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Volumn 33, Issue 8, 2009, Pages 932-938

Identification and cloning of an invertebrate-type lysozyme from Eisenia andrei

Author keywords

Annelids; Antimicrobial protein; Invertebrates; Isopeptidase activity; Peptidoglycan; Real time PCR

Indexed keywords

COMPLEMENTARY DNA; ISOPEPTIDASE; LYSOZYME; NUCLEOTIDE; PEPTIDASE; RECOMBINANT PROTEIN; UNCLASSIFIED DRUG;

EID: 67349280294     PISSN: 0145305X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.dci.2009.03.002     Document Type: Article
Times cited : (64)

References (36)
  • 3
    • 0035973859 scopus 로고    scopus 로고
    • Molecular cloning, expression and evolution of the Japanese flounder goose-type lysozyme gene, and the lytic activity of its recombinant protein
    • Hikima J., Minagawa S., Hirono I., and Aoki T. Molecular cloning, expression and evolution of the Japanese flounder goose-type lysozyme gene, and the lytic activity of its recombinant protein. Biochim Biophys Acta 1520 1 (2001) 35-44
    • (2001) Biochim Biophys Acta , vol.1520 , Issue.1 , pp. 35-44
    • Hikima, J.1    Minagawa, S.2    Hirono, I.3    Aoki, T.4
  • 4
    • 0043074437 scopus 로고    scopus 로고
    • Molecular cloning of G type lysozyme cDNA in common carp (Cyprinus carpio L.)
    • Savan R., Aman A., and Sakai M. Molecular cloning of G type lysozyme cDNA in common carp (Cyprinus carpio L.). Fish Shellfish Immunol 15 3 (2003) 263-268
    • (2003) Fish Shellfish Immunol , vol.15 , Issue.3 , pp. 263-268
    • Savan, R.1    Aman, A.2    Sakai, M.3
  • 6
    • 35248885592 scopus 로고    scopus 로고
    • Molecular characterization of goose-type lysozyme homologue of large yellow croaker and its involvement in immune response induced by trivalent bacterial vaccine as an acute-phase protein
    • Zheng W., Tian C., and Chen X. Molecular characterization of goose-type lysozyme homologue of large yellow croaker and its involvement in immune response induced by trivalent bacterial vaccine as an acute-phase protein. Immunol Lett 113 2 (2007) 107-116
    • (2007) Immunol Lett , vol.113 , Issue.2 , pp. 107-116
    • Zheng, W.1    Tian, C.2    Chen, X.3
  • 7
    • 0036213293 scopus 로고    scopus 로고
    • Phylogenetic analysis of invertebrate lysozymes and the evolution of lysozyme function
    • Bachali S., Jager M., Hassanin A., Schoentgen F., Jolles P., Fiala-Medioni A., et al. Phylogenetic analysis of invertebrate lysozymes and the evolution of lysozyme function. J Mol Evol 54 5 (2002) 652-664
    • (2002) J Mol Evol , vol.54 , Issue.5 , pp. 652-664
    • Bachali, S.1    Jager, M.2    Hassanin, A.3    Schoentgen, F.4    Jolles, P.5    Fiala-Medioni, A.6
  • 8
    • 34848901438 scopus 로고    scopus 로고
    • Crystal structure of Tapes japonica Lysozyme with substrate analogue: structural basis of the catalytic mechanism and manifestation of its chitinase activity accompanied by quaternary structural change
    • Goto T., Abe Y., Kakuta Y., Takeshita K., Imoto T., and Ueda T. Crystal structure of Tapes japonica Lysozyme with substrate analogue: structural basis of the catalytic mechanism and manifestation of its chitinase activity accompanied by quaternary structural change. J Biol Chem 282 37 (2007) 27459-27467
    • (2007) J Biol Chem , vol.282 , Issue.37 , pp. 27459-27467
    • Goto, T.1    Abe, Y.2    Kakuta, Y.3    Takeshita, K.4    Imoto, T.5    Ueda, T.6
  • 9
    • 34547456983 scopus 로고    scopus 로고
    • cDNA cloning and in situ hybridization of a novel lysozyme in the Pacific oyster, Crassostrea gigas
    • Itoh N., and Takahashi K.G. cDNA cloning and in situ hybridization of a novel lysozyme in the Pacific oyster, Crassostrea gigas. Comp Biochem Physiol B Biochem Mol Biol 148 2 (2007) 160-166
    • (2007) Comp Biochem Physiol B Biochem Mol Biol , vol.148 , Issue.2 , pp. 160-166
    • Itoh, N.1    Takahashi, K.G.2
