180-8.
214. [214] Romeo, D., Skerlavaj, B., Bolognesi, M., Gennaro, R., Structure and bactericidal activity of an antibiotic dodecapeptide purified from bovine neutrophils. J. Biol. Chem. 263 (1988), 9573–9575.
215. [215] Wu, M., Hancock, R.E.W., Interaction of the cyclic antimicrobial cationic peptide bactenecin with the outer and cytoplasmic membrane. J. Biol. Chem. 274 (1999), 29–35.
216. [216] Madhongsa, K., Pasan, S., Phophetleb, O., Nasompag, S., Thammasirirak, S., Daduang, S., et al. Antimicrobial action of the cyclic peptide bactenecin on Burkholderia pseudomallei correlates with efficient membrane permeabilization. PLoS Negl. Trop. Dis. 7 (2013), 1–13, 10.1371/journal.pntd.0002267.
217. [217] Skerlavaj, B., Romeo, D., Gennaro, R., Rapid membrane permeabilization and inhibition of vital functions of Gram-negative bacteria by bactenecins. Infect. Immun. 58 (1990), 3724–3730.
218. [218] Scocchi, M., Bontempo, D., Boscolo, S., Tomasinsig, L., Giulotto, E., Zanetti, M., Novel cathelicidins in horse leukocytes. FEBS Lett. 457 (1999), 459–464, 10.1016/S0014-5793(99)01097-2.
219. [219] Skerlavaj, B., Scocchi, M., Gennaro, R., Risso, A., Zanetti, M., Structural and functional analysis of horse cathelicidin peptides. Antimicrob. Agents Chemother. 45 (2001), 715–722, 10.1128/AAC.45.3.715-722.2001.
220. [220] Schlusselhuber, M., Torelli, R., Martini, C., Leippe, M., Cattoir, V., Leclercq, R., et al. The equine antimicrobial peptide eCATH1 is effective against the facultative intracellular pathogen Rhodococcus equi in mice. Antimicrob. Agents Chemother. 57 (2013), 4615–4621, 10.1128/AAC.02044-12.
221. [221] Niyonsaba, F., Ogawa, H., Protective roles of the skin against infection: Implication of naturally occurring human antimicrobial agents β-defensins, cathelicidin LL-37 and lysozyme. J. Dermatol. Sci. 40 (2005), 157–168, 10.1016/j.jdermsci.2005.07.009.
222. [222] Guilhelmelli, F., Vilela, N., Albuquerque, P., Derengowski, L. da S., Silva-Pereira, I., Kyaw, C.M., Antibiotic development challenges: the various mechanisms of action of antimicrobial peptides and of bacterial resistance. Front. Microbiol., 4, 2013, 353, 10.3389/fmicb.2013.00353.
223. [223] Selsted, M.E., Ouellette, A.J., Mammalian defensins in the antimicrobial immune response. Nat. Immunol. 6 (2005), 551–557, 10.1146/annurev-pathol-011811-132427.
224. [224] Lehrer, R.I., Lu, W., Α-defensins in human innate immunity. Immunol. Rev. 245 (2012), 84–112, 10.1111/j.1600-065X.2011.01082.x.
225. [225] Ayabe, T., Satchell, D.P., Wilson, C.L., Parks, W.C., Selsted, M.E., Ouellette, A.J., Secretion of microbicidal alpha-defensins by intestinal Paneth cells in response to bacteria. Nat. Immunol. 1 (2000), 113–118, 10.1038/77783.
226. [226] Zeya, H.I., Spitznagel, J.K., Cationic proteins of polymorphonuclear leukocyte lysosomes. I. Resolution of antibacterial and enzymatic activities. J. Bacteriol. 91 (1966), 750–754.
227. [227] Yamashita, T., Saito, K., Purification, primary structure, and biological activity of guinea pig neutrophil cationic peptides. Infect. Immun. 57 (1989), 2405–2409.
228. [228] Selsted, M.E., Brown, D.M., DeLange, R.J., Harwig, S.S., Lehrer, R.I., Primary structures of six antimicrobial peptides of rabbit peritoneal neutrophils. J. Biol. Chem. 260 (1985), 4579–4584.
