메뉴 건너뛰기




Volumn 16, Issue 1, 2014, Pages 46-53

Molecular Cloning of Hemocyanin cDNA from Fenneropenaeus chinensis and Antimicrobial Analysis of Two C-terminal Fragments

Author keywords

Antimicrobial peptides (AMPs); Fenneropenaeus chinensis; Hemocyanin; Pichia pastoris; Recombinant expression

Indexed keywords

AMINO ACIDS; CLONE CELLS; ELECTROPHORESIS; ENCODING (SYMBOLS); MICROORGANISMS; PEPTIDES; SIGNAL ENCODING; SODIUM DODECYL SULFATE; SULFUR COMPOUNDS;

EID: 84892881538     PISSN: 14362228     EISSN: None     Source Type: Journal    
DOI: 10.1007/s10126-013-9519-y     Document Type: Article
Times cited : (35)

References (48)
  • 4
    • 0000695553 scopus 로고    scopus 로고
    • Applications of yeast in biotechnology: protein production and genetic analysis
    • Cereghino GPL, Cregg JM (1999) Applications of yeast in biotechnology: protein production and genetic analysis. Curr Opin Biotechnol 10(5): 422-427.
    • (1999) Curr Opin Biotechnol , vol.10 , Issue.5 , pp. 422-427
    • Cereghino, G.P.L.1    Cregg, J.M.2
  • 7
    • 33846794525 scopus 로고    scopus 로고
    • Purification and characterization of eight peptides from Galleria mellonella immune hemolymph
    • Cytryńska M, Mak P, Zdybicka-Barabas A, Suder P, Jakubowicz T (2007) Purification and characterization of eight peptides from Galleria mellonella immune hemolymph. Peptides 28(3): 533-546.
    • (2007) Peptides , vol.28 , Issue.3 , pp. 533-546
    • Cytryńska, M.1    Mak, P.2    Zdybicka-Barabas, A.3    Suder, P.4    Jakubowicz, T.5
  • 8
    • 1242343403 scopus 로고    scopus 로고
    • Recent findings on phenoloxidase activity and antimicrobial activity of hemocyanins
    • Decker H, Jaenicke E (2004) Recent findings on phenoloxidase activity and antimicrobial activity of hemocyanins. Dev Comp Immunol 28: 673-687.
    • (2004) Dev Comp Immunol , vol.28 , pp. 673-687
    • Decker, H.1    Jaenicke, E.2
  • 10
    • 33746695401 scopus 로고    scopus 로고
    • Investigations into the ability of an oblique α-helical template to provide the basis for design of an antimicrobial anionic amphiphilic peptide
    • Dennison SR, Morton LHG, Brandenburg K, Harris F, Phoenix DA (2006b) Investigations into the ability of an oblique α-helical template to provide the basis for design of an antimicrobial anionic amphiphilic peptide. FEBS J 273(16): 3792-3803.
    • (2006) FEBS J , vol.273 , Issue.16 , pp. 3792-3803
    • Dennison, S.R.1    Morton, L.H.G.2    Brandenburg, K.3    Harris, F.4    Phoenix, D.A.5
  • 13
    • 0021889174 scopus 로고
    • Isolation of an antibacterial peptide from human lung lavage fluid
    • Ellison RT, Boose D, LaForce FM (1985) Isolation of an antibacterial peptide from human lung lavage fluid. J Infect Dis 151(6): 1123.
    • (1985) J Infect Dis , vol.151 , Issue.6 , pp. 1123
    • Ellison, R.T.1    Boose, D.2    LaForce, F.M.3
  • 15
    • 73549121068 scopus 로고    scopus 로고
    • Anionic antimicrobial peptides from eukaryotic organisms
    • Harris F, Dennison SR, Phoenix DA (2009) Anionic antimicrobial peptides from eukaryotic organisms. Curr Protein Pept Sc 10(6): 585-606.
