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Volumn 19, Issue 7, 2009, Pages 837-844

cDNA cloning, expression and antibacterial activity of lysozyme C in the blue shrimp (Litopenaeus stylirostris)

Author keywords

Antibacterial activity; Expression; Litopenaeus stylirostris; Lysozyme C; PCR cloning

Indexed keywords

BACTERIA; CLONING; GENE EXPRESSION; HISTOLOGY; SHELLFISH; TISSUE;

EID: 68249090712     PISSN: 10020071     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pnsc.2008.10.008     Document Type: Article
Times cited : (47)

References (35)
  • 1
    • 0000385093 scopus 로고
    • The amino acid sequence of egg white lysozyme
    • Canfield RE. The amino acid sequence of egg white lysozyme. J Biol Chem 1963;238:2698-707.
    • (1963) J Biol Chem , vol.238 , pp. 2698-2707
    • Canfield, R.E.1
  • 2
    • 0019335167 scopus 로고
    • Complete amino acid sequence of the goose-type lysozyme from the egg white of the black swan.
    • Simpson RJ, Begg GS, Dorow DS, et al. Complete amino acid sequence of the goose-type lysozyme from the egg white of the black swan. Biochemistry 1980;19:1814-9.
    • (1980) Biochemistry , vol.19 , pp. 1814-1819
    • Simpson, R.J.1    Begg, G.S.2    Dorow, D.S.3
  • 3
    • 0033556162 scopus 로고    scopus 로고
    • Amino acid sequences of lysozymes newly purified from invertebrates imply wide distribution of a novel class in the lysozyme family
    • Ito Y, Yoshikawa A, Hotani T, et al. Amino acid sequences of lysozymes newly purified from invertebrates imply wide distribution of a novel class in the lysozyme family. Eur J Biochem 1999;259:456-61.
    • (1999) Eur J Biochem , vol.259 , pp. 456-461
    • Ito, Y.1    Yoshikawa, A.2    Hotani, T.3
  • 4
    • 0141922176 scopus 로고    scopus 로고
    • Characterization and function of kuruma shrimp lysozyme possessing lytic activity against Vibrio species
    • Hikima S, Hikima J, Rojtinnakom J, et al. Characterization and function of kuruma shrimp lysozyme possessing lytic activity against Vibrio species. Gene 2003;316:187-95.
    • (2003) Gene , vol.316 , pp. 187-195
    • Hikima, S.1    Hikima, J.2    Rojtinnakom, J.3
  • 7
    • 25844438825 scopus 로고    scopus 로고
    • White shrimp (Litopenaeus vannamei) recombinant lysozyme has antibacterial activity against Gram negative bacteria: Vibrio alginolyticus, Vibrio parahemolyticus and Vibrio cholerae
    • de-la-Re-Vega E, García-Galaz AE, Díaz-Cinco M, et al. White shrimp (Litopenaeus vannamei) recombinant lysozyme has antibacterial activity against Gram negative bacteria: Vibrio alginolyticus, Vibrio parahemolyticus and Vibrio cholerae. Fish Shellfish Immun 2006;20:405-8.
    • (2006) Fish Shellfish Immun , vol.20 , pp. 405-408
    • de-la-Re-Vega, E.1    García-Galaz, A.E.2    Díaz-Cinco, M.3
  • 8
    • 21244482500 scopus 로고    scopus 로고
    • Identification of genes that are differentially expressed in hemocytes of the Pacific blue shrimp (Litopenaeus stylirostris) surviving an infection with Vibrio penaeicida
    • de Lorgeril J, Saulnier D, Janech MG, et al. Identification of genes that are differentially expressed in hemocytes of the Pacific blue shrimp (Litopenaeus stylirostris) surviving an infection with Vibrio penaeicida. Physiol Genomics 2005;21:174-83.
    • (2005) Physiol Genomics , vol.21 , pp. 174-183
    • de Lorgeril, J.1    Saulnier, D.2    Janech, M.G.3
  • 9
    • 33845600236 scopus 로고    scopus 로고