229. [229] Eisenhauer, P.B., Harwig, S.S.L., Szklarek, D., Ganz, T., Selsted, M.E., Lehrer, R.I., Purification and antimicrobial properties of three defensins from rat neutrophils. Infect. Immun. 57 (1989), 2021–2027.
230. [230] Mak, P., Wójcik, K., Thogersen, I.B., Dubin, A., Isolation, antimicrobial activities, and primary structures of hamster neutrophil defensins. Infect. Immun. 64 (1996), 4444–4449.
231. [231] Schneider, J.J., Unholzer, A., Schaller, M., Schäfer-Korting, M., Korting, H.C., Human defensins. J. Mol. Med. 83 (2005), 587–595, 10.1007/s00109-005-0657-1.
232. [232] Varkey, J., Nagaraj, R., Antibacterial activity of human neutrophil defensin HNP-1 analogs without cysteines. Antimicrob. Agents Chemother. 49 (2005), 4561–4566, 10.1128/AAC.49.11.4561-4566.2005.
233. [233] Lehrer, R.I., Lichtenstein, A.K., Ganz, T., Defensins: antimicrobial and cytotoxic peptides of mammalian cells. Annu. Rev. Immunol. 11 (1993), 105–128, 10.1146/annurev.iy.11.040193.000541.
234. [234] Zhang, Y., Lu, W., Hong, M., The membrane-bound structure and topology of a human Alpha-defensin indicate a dimer pore mechanism for membrane disruption. Biochemistry 49 (2010), 9770–9782, 10.1021/bi101512j.
235. [235] Ouellette, A.J., Paneth cell α-defensins in enteric innate immunity. Cell. Mol. Life Sci. 68 (2011), 2215–2229, 10.1007/s00018-011-0714-6.
236. [236] Ouellette, A.J., Hsieh, M.M., Nosek, M.T., Cano-Gauci, D.F., Huttner, K.M., Buick, R.N., et al. Mouse Paneth cell defensins: primary structures and antibacterial activities of numerous cryptdin isoforms. Infect. Immun. 62 (1994), 5040–5047.
237. [237] Condon, M.R., Viera, A., D'Alessio, M., Diamond, G., Induction of a rat enteric defensin gene by hemorrhagic shock. Infect. Immun. 67 (1999), 4787–4793.
238. [238] Bruhn, O., Cauchard, J., Schlusselhuber, M., Gelhaus, C., Podschun, R., Thaller, G., et al. Antimicrobial properties of the equine alpha-defensin DEFA1 against bacterial horse pathogens. Vet. Immunol. Immunopathol. 130 (2009), 102–106, 10.1016/j.vetimm.2009.01.005.
239. [239] Tanabe, H., Yuan, J., Zaragoza, M.M., Dandekar, S., Henschen-Edman, A., Selsted, M.E., et al. Paneth cell alpha-defensins from rhesus macaque small intestine. Infect. Immun. 72 (2004), 1470–1478, 10.1128/IAI.72.3.1470.
240. [240] Patil, A.A., Cai, Y., Sang, Y., Blecha, F., Zhang, G., Cross-species analysis of the mammalian beta-defensin gene family: presence of syntenic gene clusters and preferential expression in the male reproductive tract. Physiol. Genomics 23 (2005), 5–17, 10.1152/physiolgenomics.00104.2005.
241. [241] Diamond, G., Zasloff, M., Eck, H., Brasseur, M., Maloy, W.L., Bevins, C.L., Tracheal antimicrobial peptide, a cysteine-rich peptide from mammalian tracheal mucosa: peptide isolation and cloning of a cDNA. Proc. Natl. Acad. Sci. U.S.A. 88 (1991), 3952–3956, 10.1073/pnas.88.9.3952.
242. [242] Taha-Abdelaziz, K., Perez-Casal, J., Schott, C., Hsiao, J., Attah-Poku, S., Slavić, D., et al. Bactericidal activity of tracheal antimicrobial peptide against respiratory pathogens of cattle. Vet. Immunol. Immunopathol. 152 (2013), 289–294, 10.1016/j.vetimm.2012.12.016.
243. [243] Schonwetter, B.S., Stolzenberg, E.D., Zasloff, M.A., Epithelial antibiotics induced at sites of inflammation. Science 267 (1995), 1645–1648.