    • (2009) Curr Protein Pept Sc , vol.10 , Issue.6 , pp. 585-606
    • Harris, F.1    Dennison, S.R.2    Phoenix, D.A.3
  • 16
    • 0035996902 scopus 로고    scopus 로고
    • Antimicrobial anionic peptide binds in vivo to Mannheimia (Pasteurella) haemolytica attached to ovine alveolar epithelium
    • Heidari M, Hamir A, Cutlip RC, Brogden KA (2002) Antimicrobial anionic peptide binds in vivo to Mannheimia (Pasteurella) haemolytica attached to ovine alveolar epithelium. Int J Antimicrob Ag 20(1): 69-72.
    • (2002) Int J Antimicrob Ag , vol.20 , Issue.1 , pp. 69-72
    • Heidari, M.1    Hamir, A.2    Cutlip, R.C.3    Brogden, K.A.4
  • 17
    • 0030632142 scopus 로고    scopus 로고
    • Strategies for the isolation and characterization of antimicrobial peptides of invertebrates
    • Hetru C, Bulet P (1997) Strategies for the isolation and characterization of antimicrobial peptides of invertebrates. MIMB 78: 35-50.
    • (1997) Mimb , vol.78 , pp. 35-50
    • Hetru, C.1    Bulet, P.2
  • 18
    • 33749511406 scopus 로고    scopus 로고
    • Purification and part characterization of a novel antibacterial protein Scygonadin, isolated from the seminal plasma of mud crab, Scylla serrata (Forskål, 1775)
    • Huang WS, Wang KJ, Yang M, Cai JJ, Li SJ, Wang GZ (2006) 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(1): 37-42.
    • (2006) J Exp Mar Biol Ecol , vol.339 , Issue.1 , pp. 37-42
    • Huang, W.S.1    Wang, K.J.2    Yang, M.3    Cai, J.J.4    Li, S.J.5    Wang, G.Z.6
  • 19
    • 4544340747 scopus 로고    scopus 로고
    • Functional changes in the family of type 3 copper proteins during evolution
    • Jaenicke E, Decker H (2004) Functional changes in the family of type 3 copper proteins during evolution. ChemBioChem 5(2): 163-169.
    • (2004) ChemBioChem , vol.5 , Issue.2 , pp. 163-169
    • Jaenicke, E.1    Decker, H.2
  • 20
    • 0040320331 scopus 로고    scopus 로고
    • Spider hemocyanin binds ecdysone and 20-OH-ecdysone
    • Jaenicke E, Föll R, Decker H (1999) Spider hemocyanin binds ecdysone and 20-OH-ecdysone. J Biol Chem 274: 34267-34271.
    • (1999) J Biol Chem , vol.274 , pp. 34267-34271
    • Jaenicke, E.1    Föll, R.2    Decker, H.3
  • 21
    • 33750808928 scopus 로고    scopus 로고
    • Expression of recombinant hybrid peptide cecropinA(1-8)-magainin2(1-12) in Pichia pastoris: purification and characterization
    • Jin F, Xu X, Wang L, Zhang W, Gu D (2006) Expression of recombinant hybrid peptide cecropinA(1-8)-magainin2(1-12) in Pichia pastoris: purification and characterization. Protein Expres Purif 50(2): 147-156.
    • (2006) Protein Expres Purif , vol.50 , Issue.2 , pp. 147-156
    • Jin, F.1    Xu, X.2    Wang, L.3    Zhang, W.4    Gu, D.5
  • 22
    • 0021251715 scopus 로고
    • Effect of zinc and phosphate on an antibacterial peptide isolated from lung lavage
    • LaForce FM, Boose DS (1984) Effect of zinc and phosphate on an antibacterial peptide isolated from lung lavage. Infect Immun 45(3): 692-696.
    • (1984) Infect Immun , vol.45 , Issue.3 , pp. 692-696
    • LaForce, F.M.1    Boose, D.S.2
  • 23
    • 0036375765 scopus 로고    scopus 로고
    • An anionic antimicrobial peptide from toad Bombina maxima
    • Lai R, Liu H, Hui Lee W, Zhang Y (2002) An anionic antimicrobial peptide from toad Bombina maxima. Biochem Bioph Res Co 295(4): 796-799.
