Antimicrobial peptides in crustaceans

Invertebrate Survival Journal

Volumn 7, Issue 2, 2010, Pages 262-284

  Rosa, R D ^a   Barracco, Margherita A ^a  

^a FEDERAL UNIVERSITY OF SANTA CATARINA   (Brazil)

Author keywords

Antimicrobial peptides; Crustacean defense; Crustaceans; Decapods; Innate immunity

Indexed keywords

EID: 79960901109     PISSN: None     EISSN: 1824307X     Source Type: Journal    
DOI: None     Document Type: Review

References (157)

1. Aketagawa J, Miyata T, Ohtsubo S, Nakamura T, Morita T, Hayashida H, et al. Primary structure of limulus anticoagulant anti-lipopolysaccharide factor. J. Biol. Chem. 261: 7357-7365, 1986.
2. Amparyup P, Donpudsa S, Tassanakajon A. Shrimp single WAP domain (SWD)-containing protein exhibits proteinase inhibitory and antimicrobial activities. Dev. Comp. Immunol. 32: 1497-1509, 2008a.
3. Amparyup P, Kondo H, Hirono I, Aoki T, Tassanakajon A. Molecular cloning, genomic organization and recombinant expression of a crustin-like antimicrobial peptide from black tiger shrimp Penaeus monodon. Mol. Immunol. 45: 1085-1093, 2008b.
4. Antony SP, Bright Singh IS, Philip R. Molecular characterization of a crustin-like, putative antimicrobial peptide, Fi-crustin, from the Indian white shrimp, Fenneropenaeus indicus. Fish Shellfish Immunol. 28: 216-220, 2010.
5. Bachère E, Destoumieux D, Bulet P. Penaeidins, antimicrobial peptides of shrimp: a comparison with other effectors of innate immunity. Aquaculture 191: 71-88, 2000.
6. 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.
7. Bartlett TC, Cuthbertson BJ, Shepard EF, Chapman RW, Gross PS, Warr GW. Crustins, homologues of an 11. 5-kDa antibacterial peptide, from two species of penaeid shrimp, Litopenaeus vannamei and Litopenaeus setiferus. Mar. Biotechnol. (NY) 4: 278-293, 2002.
8. Battison AL, Summerfield R, Patrzykat A. Isolation and characterization of two antimicrobial peptides from haemocytes of the American lobster Homarus americanus. Fish Shellfish Immunol. 25: 181-187, 2008.
9. Beale KM, Towle DW, Jayasundara N, Smith CM, Shields JD, Small HJ, et al. Anti-lipopolysaccharide factors in the American lobster Homarus americanus: molecular characterization and transcriptional response to Vibrio fluvialis challenge. Comp. Biochem. Physiol. 3D: 263-269, 2008.
10. Bowdish DM, Davidson DJ, Hancock RE. A re-evaluation of the role of host defense peptides in mammalian immunity. Curr. Protein Pept. Sci. 6: 35-51, 2005.
11. Brockton V, Hammond JA, Smith VJ. Gene characterization, isoforms and recombinant expression of carcinin, an antibacterial protein from the shore crab, Carcinus maenas. Mol. Immunol. 44: 943-949, 2007.
12. Brogden KA. Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria? Nat. Rev. Microbiol. 3: 238-250, 2005.
13. Brown KL, Hancock RE. Cationic host defense (antimicrobial) peptides. Curr. Opin. Immunol. 18: 24-30, 2006.
14. Bulet P, Cociancich S, Dimarcq JL, Lambert J, Reichhart JM, Hoffmann D, et al. Insect immunity. Isolation from a coleopteran insect of a novel inducible antibacterial peptide and of new members of the insect defensin family. J. Biol. Chem. 266: 24520-24525, 1991.
15. Bulet P, Stöcklin R. Insect antimicrobial peptides: structures, properties and gene regulation. Protein Pept. Lett. 12: 3-11, 2005.
16. Bulet P, Stöcklin R, Menin L. Anti-microbial peptides: from invertebrates to vertebrates. Immunol. Rev. 198: 169-184, 2004.
17. Capone R, Mustata M, Jang H, Arce FT, Nussinov R, Lal R. Antimicrobial protegrin-1 forms ion channels: molecular dynamic simulation, atomic force microscopy, and electrical conductance studies. Biophys. J. 98: 2644-2652, 2010.
18. Carriel-Gomes MC, Kratz JM, Barracco MA, Bachère E, Barardi CR, Simões CM. In vitro antiviral activity of antimicrobial peptides against herpes simplex virus 1, adenovirus, and rotavirus. Mem. Inst. Oswaldo Cruz. 102: 469-472, 2007.
19. Cerenius L, Lee BL, Söderhäll K. The proPO-system: pros and cons for its role in invertebrate immunity. Trends Immunol. 29: 263-271, 2008.
