Antifungal peptides in marine invertebrates

Invertebrate Survival Journal

Volumn 7, Issue 1, 2010, Pages 53-66

  Fusetani, Nobuhiro ^a  

^a HOKKAIDO UNIVERSITY   (Japan)

Author keywords

Antifungal activity; Antimicrobial peptide; Innate immunity; Marine invertebrate; Nonribosomal peptide

Indexed keywords

EID: 78649739334     PISSN: None     EISSN: 1824307X     Source Type: Journal    
DOI: None     Document Type: Review

References (81)

1. Andrä J, Hammer MU, Grötzinger J, Jakovkin I, Lindner B, Vollmer E, et al. Significance of the cyclic structure and of arginine residues for the antibacterial activity of arenicin-1 and its interaction with phospholipid and lipopolysaccharide model membranes. Biol. Chem. 390: 337-349, 2009.
2. Arenas G, Guzmán F, Cárdenas C, Mercado L, Marshall SH. A novel antifungal peptide designed from the primary structure of a natural antimicrobial peptide purified from Argopecten purpuratus hemocyes. Peptides 30: 1405-1411, 2009.
3. Azumi K, Yokosawa H, Ishii S. Halocyamines: novel antimicrobial tetrapeptide-like substances isolated from the hemocytes of the solitary ascidian Halocynthia roretzi. Biochemistry 29: 159-165, 1990.
4. Bachère E, Destoumieux D, Bulet P. Penaeidins, antimicrobial peptides of shrimp: a comparison with other effectors of innate immunity. Aquaculture 191: 71-88, 2000.
5. Bachère E, Gueguen Y, Gonzalez M, de Lorgeril J, Garnier J, Romestand B. Insights into the anti-microbial defense of marine invertebrates: the penaeid shrimps and the oyster Crassostrea gigas. Immunol. Rev. 198: 149-168, 2004.
6. Bewley CA, Debitus C, Faulkner DJ. Microsclerodermins A and B. Antifungal cyclic peptides from the lithistid sponge Microscleroderma sp. J. Am. Chem. Soc. 116: 7631-7636, 1994.
7. Bewley CA, Faulkner DJ. Theonegramide, an antifungal glycopeptide from the Philippine lithistid sponge Theonella swinhoei. J. Org. Chem. 59: 4849-4852, 1994.
8. Bewley CA, Faulkner DJ. Lithisthid sponges: star performers or hosts to the stars. Angew. Chem. int. Ed. 37: 2162-2178, 1998.
9. Blunt JW, Copp BR, Hu W-P, Munro MHG, Northcote PT, Prinsep MR. Marine natural products. Nat. Prod. Rep. 26:: 170-244, 2009 and the previous reviews of this series.
10. Brogden KA. Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria? Nat. Rev. Microbiol. 3: 238-250, 2005.
11. Bubb MR, Senderowicz AMJ, Sausville EA, Duncan KLK, Korn ED. Jasplakinolide, a cytotoxic natural product, induces actin polymerization and competitively inhibits the binding of phalloidin to F-actin. J. Biol. Chem. 269: 14869-14871, 1994.
12. Bulet, P, Stöcklin R, Menin L. Anti-microbial peptides: from invertebrates to vertebrates. Immunol. Rev. 198: 169-184, 2004.
13. Charlet M, Chernysh S, Philippe H, Hetru C, Hoffmann JA, Bulet P. Innate immunity. Isolation of several cysteine-rich antimicrobial peptides from the blood of a mollusc, Mytilus edulis. J. Biol. Chem. 271: 21808-21813, 1996.
14. Cimino G, Ghiselin MT. Marine natural products chemistry as an evolutionary narrative. In: McClintock JB, Baker BJ (eds), Marine chemical ecology, CRC Press, Boca Raton, USA, pp115-154, 2001.
15. Clark DP, Carroll J, Naylor S, Crews P. An antifungal cyclodepsipeptide, cyclolithistide A, from the sponge Theonella swinhoei. J. Org. Chem. 63: 8757-8764, 1998.
16. Cuthbertson BJ, Shepard EF, Chapman RW, Gross PS. Diversity of the penaeidin antimicrobial peptides in two shrimp species. Immunogenetics 54: 442-445, 2002.
17. Cuthbertson BJ, Yang Y, Bachère E, Büllesbach EE, Gross PS, Aumelas A. Solution structure of synthetic penaeidin-4 with structural and functional comparisons with penaeidin-3. J. Biol. Chem. 280: 16009-16018, 2005.
18. Destoumieux D, Bulet P, Loew D, van Dorsselaer A, Bachète E. Panaeidins, a new family of antimicrobial peptides isolated from the shrimp Panaeus vannamei (Decapoda). J. Biol. Chem. 272: 28398-28406, 1997.