    • (2002) Biochem Bioph Res Co , vol.295 , Issue.4 , pp. 796-799
    • Lai, R.1    Liu, H.2    Hui Lee, W.3    Zhang, Y.4
  • 24
    • 2542564201 scopus 로고    scopus 로고
    • Two novel non-cationic defensin-like antimicrobial peptides from haemolymph of the female tick, Amblyomma hebraeum
    • Lai R, Lomas LO, Jonczy J, Turner PC, Rees HH (2004) Two novel non-cationic defensin-like antimicrobial peptides from haemolymph of the female tick, Amblyomma hebraeum. Biochem J 379: 681-5.
    • (2004) Biochem J , vol.379 , pp. 681-685
    • Lai, R.1    Lomas, L.O.2    Jonczy, J.3    Turner, P.C.4    Rees, H.H.5
  • 25
    • 61349169039 scopus 로고    scopus 로고
    • AMPed up immunity: how antimicrobial peptides have multiple roles in immune defense
    • Lai Y, Gallo RL (2009) AMPed up immunity: how antimicrobial peptides have multiple roles in immune defense. Trends Immunol 30(3): 131-141.
    • (2009) Trends Immunol , vol.30 , Issue.3 , pp. 131-141
    • Lai, Y.1    Gallo, R.L.2
  • 26
    • 0037424354 scopus 로고    scopus 로고
    • Processing of an antibacterial peptide from hemocyanin of the freshwater crayfish Pacifastacus leniusculus
    • Lee SY, Lee BL, Söderhäll K (2003) Processing of an antibacterial peptide from hemocyanin of the freshwater crayfish Pacifastacus leniusculus. J Biol Chem 278(10): 7927-7933.
    • (2003) J Biol Chem , vol.278 , Issue.10 , pp. 7927-7933
    • Lee, S.Y.1    Lee, B.L.2    Söderhäll, K.3
  • 27
    • 11844287624 scopus 로고    scopus 로고
    • High level expression, purification, and characterization of the shrimp antimicrobial peptide, Ch-penaeidin, in Pichia pastoris
    • Li L, Wang J-X, Zhao X-F, Kang C-J, Liu N, Xiang J-H, Li F-H, Sueda S, Kondo H (2005) High level expression, purification, and characterization of the shrimp antimicrobial peptide, Ch-penaeidin, in Pichia pastoris. Protein Expres Purif 39(2): 144-151.
    • (2005) Protein Expres Purif , vol.39 , Issue.2 , pp. 144-151
    • Li, L.1    Wang, J.-X.2    Zhao, X.-F.3    Kang, C.-J.4    Liu, N.5    Xiang, J.-H.6    Li, F.-H.7    Sueda, S.8    Kondo, H.9
  • 28
    • 0032079041 scopus 로고    scopus 로고
    • Shrimp diseases and current diagnostic methods
    • Lightner DV, Redman RM (1998) Shrimp diseases and current diagnostic methods. Aquaculture 164(1-4): 201-220.
    • (1998) Aquaculture , vol.164 , Issue.1-4 , pp. 201-220
    • Lightner, D.V.1    Redman, R.M.2
  • 29
    • 0037653852 scopus 로고
    • An ultracentrifugal study of the efficiency of some macromolecular inhibitors of ribonuclease
    • Littauer UZ, Sela M (1962) An ultracentrifugal study of the efficiency of some macromolecular inhibitors of ribonuclease. BBA-Specialized Section on Nucleic Acids and Related Subjects 61(4): 609-611.
    • (1962) BBA-Specialized Section on Nucleic Acids and Related Subjects , vol.61 , Issue.4 , pp. 609-611
    • Littauer, U.Z.1    Sela, M.2
  • 31
    • 0002261584 scopus 로고
    • Evolution and function of structurally diverse subunits in the respiratory protein hemocyanin from arthropods
    • Markl J (1986) Evolution and function of structurally diverse subunits in the respiratory protein hemocyanin from arthropods. Biol Bull-US 171: 90-115.