20. Cerenius L, Söderhäll K. The prophenoloxidase-activating system in invertebrates. Immunol. Rev. 198: 116-126, 2004.
21. Chen D, He N, Xu X. Mj-DWD, a double WAP domain-containing protein with antiviral relevance in Marsupenaeus japonicus. Fish Shellfish Immunol. 25: 775-781, 2008.
22. Chernysh S, Cociancich S, Briand JP, Hetru C, Bulet P. The inducible antibacterial peptides of the hemipteran insect Palomena prasina: Identification of a unique family of prolinerich peptides and of a novel insect defensin. J. Insect Physiol. 42: 81-89, 1996.
23. Chiou TT, Lu JK, Wu JL, Chen TT, Ko CF, Chen JC. Expression and characterization of tiger shrimp Penaeus monodon penaeidin (mo-penaeidin) in various tissues, during early embryonic development and moulting stages. Dev. Comp. Immunol. 31: 132-142, 2007.
24. Cho JH, Sung BH, Kim SC. Buforins: histone H2A-derived antimicrobial peptides from toad stomach. Biochim. Biophys. Acta 1788: 1564-1569, 2009.
25. Christie AE, Rus S, Goiney CC, Smith CM, Towle DW, Dickinson PS. Identification and characterization of a cDNA encoding a crustin-like, putative antibacterial protein from the American lobster Homarus americanus. Mol. Immunol. 44: 3333-3337, 2007.
26. Conlon JM. The contribution of skin antimicrobial peptides to the system of innate immunity in anurans. Cell Tissue Res. 2010.
27. Cuthbertson BJ, Bullesbach EE, Fievet J, Bachère E, Gross PS. A new class (penaeidin class 4) of antimicrobial peptides from the Atlantic white shrimp (Litopenaeus setiferus) exhibits target specificity and an independent proline-rich-domain function. Biochem. J. 381: 79-86, 2004.
28. Cuthbertson BJ, Bullesbach EE, Gross PS. Discovery of synthetic penaeidin activity against antibiotic-resistant fungi. Chem. Biol. Drug Des. 68: 120-127, 2006.
29. Cuthbertson BJ, Deterding LJ, Williams JG, Tomer KB, Etienne K, Blackshear PJ, et al. Diversity in penaeidin antimicrobial peptide form and function. Dev. Comp. Immunol. 32: 167-181, 2008.
30. Cuthbertson BJ, Shepard EF, Chapman RW, Gross PS. Diversity of the penaeidin antimicrobial peptides in two shrimp species. Immunogenetics 54: 442-445, 2002.
31. Cuthbertson BJ, Yang Y, Bachère E, Bullesbach 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.
32. Dai ZM, Zhu XJ, Yang WJ. Full-length normalization subtractive hybridization: a novel method for generating differentially expressed cDNAs. Mol. Biotechnol. 43: 257-263, 2009.
33. de la Vega E, O'Leary NA, Shockey JE, Robalino J, Payne C, Browdy CL, et al. Anti-lipopolysaccharide factor in Litopenaeus vannamei (LvALF): a broad spectrum antimicrobial peptide essential for shrimp immunity against bacterial and fungal infection. Mol. Immunol. 45: 1916-1925, 2008.
34. de Lorgeril J, Gueguen Y, Goarant C, Goyard E, Mugnier C, Fievet J, et al. A relationship between antimicrobial peptide gene expression and capacity of a selected shrimp line to survive a Vibrio infection. Mol. Immunol. 45: 3438-3445, 2008.
35. de Lorgeril J, Saulnier D, Janech MG, Gueguen Y, Bachère E. Identification of genes that are differentially expressed in hemocytes of the Pacific blue shrimp (Litopenaeus stylirostris) surviving an infection with Vibrio penaeicida. Physiol. Genomics 21: 174-183, 2005.
36. Decker H, Jaenicke E. Recent findings on phenoloxidase activity and antimicrobial activity of hemocyanins. Dev. Comp. Immunol. 28: 673-687, 2004.
37. Decker H, Rimke T. Tarantula hemocyanin shows phenoloxidase activity. J. Biol. Chem. 273: 25889-25892, 1998.
38. Destoumieux-Garzón D, Saulnier D, Garnier J, Jouffrey C, Bulet P, Bachère E. Crustacean immunity. Antifungal peptides are generated from the C terminus of shrimp hemocyanin in response to microbial challenge. J. Biol. Chem. 276: 47070-47077, 2001.
39. Destoumieux D, Bulet P, Loew D, Van Dorsselaer A, Rodriguez J, Bachère E. Penaeidins, a new family of antimicrobial peptides isolated from the shrimp Penaeus vannamei (Decapoda). J. Biol. Chem. 272: 28398-28406, 1997.