19. Destoumieux D, Bulet P, Strub J-M, van Dorsselaer A, Rodriguez J, Bachète E. Recombinant expression and range of activity of penaeidins, antimicrobial peptides from penaeid shrimp. Eur. J. Biochem. 266: 335-346, 1999.
20. Destoumieux D, Munoz M, Bulet P, Bachète E. Penaeidins, a family of antimicrobial peptides from penaeid shrimp (Crustacea, Decapoda). Cell. Mol. Life Sci. 57: 1260-1271, 2000.
21. Fedders H, Leippe M. A reverse search for antimicrobial peptides in Ciona intestinalis: identification of a gene family expressed in hemocytes and evaluation of activity. Dev. Comp. Immunol. 32: 286-298, 2008.
22. Fedders H, Michalek M, Grötzinger J, Leippe M. An exceptional salt-tolerant antimicrobial peptide derived from a novel gene family of haemocytes of the marine invertebrate Ciona intestinalis. Biochem. J. 416: 65-75, 2008.
23. Fujitani N, Kawabata S, Osaki T, Kumaki Y, Demura M, Nitta K, et al. Structure of the antimicrobial peptide tachystatin A. J. Biol. Chem. 277: 23651-23657, 2002.
24. Fusetani N. Antifungal substances from marine invertebrates. Ann. NY Acad. Sci. 544: 113-127, 1988.
25. Fusetani N, Kem W. Marine toxins: an overview. In: Fusetani N, W. Kem (eds) Marine toxins as research tools, Springer-Verlag, Berlin, Germany, pp 1-44, 2009.
26. Fusetani N., Matsunaga S. Bioactive sponge peptides. Chem. Rev. 93: 1793-1806, 1993.
27. Garson MJ. Ecological perspectives on marine natural product biosynthesis. In: McClintock JB, Baker JB (eds), Marine chemical ecology, CRC Press, Boca Raton, USA, pp71-114, 2001.
28. Gonzalez M, Gueguen Y, Desserre G, de Lorgeril J, Romestand B, Bachère E. Molecular characterization of two isoforms of defensin from hemocytes of the oyster Crassostrea gigas. Dev. Comp. Immunol. 31: 332-339, 2007.
29. Gueguen Y, Garnier J, Robert L, Lefranc M-P, Mougenot I, de Lorgeril J, et al. PenBase, the shrimp antimicrobial peptide penaeidin database: sequence-based classification and recommended nomenclature. Dev. Comp. Immunol. 30: 283-288, 2006.
30. Gueguen Y, Herpin A, Aumelas A, Garnier J, Fievet J, Escoubas J-M, et al. Characterization of a defensin from the oyster Crassostrea gigas. Recombinant production, folding, solution structure, antimicrobial activities, and gene expression. J. Biol. Chem. 281: 313-323, 2006.
31. Gueguen Y, Romestand B, Fievet J, Schmitt P, Destoumieux-Garzon D, Vandenbulcke F, et al. Oyster hemocytes express a proline-rich peptide displaying synergistic amtimicrobial activity with a defensin. Mol. Immunol. 46: 516-522, 2009.
32. Hancock REW, Brown KL, Mookherjee N. Host defence peptides from invertebrates - emerging antimicrobial strategies. Immunobiology 211: 315-322, 2006.
33. Hirsch S, Miroz A, McCarthy P, Kashman Y. Etzionin, a new antifungal metabolite from a Red Sea tunicate. Tetrahedron Lett. 30: 4291-4294, 1989.
34. Iijima R, Kisugi J, Yamazaki M. A novel antimicrobial peptide from the sea hare Dolabella auricularia. Dev. Comp. Immunol. 27: 305-311, 2003.
35. Iwanaga S, Kawabata S, Muta T. New types of clotting factors and defense molecules found in horseshoe crab hemolymph: their structures and functions. J. Biochem. 123: 1-15, 1998.
36. Iwanaga, S, Lee BL. Recent advances in the innate immunity of invertebrates animals. J. Biochem. Mol. Biol. 38: 128-150, 2005.
37. Jenssen H, Hamill P, Hancock REW. Peptide antimicrobial agents. Clin. Microbiol Rev. 19: 491-511, 2006.
38. Kawabata S, Koshiba T, Shibata T. The lipopolysaccharide-activated innate immune response network of the horseshoe crab. Invert. Surv. J. 6: 59-77, 2009.
39. Kawabata, S, Nagayama R, Hirata M, Shigenaga T, Agarwala KL, Saito T, et al. Tachycitin, a small granular component in horseshoe crab hemocytes, is an antimicrobial protein with chitin-binding activity. J. Biochem. 120: 1253-1260, 1996.