    • Lysozyme gene expression by hemocytes of Pacific white shrimp, Litopenaeus vannamei, after injection with Vibrio
    • Burge EJ, Madigan DJ, Burnett LE, et al. Lysozyme gene expression by hemocytes of Pacific white shrimp, Litopenaeus vannamei, after injection with Vibrio. Fish Shellfish Immun 2007;22:327-39.
    • (2007) Fish Shellfish Immun , vol.22 , pp. 327-339
    • Burge, E.J.1    Madigan, D.J.2    Burnett, L.E.3
  • 10
    • 0035065461 scopus 로고    scopus 로고
    • Protein purification, cDNA cloning and gene expression of lysozyme from eri-silkworm, Samia cynthia ricini
    • Fujimoto S, Toshimori-Tsuda I, Kishimoto K, et al. Protein purification, cDNA cloning and gene expression of lysozyme from eri-silkworm, Samia cynthia ricini. Comp Biochem Physiol B 2001;128:709-18.
    • (2001) Comp Biochem Physiol B , vol.128 , pp. 709-718
    • Fujimoto, S.1    Toshimori-Tsuda, I.2    Kishimoto, K.3
  • 11
    • 85030573519 scopus 로고    scopus 로고
    • FAO Fishstat Plus: Universal software for fishery statistical. FAO Fisheries Department, Fishery Information, Data and Statistics Unit
    • FAO Fishstat Plus: Universal software for fishery statistical. Time series 1950-2004. Version 2.30. FAO Fisheries Department, Fishery Information, Data and Statistics Unit; 2006. Available from: http://www.fao.org/fi/statist/fisoft/FISHPLUS.asp.
    • (2006) Time Series 1950-2004. Version 2.30.
  • 12
    • 0346337121 scopus 로고    scopus 로고
    • Residual genetic variability in domesticated populations of the Pacific blue shrimp (Litopenaeus stylirostris) of New Caledonia, French Polynesia and Hawaii and some management recommendations
    • Goyard E, Arnaud S, Vonau V, et al. Residual genetic variability in domesticated populations of the Pacific blue shrimp (Litopenaeus stylirostris) of New Caledonia, French Polynesia and Hawaii and some management recommendations. Aquat Living Resour 2003;16:501-8.
    • (2003) Aquat Living Resour , vol.16 , pp. 501-508
    • Goyard, E.1    Arnaud, S.2    Vonau, V.3
  • 14
    • 0033025304 scopus 로고    scopus 로고
    • Arbitrarily primed PCR to type Vibrio spp. pathogenic for shrimp
    • Goarant C, Merien F, Berthe F, et al. Arbitrarily primed PCR to type Vibrio spp. pathogenic for shrimp. Appl Environ Microbiol 1999;65:1145-51.
    • (1999) Appl Environ Microbiol , vol.65 , pp. 1145-1151
    • Goarant, C.1    Merien, F.2    Berthe, F.3
  • 15
    • 0036038876 scopus 로고    scopus 로고
    • Isolation of differentially expressed genes from white spot virus (WSV) infected Pacific blue shrimp (Penaeus stylirostris)
    • Astrofsky KM, Roux MM, Klimpel KR, et al. Isolation of differentially expressed genes from white spot virus (WSV) infected Pacific blue shrimp (Penaeus stylirostris). Arch Virol 2002;147:1799-812.
    • (2002) Arch Virol , vol.147 , pp. 1799-1812
    • Astrofsky, K.M.1    Roux, M.M.2    Klimpel, K.R.3
  • 16
    • 0027968068 scopus 로고    scopus 로고
    • Clustal W: improving the sensitivity of progressive multiple sequence weighting, position-specific gap penalties and weight metric choices
    • Thompson JD, Higgins DG, Gibson TJ. Clustal W: improving the sensitivity of progressive multiple sequence weighting, position-specific gap penalties and weight metric choices. Nucleic Acids Res 1997;22:4673-80.
    • (1997) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 19
    • 34247124903 scopus 로고
    • The measurement of lysozyme activity and the ultra-violet inactivation of interferon
