Phenoloxidase in Mollusca and Crustacean

Transcript

1 Chinese Journal of Zoology 2009,44 (5) : ( ; TX 78666) :,,, (phenoloxidase,po),,po,,, PO,,, : ; ; ; :Q81 :A : (2009) Phenoloxidase in Mollusca and Crustacean WU Shu WANG Shu2Hong 3 WANG Yi2Lei ZHANG Zi2Ping ( The Key Laboratory of Science and Technology for Aquaculture and Food Safety, Fisheries College, Jimei University, Xiamen , China ; Department of Chemistry and Biochemistry, Texas State University, San Marcos, TX 78666, USA) Abstract: Most of the Mollusca and Crustacean are economic species. The diseases related to environmental deterioration and germ plasm degeneration have caused great economic loss. More and more studies have been focusing on the immune defense system of Mollusca and Crustacean. As a key part of prophenoloxidase2activated system, phenoloxidase ( PO) plays an important role in initial immune defense of invertebrates. The function, tissue location and expression, gene cloning and sequence analysis, as well as phylogenetic analysis of PO in Mollusca and Crustacean are reviewed in this paper. The results from sequence and phylogenetic analysis evidently indicate that although the tyrosinase from Mollusca and the PO from Crustacean are isoenzymes, their encoded genes are quite different. This evidence challenges to the widely accepted view that PO belongs to invertebrates, while tryosinase belongs to vertebrates. Therefore, PO only should be specified to arthropod, while the tryosinase should be referred to mollusca and other non2arthropod as well as vertebrates. Key words :Phenoloxidase ; Tyrosinase ; Mollusca ; Crustacean (No. 2007N0048), (No. 2008A001),(No. ZQ ) ; 3,E2mail edu. cn ;,, ; : ; E2mail com. cn : , :

2 138 Chinese Journal of Zoology 44 ( PO),, E. C PO (monophenoloxidase) (tyrosinase), (diphenoloxidase,e. C ,,catecholoxidase) (laccase, E. C ), Sugumaran [1 ] 1996, PO, DNA, PO PO,,,PO [2 14 ] PO, PO [4 ], PO [5 ], 1,PO (prophenoloxidase,propo), propo PO, [15 ], (prophenoloxidase2activated system, propo2 As) PO propo2as [16 ],,,, propo2as [17 ],,,propo2as [12 ], PO [6 ], [18 ] PO,,, PO,, [7 ],PO,, [8 ] PO, [19 ] Munoz [20 ] 3, PO, PO, ( Biomphalaria glabrata) PO [21 ],PO, PO [22, 23 ],Nagai [24 ] PO PO L2 DOPA,, : Nagai [24 ] ( Pinctada f ucata) PO, PO

3 5 : PO, PO, 1994,Coles [3 ] ( Mytilus edulis), propo :PO, PO Asokan [13 ] ( Pema viridis), propo ;,Asokan propo 20, propo Western, propo2 Hellio [14 ] ( Crassostrea gigas) PO PO propo, (1 gπl) LPS(1 gπl) (016 gπl) (016 gπl) [25 ] ( Chlamys f arreri) ( PO) ( Fenneropenaeus chinensis) : PO nm nm 2 PO Luna [26] ( Argopecten ventricosus) ( Nodipecten subnodosus ) (Atrina maura) 4 (larval) (juvenile) PO PO, PO, PO, 4 PO,PO Munoz [20 ] ( Ruditapes philippinarum ) ( Chamelea gallina) ( Tapes decussatus), PO,proPO [27 ] ( Eriocheir sinensis) PO, PO, PO [28 ],, Sung [29 ] ( Penaeus monodon),, Ai [30 ] ( Litopenaeus vannamei) propo ( propo22), Northern PCR propo22, (white spot syndrome virus,wssv) 2, propo22, propo [31 ], PO [10 ],,, Stevenson [32 ] (epicuticle) (endocuticle) PO ; PO ;,PO Bai [21 ] ( Biomphalaria glabrata) PO, [33 ] PO,, nm nm 2, PO