40. Destoumieux D, Bulet P, Strub JM, Van Dorsselaer A, Bachère E. Recombinant expression and range of activity of penaeidins, antimicrobial peptides from penaeid shrimp. Eur. J. Biochem. 266: 335-346, 1999.
41. Destoumieux D, Muñoz M, Bulet P, Bachère E. Penaeidins, a family of antimicrobial peptides from penaeid shrimp (Crustacea, Decapoda). Cell. Mol. Life Sci. 57: 1260-1271, 2000a.
42. Destoumieux D, Muñoz M, Cosseau C, Rodriguez J, Bulet P, Comps M, et al. Penaeidins, antimicrobial peptides with chitin-binding activity, are produced and stored in shrimp granulocytes and released after microbial challenge. J Cell Sci. 113 (Pt 3): 461-469, 2000b.
43. Dong B, Xiang JH. Discovery of genes involved in defense/immunity functions in a haemocytes cDNA library from Fenneropenaeus chinensis by ESTs annotation. Aquaculture 272: 208-215, 2007.
44. Du ZQ, Li XC, Wang ZH, Zhao XF, Wang JX. A single WAP domain (SWD)-containing protein with antipathogenic relevance in red swamp crayfish, Procambarus clarkii. Fish Shellfish Immunol. 28: 134-142, 2010.
45. Du ZQ, Ren Q, Zhao XF, Wang JX. A double WAP domain (DWD)-containing protein with proteinase inhibitory activity in Chinese white shrimp, Fenneropenaeus chinensis. Comp. Biochem. Physiol. 154B: 203-210, 2009.
46. Easton DM, Nijnik A, Mayer ML, Hancock RE. Potential of immunomodulatory host defense peptides as novel anti-infectives. Trends Biotechnol. 27: 582-590, 2009.
47. Fernandes JM, Kemp GD, Molle MG, Smith VJ. Anti-microbial properties of histone H2A from skin secretions of rainbow trout, Oncorhynchus mykiss. Biochem. J. 368: 611-620, 2002.
48. Fernandes JM, Molle G, Kemp GD, Smith VJ. Isolation and characterization of oncorhyncin II, a histone H1-derived antimicrobial peptide from skin secretions of rainbow trout, Oncorhynchus mykiss. Dev. Comp. Immunol. 28: 127-138, 2004.
49. Frank RW, Gennaro R, Schneider K, Przybylski M, Romeo D. Amino acid sequences of two proline-rich bactenecins. Antimicrobial peptides of bovine neutrophils. J. Biol. Chem. 265: 18871-18874, 1990.
50. Gil-Turnes MS, Hay ME, Fenical W. Symbiotic marine bacteria chemically defend crustacean embryos from a pathogenic fungus. Science 246: 116-118, 1989.
51. Gross PS, Bartlett TC, Browdy CL, Chapman RW, Warr GW. Immune gene discovery by expressed sequence tag analysis of hemocytes and hepatopancreas in the Pacific White Shrimp, Litopenaeus vannamei, and the Atlantic White Shrimp, L. setiferus. Dev. Comp. Immunol. 25: 565-577, 2001.
52. Guaní-Guerra E, Santos-Mendoza T, Lugo-Reyes SO, Terán LM. Antimicrobial peptides: general overview and clinical implications in human health and disease. Clin. Immunol. 135: 1-11, 2010.
53. Gueguen Y, Garnier J, Robert L, Lefranc MP, 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.
54. Hagiwara K, Kikuchi T, Endo Y, Huqun, Usui K, Takahashi M, et al. Mouse SWAM1 and SWAM2 are antibacterial proteins composed of a single whey acidic protein motif. J. Immunol. 170: 1973-1979, 2003.
55. Hale JD, Hancock RE. Alternative mechanisms of action of cationic antimicrobial peptides on bacteria. Expert Rev. Anti. Infect. Ther. 5: 951-959, 2007.
56. Hancock RE, Scott MG. The role of antimicrobial peptides in animal defenses. Proc. Natl. Acad. Sci. USA 97: 8856-8861, 2000.
57. Hauton C, Brockton V, Smith VJ. Cloning of a crustin-like, single whey-acidic-domain, antibacterial peptide from the haemocytes of the European lobster, Homarus gammarus, and its response to infection with bacteria. Mol. Immunol. 43: 1490-1496, 2006.
58. Herbinière J, Braquart-Varnier C, Greve P, Strub JM, Frere J, Van Dorsselaer A, et al. Armadillidin: a novel glycine-rich antibacterial peptide directed against gram-positive bacteria in the woodlouse Armadillidium vulgare (Terrestrial Isopod, Crustacean). Dev. Comp. Immunol. 29: 489-499, 2005.