244. [244] Roosen, S., Exner, K., Paul, S., Schröder, J.-M., Kalm, E., Looft, C., Bovine beta-defensins: identification and characterization of novel bovine beta-defensin genes and their expression in mammary gland tissue. Mamm. Genome 15 (2004), 834–842, 10.1007/s00335-004-2387-z.
245. [245] Isobe, N., Nakamura, J., Nakano, H., Yoshimura, Y., Existence of functional lingual antimicrobial peptide in bovine milk. J. Dairy Sci. 92 (2009), 2691–2695, 10.3168/jds.2008-1940.
246. [246] Rieg, S., Meier, B., Fähnrich, E., Huth, A., Wagner, D., Kern, W.V., et al. Differential activity of innate defense antimicrobial peptides against Nocardia species. BMC Microbiol., 10, 2010, 61, 10.1186/1471-2180-10-61.
247. [247] Selsted, M.E., Tang, Y.Q., Morris, W.L., McGuire, P.A., Novotny, M.J., Smith, W., et al. Purification, primary structures, and antibacterial activities of beta-defensins, a new family of antimicrobial peptides from bovine neutrophils. J. Biol. Chem., 271, 1996, 16430.
248. [248] Stenbeck, G., So, T.H., James, E., Young, S.W., Qing, F., Harriman, A., et al. Production of β-defensins by human airway epithelia. Proc. Natl. Acad. Sci. U.S.A. 95 (1998), 14961–14966, 10.1073/pnas.95.25.14961.
249. [249] Pazgier, M., Hoover, D.M., Yang, D., Lu, W., Lubkowski, J., Human β-defensins. Cell. Mol. Life Sci. 63 (2006), 1294–1313, 10.1007/s00018-005-5540-2.
250. [250] Zhao, C., Wang, I., Lehrer, R.I., Widespread expression of beta-defensin hBD-1 in human secretory glands and epithelial cells. FEBS Lett. 396 (1996), 319–322, 10.1016/0014-5793(96)01123-4.
251. [251] Harder, J., Bartels, J., Christophers, E., Schröder, J.M., Isolation and characterization of human β-defensin-3, a novel human inducible peptide antibiotic. J. Biol. Chem. 276 (2001), 5707–5713, 10.1074/jbc.M008557200.
252. [252] Schroeder, B.O., Wu, Z., Nuding, S., Groscurth, S., Marcinowski, M., Beisner, J., et al. Reduction of disulphide bonds unmasks potent antimicrobial activity of human β-defensin 1. Nature 469 (2011), 419–423, 10.1038/nature09674.
253. [253] Nuding, S., Zabel, L.T., Enders, C., Porter, E., Fellermann, K., Wehkamp, J., et al. Antibacterial activity of human defensins on anaerobic intestinal bacterial species: a major role of HBD-3. Microbes Infect. 11 (2009), 384–393, 10.1016/j.micinf.2009.01.001.
254. [254] Harder, J., Bartels, J., Christophers, E., Schröder, J.-M., A peptide antibiotic from human skin. Nature, 387, 1997, 10.1038/43088 861–861.
255. [255] Kaiser, V., Diamond, G., Expression of mammalian defensin genes. J. Leukoc. Biol. 68 (2000), 779–784.
256. [256] Bals, R., Wang, X., Wu, Z., Freeman, T., Bafna, V., Zasloff, M., et al. Human beta-defensin 2 is a salt-sensitive peptide antibiotic expressed in human lung. J. Clin. Invest. 102 (1998), 874–880, 10.1172/JCI2410.
257. [257] Joly, S., Maze, C., McCray, P.B., Guthmiller, J.M., Human β-defensins 2 and 3 demonstrate strain-selective activity against oral microorganisms. J. Clin. Microbiol. 42 (2004), 1024–1029, 10.1128/JCM.42.3.1024-1029.2004.
258. [258] Sass, V., Schneider, T., Wilmes, M., Körner, C., Tossi, A., Novikova, N., et al. Human β-defensin 3 inhibits cell wall biosynthesis in staphylococci. Infect. Immun. 78 (2010), 2793–2800, 10.1128/IAI.00688-09.
259. [259] Boniotto, M., Antcheva, N., Zelezetsky, I., Tossi, A., Palumbo, V., Verga Falzacappa, M.V., et al. A study of host defence peptide beta-defensin 3 in primates. Biochem. J. 374 (2003), 707–714, 10.1042/BJ20030528.