    • Shugar D. The measurement of lysozyme activity and the ultra-violet inactivation of interferon. Biochem Biophys Acta 1952;8:302-9.
    • (1952) Biochem Biophys Acta , vol.8 , pp. 302-309
    • Shugar, D.1
  • 20
    • 0031552065 scopus 로고    scopus 로고
    • Purification, characterization and activities of two hemolytic and antibacterial proteins from coelomic fluid of the annelid Eisenia fetida andrei
    • Milochau A, Lassegues M, Valembois P. Purification, characterization and activities of two hemolytic and antibacterial proteins from coelomic fluid of the annelid Eisenia fetida andrei. Biochem Biophys Acta 1997;1337:123-32.
    • (1997) Biochem Biophys Acta , vol.1337 , pp. 123-132
    • Milochau, A.1    Lassegues, M.2    Valembois, P.3
  • 21
    • 0024362936 scopus 로고
    • The evolution of lysozyme and a-lactalbumin
    • Nitta K, Sugai S. The evolution of lysozyme and a-lactalbumin. Eur J Biochem 1989;182:111-8.
    • (1989) Eur J Biochem , vol.182 , pp. 111-118
    • Nitta, K.1    Sugai, S.2
  • 22
    • 0034288066 scopus 로고    scopus 로고
    • Molecular cloning of carp (Cyprinus carpio) leucocyte cell-derived chemotaxin 2, glia maturation factor b, CD45 and lysozyme C by use of suppression subtractive hybridization
    • Fujiki K, Shin DH, Nakao M, et al. Molecular cloning of carp (Cyprinus carpio) leucocyte cell-derived chemotaxin 2, glia maturation factor b, CD45 and lysozyme C by use of suppression subtractive hybridization. Fish Shellfish Immun 2000;10:643-50.
    • (2000) Fish Shellfish Immun , vol.10 , pp. 643-650
    • Fujiki, K.1    Shin, D.H.2    Nakao, M.3
  • 23
    • 0036213293 scopus 로고    scopus 로고
    • Phylogenetic analysis of invertebrate lysozymes and the evolution of lysozyme function
    • Bachali S, Jager M, Hassanin A, et al. Phylogenetic analysis of invertebrate lysozymes and the evolution of lysozyme function. J Mol Evol 2002;154:652-64.
    • (2002) J Mol Evol , vol.154 , pp. 652-664
    • Bachali, S.1    Jager, M.2    Hassanin, A.3
  • 24
    • 0036218061 scopus 로고    scopus 로고
    • Identifying a folding nucleus for the lysozyme/a-lactalbumin family from sequence conservation clusters
    • Ting KL, Jernigan RL. Identifying a folding nucleus for the lysozyme/a-lactalbumin family from sequence conservation clusters. J Mol Evol 2002;54:425-36.
    • (2002) J Mol Evol , vol.54 , pp. 425-436
    • Ting, K.L.1    Jernigan, R.L.2
  • 25
    • 0029052863 scopus 로고
    • The catalytic domain of a bacterial lytic transglycosylase defines a novel class of lysozymes
    • Thunnissen AM, Isaacs NW, Dijkstra BW. The catalytic domain of a bacterial lytic transglycosylase defines a novel class of lysozymes. Proteins 1995;22:245-58.
    • (1995) Proteins , vol.22 , pp. 245-258
    • Thunnissen, A.M.1    Isaacs, N.W.2    Dijkstra, B.W.3
  • 26
    • 0242288826 scopus 로고    scopus 로고
    • Urochordates carry multiple genes for goose-type lysozylne and no genes for chicken- or invertebrate-type lysozymes
    • Nilsen IW, Myrnes B, Edvardsen RB, et al. Urochordates carry multiple genes for goose-type lysozylne and no genes for chicken- or invertebrate-type lysozymes. Cell Mol Life Sci 2003;60:2210-8.
    • (2003) Cell Mol Life Sci , vol.60 , pp. 2210-2218
    • Nilsen, I.W.1    Myrnes, B.2    Edvardsen, R.B.3
  • 27
    • 0020629394 scopus 로고
    • Goose lysozyme structure: an evolutionary link between hen and bacteriophage lysozymes?
    • Griitter MG, Weaver LH, Matthews BW. Goose lysozyme structure: an evolutionary link between hen and bacteriophage lysozymes? Nature 1983;303:331-828.