  • 10
    • 0016592228 scopus 로고
    • The losozyme from Asterias rubens
    • Jolles J., and Jolles P. The losozyme from Asterias rubens. Eur J Biochem 54 1 (1975) 19-23
    • (1975) Eur J Biochem , vol.54 , Issue.1 , pp. 19-23
    • Jolles, J.1    Jolles, P.2
  • 11
    • 3142643627 scopus 로고    scopus 로고
    • Determination of the complete cDNA sequence, construction of expression systems, and elucidation of fibrinolytic activity for Tapes japonica lysozyme
    • Takeshita K., Hashimoto Y., Thujihata Y., So T., Ueda T., and Iomoto T. Determination of the complete cDNA sequence, construction of expression systems, and elucidation of fibrinolytic activity for Tapes japonica lysozyme. Protein Expr Purif 36 2 (2004) 254-262
    • (2004) Protein Expr Purif , vol.36 , Issue.2 , pp. 254-262
    • Takeshita, K.1    Hashimoto, Y.2    Thujihata, Y.3    So, T.4    Ueda, T.5    Iomoto, T.6
  • 12
    • 0141637403 scopus 로고    scopus 로고
    • A small chimerically bifunctional monomeric protein: Tapes japonica lysozyme
    • Takeshita K., Hashimoto Y., Ueda T., and Imoto T. A small chimerically bifunctional monomeric protein: Tapes japonica lysozyme. Cell Mol Life Sci 60 9 (2003) 1944-1951
    • (2003) Cell Mol Life Sci , vol.60 , Issue.9 , pp. 1944-1951
    • Takeshita, K.1    Hashimoto, Y.2    Ueda, T.3    Imoto, T.4
  • 13
    • 33846512298 scopus 로고    scopus 로고
    • A new lysozyme from the eastern oyster (Crassostrea virginica) indicates adaptive evolution of i-type lysozymes
    • Xue Q.G., Itoh N., Schey K.L., Li Y.L., Cooper R.K., and La Peyre J.F. A new lysozyme from the eastern oyster (Crassostrea virginica) indicates adaptive evolution of i-type lysozymes. Cell Mol Life Sci 64 1 (2007) 82-95
    • (2007) Cell Mol Life Sci , vol.64 , Issue.1 , pp. 82-95
    • Xue, Q.G.1    Itoh, N.2    Schey, K.L.3    Li, Y.L.4    Cooper, R.K.5    La Peyre, J.F.6
  • 15
    • 85190486866 scopus 로고    scopus 로고
    • Terwisscha van Scheltinga AC. Plant lysozymes
    • Jolles P. (Ed), Birkhäuser Verlag
    • Beintema J.J. Terwisscha van Scheltinga AC. Plant lysozymes. In: Jolles P. (Ed). Lysozymes: model enzymes in biochemistry and biology (1996), Birkhäuser Verlag 75-86
    • (1996) Lysozymes: model enzymes in biochemistry and biology , pp. 75-86
    • Beintema, J.J.1
  • 18
    • 0021285423 scopus 로고
    • Stomach lysozymes of ruminants. I. Distribution and catalytic properties
    • Dobson D.E., Prager E.M., and Wilson A.C. Stomach lysozymes of ruminants. I. Distribution and catalytic properties. J Biol Chem 259 18 (1984) 11607-11616
    • (1984) J Biol Chem , vol.259 , Issue.18 , pp. 11607-11616
    • Dobson, D.E.1    Prager, E.M.2    Wilson, A.C.3
  • 19
    • 0028046864 scopus 로고
    • Molecular adaptation of a leaf-eating bird: stomach lysozyme of the hoatzin
    • Kornegay J.R., Schilling J.W., and Wilson A.C. Molecular adaptation of a leaf-eating bird: stomach lysozyme of the hoatzin. Mol Biol Evol 11 6 (1994) 921-928
    • (1994) Mol Biol Evol , vol.11 , Issue.6 , pp. 921-928
    • Kornegay, J.R.1    Schilling, J.W.2    Wilson, A.C.3
  • 20
    • 0025940660 scopus 로고
    • Digestion of bacteria and the role of midgut lysozyme in some insect larvae
    • Lemos F.J., and Terra W.R. Digestion of bacteria and the role of midgut lysozyme in some insect larvae. Comp Biochem Physiol B 100 2 (1991) 265-268
    • (1991) Comp Biochem Physiol B , vol.100 , Issue.2 , pp. 265-268
    • Lemos, F.J.1    Terra, W.R.2
  • 21
    • 0032052770 scopus 로고    scopus 로고
    • Consensus-degenerate hybrid oligonucleotide primers for amplification of distantly related sequences
    • Rose T.M., Schultz E.R., Henikoff J.G., Pietrokovski S., McCallum C.M., and Henikoff S. Consensus-degenerate hybrid oligonucleotide primers for amplification of distantly related sequences. Nucleic Acids Res 26 7 (1998) 1628-1635