260. [260] Abou Alaiwa, M.H., Reznikov, L.R., Gansemer, N.D., Sheets, K.A., Horswill, A.R., Stoltz, D.A., et al. PH modulates the activity and synergism of the airway surface liquid antimicrobials beta-defensin-3 and LL-37. Proc. Natl. Acad. Sci. U.S.A. 111 (2014), 18703–18708, 10.1073/pnas.1422091112.
261. [261] Nuding, S., Frasch, T., Schaller, M., Stange, E.F., Zabel, L.T., Synergistic effects of antimicrobial peptides and antibiotics against Clostridium difficile. Antimicrob. Agents Chemother. 58 (2014), 5719–5725, 10.1128/AAC.02542-14.
262. [262] García, J.R., Krause, A., Schulz, S., Rodríguez-Jiménez, F.J., Klüver, E., Adermann, K., et al. Human beta-defensin 4: a novel inducible peptide with a specific salt-sensitive spectrum of antimicrobial activity. FASEB J. 15 (2001), 1819–1821, 10.1096/fj.00-0865fje.
263. [263] Sharma, H., Nagaraj, R., Human β-defensin 4 with non-native disulfide bridges exhibit antimicrobial activity. PLoS One 10 (2015), 14–18, 10.1371/journal.pone.0119525.
264. [264] Schutte, B.C., Mitros, J.P., Jennifer, A., Walters, J.D., Jia, H.P., Welsh, M.J., et al. Discovery of five conserved -defensin gene clusters using a computational search strategy. Proc. Natl. Acad. Sci. U.S.A., 99, 2002, 10.1073/pnas.222515799 14611–14611.
265. [265] Hazlett, L., Wu, M., Defensins in innate immunity. Cell Tissue Res. 343 (2011), 175–188, 10.1007/s00441-010-1022-4.
266. [266] Garcia, A.E., Ösapay, G., Tran, P.A., Yuan, J., Selsted, M.E., Isolation, synthesis, and antimicrobial activities of naturally occurring θ-defensin isoforms from baboon leukocytes. Infect. Immun. 76 (2008), 5883–5891, 10.1128/IAI.01100-08.
267. [267] Tang, Y.Q., Yuan, J., Osapay, G., Osapay, K., Tran, D., Miller, C.J., et al. A cyclic antimicrobial peptide produced in primate leukocytes by the ligation of two truncated alpha-defensins. Science 286 (1999), 498–502, 10.1126/science.286.5439.498.
268. [268] Tran, D., Tran, P.A., Tang, Y.Q., Yuan, J., Cole, T., Selsted, M.E., Homodimeric θ-defensins from Rhesus macaque leukocytes. Isolation, synthesis, antimicrobial activities, and bacterial binding properties of the cyclic peptides. J. Biol. Chem. 277 (2002), 3079–3084, 10.1074/jbc.M109117200.
269. [269] Leonova, L., Kokryakov, V.N., Aleshina, G., Hong, T., Nguyen, T., Zhao, C., et al. Circular minidefensins and posttranslational generation of molecular diversity. J. Leukoc. Biol. 70 (2001), 461–464.
270. [270] Yeaman, M.R., The role of platelets in antimicrobial host defense. Clin. Infect. Dis. 25 (1997), 951–968, 10.1086/516120 quiz 969–970.
271. [271] Ivanov, I.B., Gritsenko, G.A., Comparative activities of cattle and swine platelet microbicidal proteins. Probiotics Antimicrob. Proteins 1 (2009), 148–151, 10.1007/s12602-009-9016-9.
272. [272] Krijgsveld, J., Zaat, S.A., Meeldijk, J., van Veelen, P.A., Fang, G., Poolman, B., et al. Thrombocidins, microbicidal proteins from human blood platelets, are C-terminal deletion products of CXC chemokines. J. Biol. Chem. 275 (2000), 20374–20381, 10.1074/jbc.275.27.20374.
273. [273] Yeaman, M.R., Tang, Y.I.Q., Shen, A.J., Bayer, A.S., Selsted, M.E., Purification and in vitro activities of rabbit platelet microbicidal proteins. Infect. Immun. 65 (1997), 1023–1031.