4 140 Chinese Journal of Zoology 44, 3, RT2PCR PO mrna, [19 ] Nagai PO, [24 ],PO, cdna ( 1) 1 Table 1 Sequence analysis of several prophenoloxidase and tyrosinase gene in aquatic invertebrates Arthropod prophenoloxidase Mollusk tyrosinase Chordate tyrosinase Porifera tyrosinase Cnidaria tyrosinase NCBI Accession number Species ORF (bp) Conserved domains Π Signal peptideπ Transmembrane helices EF Eriocheir sinensis Π DQ Scylla serrata Π AF Penaeus semisulcatus Π AF P1 monodon Π DQ Macrobrachium rosenbergii Π EF Procambarus clarkii Π AB Marsupenaeus japonicus Π AY Homarus americanus Π DQ Pinctada fucata Π AJ Sepia officinalis Π AB Illex argentinus Π AB I. argentinus Π D63950 Halocynthia roretzi Π XM Ciona intestinalis Π BAJ Suberites domuncula Π XM Hydra magnipapillata Π, Gai [34 ] bp propo cdna, propo 52 % 68 % ( Scylla serrata) [35 ] propo bp, 673, (molecular weight, MW) (isoelectric point,pi) 7715 ku 5196 propo propo, ( Cancer magister) 78 % [36 ] ( Penaeus semisulcatus) bp, 684, MW u,pi bp, 686, MW u,pi 5183, 93 % 92 % ( Macrobrachium rosenbergii ) [31 ] propo cdna bp, MW 7617

5 5 : 141 ku,pi 7105 propo, ( Procambarus clarkii) ( Marsupenaeus japonicus) ( Homarus americanus) propo (NCBI : EF AB AY655139) propo, propo C propo ( GCGWPRHM), 2 6 [36 ], PO, Zhang [19 ] bpcdna,1 338 bp (open reading frame,orf) 445, 47 ku,,( Sepia officinalis) bpcdna (NCBI : AJ297474),1 821 bp ORF 606 ; ( Illex argentinus) cdna [37 ],,,, PO Sato [38 ] ( Halocynthia roretzi) bpcdna, 596, PO Muller [39 ] ( Suberites domuncula) bp, ( Ciona intestinalis ) ( Hydra magnipapillata) cdna (NCBI : XM XM ) propo, propo [40 ],, propo,ai [29 ], propo ( propo22), propo22 cdna bp, bp ORF 691 propo22 propo21 72 %, propo [41 ],,, PO ( Bombyx mori) propo,, propo [42 ] 4 ( ) NCBI, MEGA4, MEGA4 NJ, Bootstrap ( 500 ) ( 1,2) [19, 37 ] PO 6,6 PO CuA CuB,, PO ( 1,2),,

6 142 Chinese Journal of Zoology 44, ( 1,2), 36 % 39 %,, [38 ], ( 1 ), ( Drosophila melanogaster) propo, propo, [43 ] 1 NJ Fig. 1 Neighbor2joining phylogenetic tree derived from PO,tyrosinase and hemocyanin amino acid sequences (500 ),EsP : PO ;SsP : PO ; PmP : PO ; PsP : PO ;PmH:;LpH: II ;HdH:;SoH: ;IaY1 IaY2 : 1 2 ;SoY: ;Pf Y: ;HrY:;CiY:;SdY: ;HmY: ;SgY: ;MmY:;HsY: Numbers above the branches represent the bootstrap values ( %) for 500 simulations. Abbreviated protein names as follows, EsP : Eriocheir sinensis PO ; SsP : Scylla serrata PO ; PmP : Penaeus monodon PO ; PsP : P. semisulcatus PO ; PmH: P. monodon hemocyanin ; LpH: Limulus polyphemus hemocyanin subunit II ; HdH: Haliotis diversicolor supertexta hemocyanin ; SoH: Sepia officinalis hemocyanin ; IaY1 and IaY2 : Illex argentinus tyrosinase precursor 1 and 2 ; SoY: S. officinalis tyrosinase ; PfY: Pinctada fucata tyrosinase ; SgY: Streptomyces glaucescens tyrosinase ; HrY: Halocynthia roretzi tyrosinase ; CiY: Ciona intestinalis tyrosinase ; SdY: Suberites domuncula tyrosinase ; HmY: Hydra magnipapillata tyrosinase ; MmY: Mus musculus tyrosinase ; HsY: Homo sapiens tyrosinase. [44 ], PO [45 ], Siddiqui, ( Helix pomatia) O2, [46 ] Zlateva [47 ] ( Carcinus PO [46 51 ] maenas) O2

7 5 : 143 Decker [48 ] ( Eurypelma californicum) Pless [49 ] ( Bathynomus giganteus) SDS(sodium dodecylsulfate) O2 [50 ] PO,,PO [51 ] 1 2, PO ( ) Van Holde [52 ], PO, (a ) (b ) a, b PO2 ( 1), a, b, PO, PO 2 NJ Fig. 2 Neighbor2joining phylogenetic tree derived from PO, tyrosinase and hemocyanin nucleotide sequences (500 ) 1 Numbers above the branches represent the bootstrap values ( %) for 500 simulations. For abbreviated names, see Fig 1. 5,Sugumaran [1 ],, [19, 37, 38, 53 ], ( 1,2) ( 1,2),