59. Hoess A, Watson S, Siber GR, Liddington R. Crystal structure of an endotoxin-neutralizing protein from the horseshoe crab, Limulus anti-LPS factor, at 1. 5 A resolution. EMBO J. 12: 3351-3356, 1993.
60. Huang WS, Wang KJ, Yang M, Cai JJ, Li SJ, Wang GZ. Purification and part characterization of a novel antibacterial protein Scygonadin, isolated from the seminal plasma of mud crab, Scylla serrata (Forskål, 1775). J. Exp. Mar. Biol. Ecol. 339: 37-42, 2006.
61. Imjongjirak C, Amparyup P, Tassanakajon A, Sittipraneed S. Antilipopolysaccharide factor (ALF) of mud crab Scylla paramamosain: molecular cloning, genomic organization and the antimicrobial activity of its synthetic LPS binding domain. Mol. Immunol. 44: 3195-3203, 2007.
62. Imjongjirak C, Amparyup P, Tassanakajon A, Sittipraneed S. Molecular cloning and characterization of crustin from mud crab Scylla paramamosain. Mol. Biol. Rep. 36: 841-850, 2009.
63. Iwanaga S. The molecular basis of innate immunity in the horseshoe crab. Curr. Opin. Immunol. 14: 87-95, 2002.
64. Iwanaga S, Lee BL. Recent advances in the innate immunity of invertebrate animals. J. Biochem. Mol. Biol. 38: 128-150, 2005.
65. Jia YP, Sun YD, Wang ZH, Wang Q, Wang XW, Zhao XF, et al. A single whey acidic protein domain (SWD)-containing peptide from fleshy prawn with antimicrobial and proteinase inhibitory activities. Aquaculture 284: 246-259, 2008.
66. Jiménez-Vega F, Vargas-Albores F. A secretory leukocyte proteinase inhibitor (SLPI)-like protein from Litopenaeus vannamei haemocytes. Fish Shellfish Immunol. 23: 1119-1126, 2007.
67. Jiménez-Vega F, Yepiz-Plascencia G, Söderhäll K, Vargas-Albores F. A single WAP domain-containing protein from Litopenaeus vannamei hemocytes. Biochem. Biophys. Res. Commun. 314: 681-687, 2004.
68. Jiravanichpaisal P, Lee BL, Söderhäll K. Cell-mediated immunity in arthropods: hematopoiesis, coagulation, melanization and opsonization. Immunobiology 211: 213-236, 2006.
69. Jiravanichpaisal P, Lee SY, Kim YA, Andren T, Söderhäll I. Antibacterial peptides in hemocytes and hematopoietic tissue from freshwater crayfish Pacifastacus leniusculus: characterization and expression pattern. Dev. Comp. Immunol. 31: 441-455, 2007a.
70. Jiravanichpaisal P, Puanglarp N, Petkon S, Donnuea S, Söderhäll I, Söderhäll K. Expression of immune-related genes in larval stages of the giant tiger shrimp, Penaeus monodon. Fish Shellfish Immunol. 23: 815-824, 2007b.
71. Kamysz W, Okroj M, Lukasiak J. Novel properties of antimicrobial peptides. Acta Biochim. Pol. 50: 461-469, 2003.
72. Kang CJ, Xue JF, Liu N, Zhao XF, Wang JX. Characterization and expression of a new subfamily member of penaeidin antimicrobial peptides (penaeidin 5) from Fenneropenaeus chinensis. Mol Immunol. 44: 1535-1543, 2007.
73. Kashima M. H1 histones contribute to candidacidal activities of human epidermal extract. J. Dermatol. 18: 695-706, 1991.
74. Kawabata S, Koshiba T, Shibata T. The lipopolysaccharide-activated innate immune response network of the horseshoe crab. Inv. Surv. J. 6: 59-77, 2009.
75. Khoo L, Robinette DW, Noga EJ. Callinectin, an antibacterial peptide from blue crab, Callinectes sapidus, hemocytes. Mar. Biotechnol. (NY) 1: 44-51, 1999.
76. Lai Y, Gallo RL. AMPed up immunity: how antimicrobial peptides have multiple roles in immune defense. Trends Immunol. 30: 131-141, 2009.
77. Lee IH, Cho Y, Lehrer RI. Effects of pH and salinity on the antimicrobial properties of clavanins. Infect. Immun. 65: 2898-2903, 1997.
78. Lee SY, Lee BL, Söderhäll K. Processing of an antibacterial peptide from hemocyanin of the freshwater crayfish Pacifastacus leniusculus. J. Biol. Chem. 278: 7927-7933, 2003.
79. Li C, Zhao J, Song L, Mu C, Zhang H, Gai Y, et al. Molecular cloning, genomic organization and functional analysis of an anti-lipopolysaccharide factor from Chinese mitten crab Eriocheir sinensis. Dev. Comp. Immunol. 32: 784-794, 2008.