274. [274] Krause, A., Neitz, S., Schulz, A., Forssmann, W., Schulz-knappe, P., Adermann, K., LEAP-1, a novel highly disulfide-bonded human peptide, exhibits antimicrobial activity. FEBS Lett. 480 (2000), 147–150.
275. [275] Park, C.H., Valore, E.V., Waring, A.J., Ganz, T., Hepcidin, a urinary antimicrobial peptide synthesized in the liver. J. Biol. Chem. 276 (2001), 7806–7810, 10.1074/jbc.M008922200.
276. [276] Krause, A., Sillard, R., Kleemeier, B., Klüver, E., Maronde, E., Conejo-García, J.R., et al. Isolation and biochemical characterization of LEAP-2, a novel blood peptide expressed in the liver. Protein Sci. 12 (2003), 143–152, 10.1110/ps.0213603.
277. [277] Schittek, B., Hipfel, R., Sauer, B., Bauer, J., Kalbacher, H., Stevanovic, S., et al. Dermcidin: a novel human antibiotic peptide secreted by sweat glands. Nat. Immunol. 2 (2001), 1133–1137, 10.1038/ni732.
278. [278] Schittek, B., The multiple facets of dermcidin in cell survival and host defense. J. Innate Immun. 4 (2012), 349–360, 10.1159/000336844.
279. [279] Li, Y., Recombinant production of antimicrobial peptides in Escherichia coli: a review. Protein Expr. Purif. 80 (2011), 260–267, 10.1016/j.pep.2011.08.001.
280. [280] Boman, H.G., Wade, D., Boman, I.A., Wåhlin, B., Merrifield, R.B., Antibacterial and antimalarial properties of peptides that are cecropin-melittin hybrids. FEBS Lett. 259 (1989), 103–106, 10.1016/0014-5793(89)81505-4.
281. [281] Merrifield, R.B., Juvvadi, P., Andreu, D., Ubach, J., Boman, A., Boman, H.G., Retro and retroenantio analogs of cecropin-melittin hybrids. Proc. Natl. Acad. Sci. U.S.A. 92 (1995), 3449–3453, 10.1073/pnas.92.8.3449.
282. [282] Andreu, D., Ubach, J., Boman, A., Wåhlin, B., Wade, D., Merrifield, R.B., et al. Shortened cecropin A-melittin hybrids significant size reduction retains potent antibiotic activity. FEBS Lett. 296 (1992), 190–194, 10.1016/0014-5793(92)80377-S.
283. [283] Oh, H., Hedberg, M., Wade, D., Edlund, C., Activities of synthetic hybrid peptides against anaerobic bacteria: aspects of methodology and stability. Antimicrob. Agents Chemother. 44 (2000), 68–72, 10.1128/AAC.44.1.68-72.2000.
284. [284] Badosa, E., Ferre, R., Planas, M., Feliu, L., Besalú, E., Cabrefiga, J., et al. A library of linear undecapeptides with bactericidal activity against phytopathogenic bacteria. Peptides 28 (2007), 2276–2285, 10.1016/j.peptides.2007.09.010.
285. [285] Ferre, R., Melo, M.N., Correia, A.D., Feliu, L., Bardaji, E., Planas, M., et al. Synergistic effects of the membrane actions of cecropin-melittin antimicrobial hybrid peptide BP100. Biophys. J. 96 (2009), 1815–1827, 10.1016/j.bpj.2008.11.053.
286. [286] Torcato, I.M., Huang, Y.-H., Franquelim, H.G., Gaspar, D., Craik, D.J., Castanho, M.A.R.B., et al. Design and characterization of novel antimicrobial peptides, R-BP100 and RW-BP100, with activity against Gram-negative and Gram-positive bacteria. Biochim. Biophys. Acta 2013 (1828), 944–955, 10.1016/j.bbamem.2012.12.002.
287. [287] Alves, C.S., Melo, M.N., Franquelim, H.G., Ferre, R., Planas, M., Feliu, L., et al. Escherichia coli cell surface perturbation and disruption induced by antimicrobial peptides BP100 and pepR. J. Biol. Chem. 285 (2010), 27536–27544, 10.1074/jbc.M110.130955.