8 144 Chinese Journal of Zoology 44, ( 1),,, PO [5, 6 ],, [53 ],,,,,,,, PO,,, PO PO,,, [ 1 ] Sugumaran M. Roles of the insect cuticle in host defence reactions. In : Soderhall K, Iwanaga S, Vasta G eds. New Directions in Invertebrates Immunology. Fair Haven, NJ : SOS Publications, 1996, [ 2 ] Kawabata T, Yasuhara Y, Ochiai M, et al. Molecular cloning of insect pro2phenol oxidase : a copper2containing protein homologous to arthropod hemocyanin. Sci, 1995, 92 : Proc Natl Acad [ 3 ] Coles J A, Pipe R K. Phenoloxidase activity in the haemolymph and haemocytes of the marine mussel Mytilus edulis. Fish Shellfish Immunol, 1994, 4 : [ 4 ] Prota G. Melanins and Melanogenesis. San Diego : Academic Press, [ 5 ],,.., 2008, 8(1) : [ 6 ],,. ( )., 2008, 8 (7) : [ 7 ] Sugumaran M. Comparative biochemistry of eumelanogenesis and the protective roles of phenoloxidase and melanin in insects. Pigment Cell Res, 2002, 15 (1) : 2 9. [ 8 ] Sugumaran M. Characterization of phenoloxidase complexes. In : Wiesner A ed. Techniques in Insect Immunology. Haven, NJ : SOS Publications, 1998, Fair [ 9 ] Sugamaran M. Prophenoloxidase activation and insect immunity. UCLA Symp Mol Cell Biol, 1990, 121 : [10 ],,.., 2002, 8 : [11 ] Cerenius L, Lee B L, Soderhall K. The propo2system : pros and cons for its role in invertebrate immunity. Immunol, 2008, 29 (6) : Trends [12 ] Soderhall K, Cerenius L. Role of the prophenoloxidase2 activating system in invertebrate immunity. Curr Opin Immunol, 1998, 10 : [13 ] Asokan R, Arumugam M, Mullainadhan P. Activation of prophenoloxidase in the plasma and haemocytes of the marine mussel Pernaviridis linnaeus. Dev Comp Immunol, 1997, 21 (1) : [14 ] Hellio C, Anne B N, Gagnaire B, et al. Demonstration of a true phenoloxidase activity and activation of a ProPO cascade in Pacific oyster, Crassostrea gigas (Thunberg) in vitro. Shellfish Immunol, 2007, 22 : Fish [15 ] Meng F L, Zhang Y Z, Kong J, et al. The research review of phenoloxidase activating system in crustacean. Limnologia Sinica, 1999, 30(1) : Oceanologia et [16 ] Sung H H, Chang H J, Her C H, et al. Phenoloxidase activity of hemocytes derived from Penaeus monodon and Macrobrachium rosenbergii. Invertebr Pathol, 1998, 71 (1) : [17 ] Barracco M A, Duvic B, Soderhall K. The 21, 32glucan binding protein from the crayfish Pacifastacus ieniusculus, when reached with a 43 man, induces spreading and degranulation of crayfish granular cells. Cell Tissue Res, 1991, 266 : [18 ].., 1990, 5 : [19 ] Zhang C, Xie L P, Huang J, et al. A novel putative tyrosinase involved in periostracum formation from the pearl oyster ( Pinctada fucata). Biochem Biophys Res Commun, 2006, 342 : [20 ] Munoz P, Meseguer J, Esteban M A. Phenoloxidase activity in three commercial bivalve species. Changes due to nature