80. Li L, Wang JX, Zhao XF, Kang CJ, Liu N, Xiang JH, et al. High level expression, purification, and characterization of the shrimp antimicrobial peptide, Ch-penaeidin, in Pichia pastoris. Protein Exp. Purif. 39: 144-151, 2005.
81. Liu F, Liu Y, Li F, Dong B, Xiang J. Molecular cloning and expression profile of putative antilipopolysaccharide factor in Chinese shrimp (Fenneropenaeus chinensis). Mar. Biotechnol. (NY) 7: 600-608, 2005.
82. Liu H, Jiravanichpaisal P, Söderhäll I, Cerenius L, Söderhäll K. Antilipopolysaccharide factor interferes with white spot syndrome virus replication in vitro and in vivo in the crayfish Pacifastacus leniusculus. J. Virol. 80: 10365-10371, 2006.
83. Löfgren SE, Smânia A, Smânia EFA, Bachère E, Barracco MA. Comparative activity and stability under salinity conditions of different antimicrobial peptides isolated from aquatic animals. Aquaculture Res. 40: 1805-1812, 2009.
84. Lorenzini DM, da Silva PIJ, Fogaca AC, Bulet P, Daffre S. Acanthoscurrin: a novel glycine-rich antimicrobial peptide constitutively expressed in the hemocytes of the spider Acanthoscurria gomesiana. Dev. Comp. Immunol. 27: 781-791, 2003.
85. Lu KY, Sung HJ, Liu CL, Sung HH. Differentially enhanced gene expression in hemocytes from Macrobrachium rosenbergii challenged in vivo with lipopolysaccharide. J. Invertebr. Pathol. 100: 9-15, 2009.
86. Mangoni ML. Temporins, anti-infective peptides with expanding properties. Cell. Mol. Life Sci. 63: 1060-1069, 2006.
87. McTaggart SJ, Conlon C, Colbourne JK, Blaxter ML, Little TJ. The components of the Daphnia pulex immune system as revealed by complete genome sequencing. BMC Genomics 10: 175, 2009.
88. Morita T, Ohtsubo S, Nakamura T, Tanaka S, Iwanaga S, Ohashi K, et al. Isolation and biological activities of limulus anticoagulant (anti-LPS factor) which interacts with lipopolysaccharide (LPS). J. Biochem. 97: 1611-1620, 1985.
89. Mu C, Zheng P, Zhao J, Wang L, Zhang H, Qiu L, et al. Molecular characterization and expression of a crustin-like gene from Chinese mitten crab, Eriocheir sinensis. Dev. Comp. Immunol. 34: 734-740, 2010.
90. Muñoz M, Vandenbulcke F, Garnier J, Gueguen Y, Bulet P, Saulnier D, et al. Involvement of penaeidins in defense reactions of the shrimp Litopenaeus stylirostris to a pathogenic vibrio. Cell. Mol. Life Sci. 61: 961-972, 2004.
91. Muñoz M, Vandenbulcke F, Gueguen Y, Bachère E. Expression of penaeidin antimicrobial peptides in early larval stages of the shrimp Penaeus vannamei. Dev. Comp. Immunol. 27: 283-289, 2003.
92. Muñoz M, Vandenbulcke F, Saulnier D, Bachère E. Expression and distribution of penaeidin antimicrobial peptides are regulated by haemocyte reactions in microbial challenged shrimp. Eur. J. Biochem. 269: 2678-2689, 2002.
93. Muta T, Miyata T, Tokunaga F, Nakamura T, Iwanaga S. Primary structure of anti-lipopolysaccharide factor from American horseshoe crab, Limulus polyphemus. J. Biochem. 101: 1321-1330, 1987.
94. Nagai T, Kawabata S. A link between blood coagulation and prophenol oxidase activation in arthropod host defense. J. Biol. Chem. 275: 29264-29267, 2000.
95. Nagoshi H, Inagawa H, Morii K, Harada H, Kohchi C, Nishizawa T, et al. Cloning and characterization of a LPS-regulatory gene having an LPS binding domain in kuruma prawn Marsupenaeus japonicus. Mol. Immunol. 43: 2061-2069, 2006.
96. Nicolas P. Multifunctional host defense peptides: intracellular-targeting antimicrobial peptides. FEBS J. 276: 6483-6496, 2009.
97. O'Leary NA, Gross PS. Genomic structure and transcriptional regulation of the penaeidin gene family from Litopenaeus vannamei. Gene 371: 75-83, 2006.
98. Park IY, Park CB, Kim MS, Kim SC. Parasin I, an antimicrobial peptide derived from histone H2A in the catfish, Parasilurus asotus. FEBS Lett. 437: 258-262, 1998.