    • (1986) Biol Bull-US , vol.171 , pp. 90-115
    • Markl, J.1
  • 34
    • 0023700978 scopus 로고
    • Tachyplesin, a class of antimicrobial peptide from the hemocytes of the horseshoe crab (Tachypleus tridentatus). Isolation and chemical structure
    • Nakamura T, Furunaka H, Miyata T, Tokunaga F, Muta T, Iwanaga S, Niwa M, Takao T, Shimonishi Y (1988) Tachyplesin, a class of antimicrobial peptide from the hemocytes of the horseshoe crab (Tachypleus tridentatus). Isolation and chemical structure. J Biol Chem 263(32): 16709-16713.
    • (1988) J Biol Chem , vol.263 , Issue.32 , pp. 16709-16713
    • Nakamura, T.1    Furunaka, H.2    Miyata, T.3    Tokunaga, F.4    Muta, T.5    Iwanaga, S.6    Niwa, M.7    Takao, T.8    Shimonishi, Y.9
  • 35
    • 0027962943 scopus 로고
    • Gas transport in the haemolymph of arachnids-oxygen transport and the physiological role of haemocyanin
    • Paul R, Bergner B, Pfeffer-Seidl A, Decker H, Efinger R, Storz H (1994) Gas transport in the haemolymph of arachnids-oxygen transport and the physiological role of haemocyanin. J Exp Biol 188: 25-46.
    • (1994) J Exp Biol , vol.188 , pp. 25-46
    • Paul, R.1    Bergner, B.2    Pfeffer-Seidl, A.3    Decker, H.4    Efinger, R.5    Storz, H.6
  • 36
    • 0005401151 scopus 로고    scopus 로고
    • The physiological significance of respiratory proteins in invertebrates
    • Paul RJ, Pirow R (1998) The physiological significance of respiratory proteins in invertebrates. Zoology 100: 319-327.
    • (1998) Zoology , vol.100 , pp. 319-327
    • Paul, R.J.1    Pirow, R.2
  • 37
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schägger H, Von Jagow G (1987) Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal Biochem 166(2): 368-379.
    • (1987) Anal Biochem , vol.166 , Issue.2 , pp. 368-379
    • Schägger, H.1    Von Jagow, G.2
  • 38
    • 0017169432 scopus 로고
    • Bacterial growth inhibition by amniotic fluid. VI. Evidence for a zinc-peptide antibacterial system
    • Schlievert P, Johnson W, Galask R (1976) Bacterial growth inhibition by amniotic fluid. VI. Evidence for a zinc-peptide antibacterial system. AJOG 125(7): 906.
    • (1976) Ajog , vol.125 , Issue.7 , pp. 906
    • Schlievert, P.1    Johnson, W.2    Galask, R.3
  • 39
    • 0031589162 scopus 로고    scopus 로고
    • Molecular cloning of hemocyanin cDNA from Penaeus vannamei (Crustacea, Decapoda): structure, evolution and physiological aspects
    • Sellos D, Lemoine S, van Wormhoudt A (1997) Molecular cloning of hemocyanin cDNA from Penaeus vannamei (Crustacea, Decapoda): structure, evolution and physiological aspects. FEBS Lett 407(2): 153-158.
    • (1997) FEBS Lett , vol.407 , Issue.2 , pp. 153-158
    • Sellos, D.1    Lemoine, S.2    van Wormhoudt, A.3
  • 40
    • 77952579210 scopus 로고    scopus 로고
    • Conventional and unconventional antimicrobials from fish, marine invertebrates and micro-algae
    • Smith VJ, Desbois AP, Dyrynda EA (2010) Conventional and unconventional antimicrobials from fish, marine invertebrates and micro-algae. Mar Drugs 8(4): 1213-1262.