9 5 : 145 infestation with Perkinsus atlanticus. Fish Shellfish Immunol, 2006, 20 (1) : [21 ] Bai G, Brown J F, Watson C, et al. Isolation and characterization of phenoloxidase from egg masses of the gastropod mollusc, Biomphalaria glabrata. Physiol B, 1997, 118 : Comp Biochem [22 ] Gordon J, Carriker M R. Sclerotized protein in the shell matrix of a bivalve mollusk. Mar Biol, 1980, 57 : [23 ] Waite J H, Tanzer M L. The bioadhesive of Mytilus byssus : a protein containing L2DOPA. Biochem Biopyhs Res Commun, 1980, 96 : [24 ] Nagai K, Yano M, Morimoto K, et al. Tyrosinase localization in mollusc shells. Comp Biochem Physiol B, 2007, 146 : [25 ],.., 1999, 6(2) : [26 ] Luna G A, Maeda M A, Vargas A F. Phenoloxidase activity in larval and juvenile homogenates and adult plasma and haemocytes of bivalve molluscs. Fish Shellfish Immunol, 2003, 15 (4) : [27 ],,.., 2007, 16 (3) : [28 ],,.., 2006, 18 (1) : [29 ] Sung H H, Yang Y L, Song Y L. Enhancement of microbicidalacity in the tiger2shrimp P. mondon via immunostimulation. Crust Biol, 1996, 16 (2) : [30 ] Ai H S, Liao J X, Huang X D, et al. A novel prophenoloxidase 2 exists in shrimp hemocytes. Immunol, 2009, 33 : [31 ] Liu C H, Tseng D Y, Lai C Y. Dev Comp Molecular cloning and characterisation of prophenoloxidase cdna from haemocytes of the giant freshwater prawn, Macrobrachium rosenbergii, and its transcription in relation with the moult stage. Immunol, 2006, 21 (1) : Fish Shellfish [32 ] Stevenson J R, Adomako T Y. Diphenol oxidase in the crayfish cuticle : Localization and changes in activity during the molting cycle. Insect Physiol, 1967, 13 : [33 ],,.. ( ), 2007, 23(1) : [34 ] Gai Y, Zhao J, Song L, et al. A prophenoloxidase from the Chinese mitten crab Eriocheir sinensis : gene cloning, expression and activity analysis. Fish Shellfish Immunol, 2008, 24 (2) : [35 ] Ko C F, Chiou T T, Vaseeharan B. Cloning and characterisation of a prophenoloxidase from the haemocytes of mud crab Scylla serrata. Dev Comp Immunol, 2007, 31 (1) : [36 ],,.., 2003, 34 (5) : [37 ] Naraoka T, Uchisawa H, Mori H, et al. Purification, characterization and molecular cloning of tyrosinase from the cephalopod mollusk, Illex argentinus. Eur J Biochem, 2003, 270 (19) : [38 ] Sato S, Masuya H, Numakunai T, et al. Ascidian tyrosinase gene: its unique structure and expression in the developing brain. Dev Dyn, 1997, 208 (3) : [39 ] M ller W E, Grebenjuk V A, Thakur N L, et al. Oxygen2 controlled bacterial growth in the sponge Suberites domuncula : toward a molecular understanding of the symbiotic relationships between sponge and bacteria. Appl Environ Microbiol, 2004, 70 (4) : [40 ] Yamamoto K, Yakiyama M, Fujii H. Expression of prophenoloxidase mrna during silkworm hemocyte development. Biosci Biotechnol Biochem, 2000, 64 ( 6 ) : [41 ] Morgan T D, Thomas B R, Yonekura M, et al. Soluble tyrosinases from pharate pupal integument of the tobato hornworm, Manduca sexta (L. ). Insect Biochem, 1990, 20 : [42 ] Masaaki A, Paul T B. Role of the integument in insect defense : Pro2phenol oxidase cascade in the cuticular matrix. Proc Natl Acad Sci, 1995, 92 : [43 ] Fujimoto K, Okino N, Kawabata S, et al. Nucleotide sequence of the cdna encoding the proenzyme of phenol oxidase A1 of Drosophila melanogaster. Proc Natl Acad Sci, 1995, 92 : [44 ] Paul R J, Pirow R. The physiological significance of respiratory proteins in invertebrates. Zoology ( Jena), 1998, 100 : [45 ],,.., 2005, 12 (4) : [46 ] Siddiqui N I, Akosung R F, Gielens C. Location of intrinsic and inducible phenoloxidase activity in molluscan hemocyanin. Biochem Biophys Res Commun, 2006, 48 : [47 ] Zlateva T, Dimuro P, Salvato B, et al. The O2diphenol oxidase activity of arthropod hemocyanin. FEBS Lett, 1996, 384 : [48 ] Decker H, Rimke T. Tarantula hemocyanin shows phenoloxidase activity. Biol Chem, 1998, 273 :

10 146 Chinese Journal of Zoology [49 ] Pless D, Aguilar M, Falcon A, et al. Latent phenoloxidase activity and N2terminal amino acid sequence of hemocyanin from Bathynomus giganteus, a primitive crustacean. Arch Biochem Biophys, 2003, 409 : [50 ],,.., 2008, 27(1) : 5 8. [51 ] Decker H, Tuczek F. TyrosinaseΠcatecholoxidase activity of hemocyanins: structural basis and molecular mechanism. Trends Biochem Sci, 2000, 25 : [52 ] Van Holde K E, Miller K I, Decker H. Hemocyanins and invertebrate evolution. Biol Chem, 2001, 276 : [53 ] Decker H, Terwilliger N. Cops and robbers : Putative evolution of copper oxygen2binding proteins. J Exp Biol, 2000, 203 : ,( E,37 27 N) ( 22 cm), ( 1),,,,,, 5 7,pip,,,,, ( Mycerobas affinis),,,,, 1 ( )