99. Patat SA, Carnegie RB, Kingsbury C, Gross PS, Chapman R, Schey KL. Antimicrobial activity of histones from hemocytes of the Pacific white shrimp. Eur. J. Biochem. 271: 4825-4833, 2004.
100. Pazgier M, Hoover DM, Yang D, Lu W, Lubkowski J. Human beta-defensins. Cell. Mol. Life Sci. 63: 1294-1313, 2006.
101. Peng H, Yang M, Huang WS, Ding J, Qu HD, Cai JJ, et al. Soluble expression and purification of a crab antimicrobial peptide scygonadin in different expression plasmids and analysis of its antimicrobial activity. Protein Exp. Purif. 70: 109-115, 2010.
102. Pisuttharachai D, Fagutao FF, Yasuike M, Aono H, Yano Y, Murakami K, et al. Characterization of crustin antimicrobial proteins from Japanese spiny lobster Panulirus japonicus. Dev. Comp. Immunol. 33: 1049-1054, 2009c.
103. Pisuttharachai D, Yasuike M, Aono H, Murakami K, Kondo H, Aoki T, et al. Expressed sequence tag analysis of phyllosomas and hemocytes of Japanese spiny lobster Panulirus japonicus. Fish Sci. 75: 195-206, 2009a.
104. Pisuttharachai D, Yasuike M, Aono H, Yano Y, Murakami K, Kondo H, et al. Characterization of two isoforms of Japanese spiny lobster Panulirus japonicus defensin cDNA. Dev. Comp. Immunol. 33: 434-438, 2009b.
105. Ranganathan S, Simpson KJ, Shaw DC, Nicholas KR. The whey acidic protein family: a new signature motif and three-dimensional structure by comparative modeling. J. Mol. Graph. Model 17: 106-113, 134-106, 1999.
106. Rattanachai A, Hirono I, Ohira T, Takahashi Y, Aoki T. Cloning of kuruma prawn Marsupenaeus japonicus crustin-like peptide cDNA and analysis of its expression. Fish Sci. 70: 765-771, 2004.
107. Relf JM, Chisholm JR, Kemp GD, Smith VJ. Purification and characterization of a cysteine-rich 11. 5-kDa antibacterial protein from the granular haemocytes of the shore crab, Carcinus maenas. Eur. J. Biochem. 264: 350-357, 1999.
108. Richards RC, O'Neil DB, Thibault P, Ewart KV. Histone H1: an antimicrobial protein of Atlantic salmon (Salmo salar). Biochem. Biophys. Res. Commun. 284: 549-555, 2001.
109. Robalino J, Almeida JS, McKillen D, Colglazier J, Trent HF, 3rd, Chen YA, et al. Insights into the immune transcriptome of the shrimp Litopenaeus vannamei: tissue-specific expression profiles and transcriptomic responses to immune challenge. Physiol. Genomics 29: 44-56, 2007.
110. Robalino J, Carnegie RB, O'Leary N, Ouvry-Patat SA, de la Vega E, Prior S, et al. Contributions of functional genomics and proteomics to the study of immune responses in the Pacific white leg shrimp Litopenaeus vannamei. Vet. Immunol. Immunopathol. 128: 110-118, 2009.
111. Robinette D, Wada S, Arroll T, Levy MG, Miller WL, Noga EJ. Antimicrobial activity in the skin of the channel catfish Ictalurus punctatus: characterization of broad-spectrum histone-like antimicrobial proteins. Cell. Mol. Life Sci. 54: 467-475, 1998.
112. Rojtinnakorn J, Hirono I, Itami T, Takahashi Y, Aoki T. Gene expression in haemocytes of kuruma prawn, Penaeus japonicus, in response to infection with WSSV by EST approach. Fish Shellfish Immunol. 13: 69-83, 2002.
113. Rolland JL, Abdelouahab M, Dupont J, Lefevre F, Bachère E, Romestand B. Stylicins, a new family of antimicrobial peptides from the Pacific blue shrimp Litopenaeus stylirostris. Mol. Immunol. 47: 1269-1277, 2010.
114. Rosa RD, Bandeira PT, Barracco MA. Molecular cloning of crustins from the hemocytes of Brazilian penaeid shrimps. FEMS Microbiol. Lett. 274: 287-290, 2007.
115. Rosa RD, Stoco PH, Barracco MA. Cloning and characterization of cDNA sequences encoding for anti-lipopolysaccharide factors (ALFs) in Brazilian palaemonid and penaeid shrimps. Fish Shellfish Immunol. 25: 693-696, 2008.
116. Saito T, Kawabata S, Shigenaga T, Takayenoki Y, Cho J, Nakajima H, et al. A novel big defensin identified in horseshoe crab hemocytes: isolation, amino acid sequence, and antibacterial activity. J. Biochem. 117: 1131-1137, 1995.