40. Kobayashi, J, Tsuda M, Nakamura T, Mikami Y, Shigemori H. Hymenamides A and B, new proline-rich cyclic heptapeptides from the Okinawan marine sponge Hymeniacidon sp. Tetrahedron 49: 2391-2402, 1993.
41. Lee IH, Zhao C, Cho Y, Harwig SSL, Cooper EL, Lehrer RI. Clavanins, α-helical antimicrobial peptides from tunicate hemocytes. FEBS Lett. 400: 158-162, 1997.
42. Lee I-H, Zhao C, Nguyen T, Menzel L, Waring AJ, Sherman MA, Lehrer RI. Clavaspirin, an antibacterial and haemolytic peptide from Styela clava. J. Pept. Res. 58: 445-456, 2001.
43. Lehrer RI, Tincu JA, Taylor SW, Menzel LP, Waring AJ. Natural peptide antibiotics from tunicates: structures, functions and potential uses. Integr. Comp. Biol. 43: 313-322, 2003.
44. Li C, Haug T, Styrvold OB, Jørgensen TØ, Stensvåg K. Strongylocins, novel antimicrobial peptides from the green sea urchin, Strongylocentrotus droebachiensis. Dev. Comp. Immunol. 32: 1430-1440, 2008.
45. Li HY, Matsunaga S, Fusetani N. Antifungal metabolites from marine sponges. Curr. Org. Chem. 2: 649-682, 1998.
46. Matsunaga S, Fusetani N. Nonribosomal peptides from marine sponges. Curr. Org. Chem. 7: 945-966, 2003.
47. McIntosh JA, Donia MS, Schmidt EW. Ribosomal peptide natural products: bridging the ribosomal and nonribosomal worlds. Nat. Prod. Rep. 26: 537-559, 2009.
48. Milanowski DJ, Gustafson KR, Rashid MA, Pannell LK, McMahon JB, Boyd MR. Gymnangiamide, a cytotoxic pentapeptide from the marine hydroid Gymnangium regae. J. Org. Chem. 69: 3036-3042, 2004.
49. Mitta G, Hubert F, Noël T, Roch P. Myticin, a novel cysteine-rich antimicrobial peptide isolated from haemocytes and plasma of the mussel Mytilus galloprovincialis. Eur. J. Biochem. 265: 71-78, 1999a.
50. Mitta G, Vandenbulcke F, Hubert F, Roch P. Mussel defensins are synthesized and processed in granulocytes then released into the plasma after bacterial challenge. J. Cell Sci. 112: 4233-4242, 1999b.
51. Mitta G, Vandenbulcke F, Hubert F, Salzet M, Roch P. Involvement of mytilins in mussel antimicrobial defense. J. Biol. Chem. 275: 12954-12962, 2000.
52. 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: 663-668, 1989.
53. Molinski TF. Antifungal compounds from marine organisms. Anti-infect. Agents Med. Chem. 3: 197-220, 2004.
54. Müller WEG, Blumbach B, Müller IM. Evolution of the innate and adaptive immune systems: relationships between potential immune molecules in the lowest metazoan phylum (Porifera) and those in vertebrates. Transplantation 68: 1215-1227, 1999.
55. Mydlarz LD, Jones LE, Harvell CD. Innate immunity, environmental drivers, and disease ecology of marine and freshwater invertebrates. Annu. Rev. Ecol. Evol. Syst. 37: 251-288, 2006.
56. Nakamura T, Furunaka H, Miyata T, Tokunaga F, Muta T, Iwanaga S. 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.
57. Osaki T, Omotezako M, Nagayama R, Hirata M, Iwanaga S, Kasahara J, et al. Horseshoe crab hemocyte-derived antimicrobial polypeptides, tachystatins, with sequence similarity to spider neurotoxins. J. Biol. Chem. 274: 26172-26178, 1999.
58. Ovchinnikova TV, Aleshina GM, Balandin SV, Krasnosdembskaya AD, Markelov ML, Frolova EI, et al. Purification and primary structure of two isoforms of arenicin, a novel antimicrobial peptide from marine polychaeta Arenicola marina. FEBS Lett. 577: 209-214, 2004.
59. Ovchinnikova TV, Balandin SV, Aleshina GM, Tagaev AA, Leonova YF, Krasnodembsky EG, 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: 514-523, 2006.
60. Ovchinnikova TV, Shenkarev ZO, Nadezhdin KD, Balandin SV, Zhmak MN, Kudelina IA, et al. Recombinant expression, synthesis, purification, and solution structure of arenicin. Biochem. Biophys. Res. Commun. 360: 156-162, 2007.