    • (2010) Mar Drugs , vol.8 , Issue.4 , pp. 1213-1262
    • Smith, V.J.1    Desbois, A.P.2    Dyrynda, E.A.3
  • 41
    • 40849102419 scopus 로고    scopus 로고
    • Crustins: enigmatic WAP domain-containing antibacterial proteins from crustaceans
    • Smith VJ, Fernandes JMO, Kemp GD, Hauton C (2008) Crustins: enigmatic WAP domain-containing antibacterial proteins from crustaceans. DCI 32(7): 758-772.
    • (2008) Dci , vol.32 , Issue.7 , pp. 758-772
    • Smith, V.J.1    Fernandes, J.M.O.2    Kemp, G.D.3    Hauton, C.4
  • 42
    • 0032005367 scopus 로고    scopus 로고
    • Role of the prophenoloxidase-activating system in invertebrate immunity
    • Söderhäll K, Cerenius L (1998) Role of the prophenoloxidase-activating system in invertebrate immunity. Curr Opin Immunol 10: 23-28.
    • (1998) Curr Opin Immunol , vol.10 , pp. 23-28
    • Söderhäll, K.1    Cerenius, L.2
  • 43
    • 0033044218 scopus 로고    scopus 로고
    • Molecular cloning and characterization of prophenoloxidase in the black tiger shrimp, Penaeus monodon
    • Sritunyalucksana K, Cerenius L, Söderhäll K (1999) Molecular cloning and characterization of prophenoloxidase in the black tiger shrimp, Penaeus monodon. DCI 23(3): 179-186.
    • (1999) Dci , vol.23 , Issue.3 , pp. 179-186
    • Sritunyalucksana, K.1    Cerenius, L.2    Söderhäll, K.3
  • 44
    • 0019386682 scopus 로고
    • Sequence and specificity of two antibacterial proteins involved in insect immunity
    • Steiner H, Hultmark D, Engström Å, Bennich H, Boman H (1981) Sequence and specificity of two antibacterial proteins involved in insect immunity. Nature 292: 246-248.
    • (1981) Nature , vol.292 , pp. 246-248
    • Steiner, H.1    Hultmark, D.2    Engström, Å.3    Bennich, H.4    Boman, H.5
  • 45
    • 84965187370 scopus 로고
    • Inhibitors of ribonuclease activity
    • Vandendriessche L (1956) Inhibitors of ribonuclease activity. Arch Biochem Biophys 65(1): 347-353.
    • (1956) Arch Biochem Biophys , vol.65 , Issue.1 , pp. 347-353
    • Vandendriessche, L.1
  • 46
    • 0024975122 scopus 로고
    • Crystal structure of hexameric haemocyanin from Panulirus interruptus refined at 3.2 Å resolution
    • Volbeda A, Hol W (1989) Crystal structure of hexameric haemocyanin from Panulirus interruptus refined at 3. 2 Å resolution. J Mol Biol 209: 249-279.
    • (1989) J Mol Biol , vol.209 , pp. 249-279
    • Volbeda, A.1    Hol, W.2
  • 47
    • 34548398528 scopus 로고    scopus 로고
    • Expression and purification of ancrod, an anticoagulant drug, in Pichia pastoris
    • Yu X, Li Z, Xia X, Fang H, Zhou C, Chen H (2007) Expression and purification of ancrod, an anticoagulant drug, in Pichia pastoris. Protein Expr Purif 55(2): 257-261.
    • (2007) Protein Expr Purif , vol.55 , Issue.2 , pp. 257-261
    • Yu, X.1    Li, Z.2    Xia, X.3    Fang, H.4    Zhou, C.5    Chen, H.6
  • 48
    • 0344736987 scopus 로고    scopus 로고
    • Antiviral properties of hemocyanin isolated from shrimp Penaeus monodon
    • Zhang X, Huang C, Qin Q (2004) Antiviral properties of hemocyanin isolated from shrimp Penaeus monodon. Antivir Res 61(2): 93-99.
    • (2004) Antivir Res , vol.61 , Issue.2 , pp. 93-99
    • Zhang, X.1    Huang, C.2    Qin, Q.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.