117. Salditt T, Li C, Spaar A. Structure of antimicrobial peptides and lipid membranes probed by interface-sensitive X-ray scattering. Biochim. Biophys. Acta 1758: 1483-1498, 2006.
118. Schnapp D, Kemp GD, Smith VJ. 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.
119. Shi XZ, Zhang RR, Jia YP, Zhao XF, Yu XQ, Wang JX. Identification and molecular characterization of a Spatzle-like protein from Chinese shrimp (Fenneropenaeus chinensis). Fish Shellfish Immunol. 27: 610-617, 2009.
120. Shockey JE, O'Leary NA, de la Vega E, Browdy CL, Baatz JE, Gross PS. The role of crustins in Litopenaeus vannamei in response to infection with shrimp pathogens: An in vivo approach. Dev. Comp. Immunol. 33: 668-673, 2009.
121. Simmaco M, Mignogna G, Canofeni S, Miele R, Mangoni ML, Barra D. Temporins, antimicrobial peptides from the European red frog Rana temporaria. Eur. J. Biochem. 242: 788-792, 1996.
122. Smith VJ, Desbois AP, Dyrynda EA. Conventional and unconventional antimicrobials from fish, marine invertebrates and micro-algae. Mar. Drugs 8: 1213-1262, 2010.
123. Smith VJ, Fernandes JM, Kemp GD, Hauton C. Crustins: enigmatic WAP domain-containing antibacterial proteins from crustaceans. Dev. Comp. Immunol. 32: 758-772, 2008.
124. Somboonwiwat K, Bachère E, Rimphanitchayakit V, Tassanakajon A. Localization of anti-lipopolysaccharide factor (ALFPm3) in tissues of the black tiger shrimp, Penaeus monodon, and characterization of its binding properties. Dev. Comp. Immunol. 32: 1170-1176, 2008.
125. Somboonwiwat K, Marcos M, Tassanakajon A, Klinbunga S, Aumelas A, Romestand B, et al. Recombinant expression and anti-microbial activity of anti-lipopolysaccharide factor (ALF) from the black tiger shrimp Penaeus monodon. Dev. Comp. Immunol. 29: 841-851, 2005.
126. 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, 2009a.
127. Sperstad SV, Haug T, Vasskog T, Stensvåg K. Hyastatin, a glycine-rich multi-domain antimicrobial peptide isolated from the spider crab (Hyas araneus) hemocytes. Mol. Immunol. 46: 2604-2612, 2009b.
128. Sperstad SV, Smith VJ, Stensvåg K. Expression of antimicrobial peptides from Hyas araneus haemocytes following bacterial challenge in vitro. Dev. Comp. Immunol. 34: 618-624, 2010.
129. Stensvåg K, Haug T, Sperstad SV, Rekdal O, Indrevoll B, Styrvold OB. Arasin 1, a proline-arginine-rich antimicrobial peptide isolated from the spider crab, Hyas araneus. Dev. Comp. Immunol. 32: 275-285, 2008.
130. Stoss TD, Nickell MD, Hardin D, Derby CD, McClintock TS. Inducible transcript expressed by reactive epithelial cells at sites of olfactory sensory neuron proliferation. J. Neurobiol. 58: 355-368, 2004.
131. Sun C, Du XJ, Xu WT, Zhang HW, Zhao XF, Wang JX. Molecular cloning and characterization of three crustins from the Chinese white shrimp, Fenneropenaeus chinensis. Fish Shellfish Immunol. 28: 517-524, 2010.
132. Supungul P, Klinbunga S, Pichyangkura R, Hirono I, Aoki T, Tassanakajon A. Antimicrobial peptides discovered in the black tiger shrimp Penaeus monodon using the EST approach. Dis. Aquat. Organ 61: 123-135, 2004.
133. Supungul P, Klinbunga S, Pichyangkura R, Jitrapakdee S, Hirono I, Aoki T, et al. Identification of immune-related genes in hemocytes of black tiger shrimp (Penaeus monodon). Mar. Biotechnol. (NY) 4: 487-494, 2002.
134. Supungul P, Tang S, Maneeruttanarungroj C, Rimphanitchayakit V, Hirono I, Aoki T, et al. Cloning, expression and antimicrobial activity of crustinPm1, a major isoform of crustin, from the black tiger shrimp Penaeus monodon. Dev. Comp. Immunol. 32: 61-70, 2008.
135. Tanaka S, Nakamura T, Morita T, Iwanaga S. Limulus anti-LPS factor: an anticoagulant which inhibits the endotoxin mediated activation of Limulus coagulation system. Biochem. Biophys. Res. Commun. 105: 717-723, 1982.
136. Tassanakajon A, Amparyup P, Somboonwiwat K, Supungul P. Cationic Antimicrobial Peptides in Penaeid Shrimp. Mar. Biotechnol. (NY), 2010 [Epub ahead of print].