61. Pan W, Liu X, Ge F, Han J, Zheng T. Perinerin, a novel antimicrobial peptide purified from the clamworm Perinereis aibuhitensis Grube and its partial characterization. J. Biochem. 135: 297-304, 2004.
62. Park C, Lee DG. Fungicidal effect of antimicrobial peptide arenicin-1. Biochim. Biophys. Acta 1788: 1790-1796, 2009.
63. Pettit RK, Pettit GR, Hazen KC. Specific activities of dolastatin 10 and peptide derivatives afainst Cryptococcus neoformans. Antimicrob. Agents Chemother. 42: 2961-2965, 1998.
64. Piel J. Metabolites from symbiotic bacteria. Nat. Prod. Rep. 21: 519-538, 2004.
65. Saito T, Kawabata S, Shigenaga T, Takayenoki Y, Cho J, Nakajima H, et al. A novel big defensin identified in horseshoe crab hemocyes: isolation, amino acid sequence, and antibacterial activity. J. Biochem. 117: 1131-1137, 1995.
66. Scott VR, Boehme R, Matthews TS. New class of antifungal agents: jasplakinolide, a cyclodepsipeptide from the marine sponge, Jaspis species. Antimicrob. Agents Chemother. 32: 1154-1157, 1988.
67. Shida K, Terajima D, Uchio R, Ikawa S, Ikeda M, Asano K, et al. Hemocytes of Ciona intestinalis express multiple genes involved in innate immune host defense. Biochem. Biophys. Res. Commun. 302: 207-218, 2003.
68. Shilabin AG, Kasanah N, Wedge DE, Hamann MT. Lysosome and HER3 (ErbB3) selective anticancer agent kahalalide F: semisynthetic modifications and antifungal lead-exploration studies. J. Med. Chem. 50: 4340-4350, 2007.
69. Smith VJ, Fernandes JMO, Kemp GD, Hauton C. Crustins: enigmatic WAP domain-containing antibacterial proteins from crustaceans. Dev. Comp. Immunol. 32: 758-772, 2008.
70. Sperstad SV, Haug T, Paulsen V, Rode TM, Strandskog G, Solem ST, et al. Characterization of crustins from the hemocytes of the spider crab, Hyas araneus, and the red king crab, Paralithodes camtschaticus. Dev. Comp. Immunol. 33: 583-591, 2009.
71. Sperstad SV, Haug T, Vasskog T, Stensvåg K. Hyastatin, a glycine-rich multi-domain antimicrobial peptide isolated from the spinder crab (Hya araneus) hemocytes. Mol. Immunol. 46: 2604-2612, 2009.
72. Sung WS, Park SH, Lee DG. Antimicrobial effect and membrane-active mechanism of urechistachykinins, neuropeptides derived from Urechis unicinctus. FEBS Lett. 582: 2463-2466, 2008.
73. Thakur NL, Hentschel U, Krasko A, Pabel CT, Anil AC, Müller WEG. Antibacterial activity of the sponge Suberites domuncula and its primmorphs: potential basis for epibacterial chemical defense. Aquat. Microb. Ecol. 31: 77-83, 2003.
74. Tincu JA, Taylor SW. Antimicrobial peptides from marine invertebrates. Antimicrob. Angents Chemother. 48: 3645-3654, 2004.
75. Wang G, Li X, Wang Z. APD2: the updated antimicrobial peptide database and its application in peptide design. Nucleic Acids Res. 37: D933-D937, 2009.
76. Yang Y-S, Mitta G, Chavanieu A, Calas B, Sanchez JF, Roch P et al. Solution structure and activity of the synthetic four-disulfide bond Mediterranean mussel defensin (MGD-1). Biochemistry 39: 14436-14447, 2000.
77. Yang YS, Poncet J, Garnier J, Zatylny C, Bachère E, Aumelas A. Solution structure of the recombinant penaeidin-3, a shrimp antimicrobial peptide. J. Biol. Chem. 278: 36859-36867, 2003.
78. Yeaman MR, Yount NY. Mechanisms of antimicrobial peptide action and resistance. Pharmacol. Rev. 55: 27-55, 2003.
79. Zampella A, D'Auria MV, Paloma LG, Casapullo A, Minale L, Debitus C, et al. Callipeltin A, an anti-HIV cyclic depsipeptide from the New Caledonian litisthida sponge Callipelta sp. J. Am. Chem. Soc. 118: 6202-6209, 1996.
80. Zasloff M. Antimicrobial peptides of multicellular organisms. Nature 415: 389-395, 2002.
81. Zhao J, Song L, Li C, Ni D, Wu L, Zhu L, et al. Molecular cloning, expression of a big defensin gene from bay scallop Argopecten irradians and the antimicrobial activity of its recombinant protein. Mol. Immunol. 44: 360-368, 2007.