288. [288] Jindal, H.M., Le, C.F., Mohd Yusof, M.Y., Velayuthan, R.D., Lee, V.S., Zain, S.M., et al. Antimicrobial activity of novel synthetic peptides derived from indolicidin and ranalexin against Streptococcus pneumoniae. PLoS One, 10, 2015, e0128532, 10.1371/journal.pone.0128532.
289. [289] Gottler, L.M., Ramamoorthy, A., Structure, membrane orientation, mechanism, and function of pexiganan – a highly potent antimicrobial peptide designed from magainin. Biochim. Biophys. Acta 1788 (2009), 1680–1686, 10.1016/j.bbamem.2008.10.009.
290. [290] Ge, Y., Macdonald, D.L., Holroyd, K.J., Thornsberry, C., Wexler, H., Zasloff, M., et al. In Vitro antibacterial properties of pexiganan, an analog of magainin. Antimicrob. Agents Chemother. 43 (1999), 782–788.
291. [291] Lipsky, B.A., Holroyd, K.J., Zasloff, M., Topical versus systemic antimicrobial therapy for treating mildly infected diabetic foot ulcers: a randomized, controlled, double-blinded, multicenter trial of pexiganan cream. Clin. Infect. Dis. 47 (2008), 1537–1545, 10.1086/593185.
292. [292] Helmerhorst, E.J., Van't Hof, W., Veerman, E.C., Simoons-Smit, I., Nieuw Amerongen, A.V., Synthetic histatin analogues with broad-spectrum antimicrobial activity. Biochem. J. 326 (1997), 39–45.
293. [293] Welling, M.M., Brouwer, C.P.J.M., van 't Hof, W., Veerman, E.C.I., Amerongen, A.V.N., Histatin-derived monomeric and dimeric synthetic peptides show strong bactericidal activity towards multidrug-resistant Staphylococcus aureus in vivo. Antimicrob. Agents Chemother. 51 (2007), 3416–3419, 10.1128/AAC.00196-07.
294. [294] Nielsen, S.L., Frimodt-møller, N., Kragelund, B.B., Hansen, P.R., Structure – activity study of the antibacterial peptide fallaxin. Protein Sci. 16 (2007), 1969–1976, 10.1110/ps.072966007.Protein.
295. [295] Gottschalk, S., Gottlieb, C.T., Vestergaard, M., Hansen, P.R., Gram, L., Ingmer, H., et al. The amphibian antimicrobial peptide fallaxin analogue, FL9, affects virulence gene expression and DNA replication in Staphylococcus aureus. J. Med. Microbiol. 9 (2015), 2052–2058, 10.1099/jmm.0.000177.
296. [296] Cantisani, M., Finamore, E., Mignogna, E., Falanga, A., Nicoletti, G.F., Pedone, C., et al. Structural insights into and activity analysis of the antimicrobial peptide myxinidin. Antimicrob. Agents Chemother. 58 (2014), 5280–5290, 10.1128/AAC.02395-14.
297. [297] Lee, D.L., Hodges, R.S., Structure-activity relationships of de novo designed cyclic antimicrobial peptides based on gramicidin S. Biopolym. Pept. Sci. Sect. 71 (2003), 28–48, 10.1002/bip.10374.
298. [298] Frecer, V., Ho, B., Ding, J., De novo design of potent antimicrobial peptides. Antimicrob. Agents Chemother. 48 (2004), 3349–3357, 10.1128/AAC.48.9.3349.
299. [299] Deslouches, B., Phadke, S.M., Lazarevic, V., Cascio, M., Islam, K., Montelaro, R.C., et al. De Novo generation of cationic antimicrobial peptides: influence of length and tryptophan substitution on antimicrobial activity. Antimicrob. Agents Chemother. 49 (2005), 316–322, 10.1128/AAC.49.1.316.
300. [300] Romani, A.A., Baroni, M.C., Taddei, S., Ghidini, F., Sansoni, P., Cavirani, S., et al. In vitro activity of novel in silico-developed antimicrobial peptides against a panel of bacterial pathogens. J. Pept. Sci. 19 (2013), 554–565, 10.1002/psc.2532.
301. [301] Makovitzki, A., Avrahami, D., Shai, Y., Ultrashort antibacterial and antifungal lipopeptides. Proc. Natl. Acad. Sci. U.S.A. 103 (2006), 15997–16002, 10.1073/pnas.0606129103.