137. Tassanakajon A, Klinbunga S, Paunglarp N, Rimphanitchayakit V, Udomkit A, Jitrapakdee S, et al. Penaeus monodon gene discovery project: the generation of an EST collection and establishment of a database. Gene 384: 104-112, 2006.
138. Taylor K, Barran PE, Dorin JR. Structure-activity relationships in beta-defensin peptides. Biopolymers 90: 1-7, 2008.
139. Tharntada S, Ponprateep S, Somboonwiwat K, Liu H, Söderhäll I, Söderhäll K, et al. Role of anti-lipopolysaccharide factor from the black tiger shrimp, Penaeus monodon, in protection from white spot syndrome virus infection. J. Gen. Virol. 90: 1491-1498, 2009.
140. Tharntada S, Somboonwiwat K, Rimphanitchayakit V, Tassanakajon A. Anti-lipopolysaccharide factors from the black tiger shrimp, Penaeus monodon, are encoded by two genomic loci. Fish Shellfish Immunol. 24: 46-54, 2008.
141. Theopold U, Schmidt O, Söderhäll K, Dushay MS. Coagulation in arthropods: defense, wound closure and healing. Trends Immunol. 25: 289-294, 2004.
142. Thomas S, Karnik S, Barai RS, Jayaraman VK, Idicula-Thomas S. CAMP: a useful resource for research on antimicrobial peptides. Nucleic Acids Res. 38: D774-780, 2010.
143. Tossi A, Sandri L. Molecular diversity in gene-encoded, cationic antimicrobial polypeptides. Curr. Pharm. Des. 8: 743-761, 2002.
144. van Holde KE, Miller KI, Decker H. Hemocyanins and invertebrate evolution. J. Biol. Chem. 276: 15563-15566, 2001.
145. Vatanavicharn T, Supungul P, Puanglarp N, Yingvilasprasert W, Tassanakajon A. Genomic structure, expression pattern and functional characterization of crustinPm5, a unique isoform of crustin from Penaeus monodon. Comp. Biochem. Physiol. 153B: 244-252, 2009.
146. Wang DN, Liu JW, Yang GZ, Zhang WJ, Wu XF. Cloning of anti-lPS factor cDNA from Tachypleus tridentatus, expression in Bombyx mori larvae and its biological activity in vitro. Mol. Biotechnol. 21: 1-7, 2002.
147. Wang KJ, Huang WS, Yang M, Chen HY, Bo J, Li SJ, et al. A male-specific expression gene, encodes a novel anionic antimicrobial peptide, scygonadin, in Scylla serrata. Mol. Immunol. 44: 1961-1968, 2007.
148. Wicker C, Reichhart JM, Hoffmann D, Hultmark D, Samakovlis C, Hoffmann JA. Insect immunity. Characterization of a Drosophila cDNA encoding a novel member of the diptericin family of immune peptides. J. Biol. Chem. 265: 22493-22498, 1990.
149. Yang Y, Boze H, Chemardin P, Padilla A, Moulin G, Tassanakajon A, et al. NMR structure of rALF-Pm3, an anti-lipopolysaccharide factor from shrimp: model of the possible lipid A-binding site. Biopolymers 91: 207-220, 2009.
150. Yang Y, 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.
151. Yedery RD, Reddy KV. Identification, cloning, characterization and recombinant expression of an anti-lipopolysaccharide factor from the hemocytes of Indian mud crab, Scylla serrata. Fish Shellfish Immunol. 27: 275-284, 2009a.
152. Yedery RD, Reddy KV. Purification and characterization of antibacterial proteins from granular hemocytes of Indian mud crab, Scylla serrata. Acta Biochim. Pol. 56: 71-82, 2009b.
153. Yount NY, Bayer AS, Xiong YQ, Yeaman MR. Advances in antimicrobial peptide immunobiology. Biopolymers 84: 435-458, 2006.
154. Yue F, Pan L, Miao J, Zhang L, Li J. Molecular cloning, characterization and mRNA expression of two antibacterial peptides: crustin and anti-lipopolysaccharide factor in swimming crab Portunus trituberculatus. Comp. Biochem. Physiol. 156B: 77-85, 2010.
155. Zhang J, Li F, Wang Z, Xiang J. Cloning and recombinant expression of a crustin-like gene from Chinese shrimp, Fenneropenaeus chinensis. J. Biotechnol. 127: 605-614, 2007.
156. Zhang Y, Söderhäll I, Söderhäll K, Jiravanichpaisal P. Expression of immune-related genes in one phase of embryonic development of freshwater crayfish, Pacifastacus leniusculus. Fish Shellfish Immunol. 28: 649-653, 2010.
157. Zhao XF, Wang JX. The antimicrobial peptides of the immune response of shrimp. Inv. Surv. J. 5: 162-179, 2008.