    • (1983) Nature , vol.303 , pp. 331-828
    • Griitter, M.G.1    Weaver, L.H.2    Matthews, B.W.3
  • 28
    • 0021490172 scopus 로고
    • What's new in lysozyme research? Always a model system, today as yesterday
    • Jollés P, Jollés J. What's new in lysozyme research? Always a model system, today as yesterday. Mol Cell Biochem 1984;63:165-89.
    • (1984) Mol Cell Biochem , vol.63 , pp. 165-189
    • Jollés, P.1    Jollé, J.2
  • 29
    • 0036784920 scopus 로고    scopus 로고
    • The roles of haemocytes and the lymphoid organ in the clearance of injected Vibrio bacteria in Penaeus monodon shrimp
    • Van de Braak CBT, Botterbloma MHA, Taverneb N, et al. The roles of haemocytes and the lymphoid organ in the clearance of injected Vibrio bacteria in Penaeus monodon shrimp. Fish Shellfish Immunol 2002;13(4):293-309.
    • (2002) Fish Shellfish Immunol , vol.13 , Issue.4 , pp. 293-309
    • Van de Braak, C.B.T.1    Botterbloma, M.H.A.2    Taverneb, N.3
  • 30
    • 18044378595 scopus 로고    scopus 로고
    • Localization and bacteriostasis of Vibrio introduced into the Pacific white shrimp, Litopenaeus vannamei
    • Burgents JE, Burnetta LE, Stabbb EV, et al. Localization and bacteriostasis of Vibrio introduced into the Pacific white shrimp, Litopenaeus vannamei. Dev Comp Immunol 2005;29(8):681-91.
    • (2005) Dev Comp Immunol , vol.29 , Issue.8 , pp. 681-691
    • Burgents, J.E.1    Burnetta, L.E.2    Stabbb, E.V.3
  • 31
    • 0036274247 scopus 로고    scopus 로고
    • Expression and distribution of penaeidin antimicrobial peptides are regulated by haemocyte reactions in microbial challenged shrimp
    • Munoz M, Vandenbulcke F, Saulnier D, et al. Expression and distribution of penaeidin antimicrobial peptides are regulated by haemocyte reactions in microbial challenged shrimp. Eur J Biochem 2002;269:2678-89.
    • (2002) Eur J Biochem , vol.269 , pp. 2678-2689
    • Munoz, M.1    Vandenbulcke, F.2    Saulnier, D.3
  • 33
    • 0026901107 scopus 로고
    • Bactericidal action of lysozyme against Gram-negative bacteria due to insertion of a hydrophobic pentapeptide into its C-terminus
    • Ibrahim HR, Yamada M, Kobayashi K, et al. Bactericidal action of lysozyme against Gram-negative bacteria due to insertion of a hydrophobic pentapeptide into its C-terminus. Biosci Biotechnol Biochem 1992;56:1361-3.
    • (1992) Biosci Biotechnol Biochem , vol.56 , pp. 1361-1363
    • Ibrahim, H.R.1    Yamada, M.2    Kobayashi, K.3
  • 34
    • 0028071629 scopus 로고
    • Enhanced bactericidal action of lysozyme to Escherichia coli by inserting a hydrophobic pentapeptide into its C terminus
    • Ibrahim HR, Yamada M, Matsushita K, et al. Enhanced bactericidal action of lysozyme to Escherichia coli by inserting a hydrophobic pentapeptide into its C terminus. J Biol Chem 1994;269:5059-63.
    • (1994) J Biol Chem , vol.269 , pp. 5059-5063
    • Ibrahim, H.R.1    Yamada, M.2    Matsushita, K.3
  • 35
    • 0242607058 scopus 로고    scopus 로고
    • Relationships between conformational changes and antimicrobial activity of lysozyme upon reduction of its disulfide bonds
    • Touch V, Hayakawa S, Saitoh K. Relationships between conformational changes and antimicrobial activity of lysozyme upon reduction of its disulfide bonds. Food Chem 2004;84:421-8.
    • (2004) Food Chem , vol.84 , pp. 421-428
    • Touch, V.1    Hayakawa, S.2    Saitoh, K.3


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