    • (1998) Nucleic Acids Res , vol.26 , Issue.7 , pp. 1628-1635
    • Rose, T.M.1    Schultz, E.R.2    Henikoff, J.G.3    Pietrokovski, S.4    McCallum, C.M.5    Henikoff, S.6
  • 22
    • 0017681196 scopus 로고
    • DNA sequencing with chain-terminating inhibitors
    • Sanger F., Nicklen S., and Coulson A.R. DNA sequencing with chain-terminating inhibitors. Proc Natl Acad Sci USA 74 12 (1977) 5463-5467
    • (1977) Proc Natl Acad Sci USA , vol.74 , Issue.12 , pp. 5463-5467
    • Sanger, F.1    Nicklen, S.2    Coulson, A.R.3
  • 23
    • 0039001059 scopus 로고
    • Improved double-stranded DNA sequencing using the linear polymerase chain reaction
    • Murray V. Improved double-stranded DNA sequencing using the linear polymerase chain reaction. Nucleic Acids Res 17 21 (1989) 8889
    • (1989) Nucleic Acids Res , vol.17 , Issue.21 , pp. 8889
    • Murray, V.1
  • 24
    • 3042521098 scopus 로고    scopus 로고
    • Improved prediction of signal peptides: SignalP 3.0
    • Bendtsen J.D., Nielsen H., von Heijne G., and Brunak S. Improved prediction of signal peptides: SignalP 3.0. J Mol Biol 340 4 (2004) 783-795
    • (2004) J Mol Biol , vol.340 , Issue.4 , pp. 783-795
    • Bendtsen, J.D.1    Nielsen, H.2    von Heijne, G.3    Brunak, S.4
  • 26
    • 0027968068 scopus 로고
    • CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson J.D., Higgins D.G., and Gibson T.J. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res 22 22 (1994) 4673-4680
    • (1994) Nucleic Acids Res , vol.22 , Issue.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 27
    • 0032544658 scopus 로고    scopus 로고
    • Identification and cloning of a glucan- and lipopolysaccharide-binding protein from Eisenia foetida earthworm involved in the activation of prophenoloxidase cascade
    • Beschin A., Bilej M., Hanssens F., Raymakers J., Van Dyck E., Revets H., et al. Identification and cloning of a glucan- and lipopolysaccharide-binding protein from Eisenia foetida earthworm involved in the activation of prophenoloxidase cascade. J Biol Chem 273 38 (1998) 24948-24954
    • (1998) J Biol Chem , vol.273 , Issue.38 , pp. 24948-24954
    • Beschin, A.1    Bilej, M.2    Hanssens, F.3    Raymakers, J.4    Van Dyck, E.5    Revets, H.6
  • 28
    • 0022461022 scopus 로고
    • Improved agar plate assays of bovine lysozyme and haemolytic complement activity
    • Lie O., Syed M., and Solbu H. Improved agar plate assays of bovine lysozyme and haemolytic complement activity. Acta Vet Scand 27 1 (1986) 23-32
    • (1986) Acta Vet Scand , vol.27 , Issue.1 , pp. 23-32
    • Lie, O.1    Syed, M.2    Solbu, H.3
  • 29
    • 33646733873 scopus 로고    scopus 로고
    • Cell wall substrate specificity of six different lysozymes and lysozyme inhibitory activity of bacterial extracts
    • Nakimbugwe D., Masschalck B., Deckers D., Callewaert L., Aertsen A., and Michiels C.W. Cell wall substrate specificity of six different lysozymes and lysozyme inhibitory activity of bacterial extracts. FEMS Microbiol Lett 259 1 (2006) 41-46
    • (2006) FEMS Microbiol Lett , vol.259 , Issue.1 , pp. 41-46
    • Nakimbugwe, D.1    Masschalck, B.2    Deckers, D.3    Callewaert, L.4    Aertsen, A.5    Michiels, C.W.6
  • 30
    • 0042787150 scopus 로고
    • Lysozyme activity in the coelomic fluid and coelomocytes of the earthworm Eisenia foetida sav. In relation to bacterial infection
    • Çotuk A., and Dales R.P. Lysozyme activity in the coelomic fluid and coelomocytes of the earthworm Eisenia foetida sav. In relation to bacterial infection. Comp Biochem Physiol A 78 3 (1984) 469-474
    • (1984) Comp Biochem Physiol A , vol.78 , Issue.3 , pp. 469-474
    • Çotuk, A.1    Dales, R.P.2
  • 31
    • 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., Fukuda S., Sugimura K., and Imoto T. Amino acid sequences of lysozymes newly purified from invertebrates imply wide distribution of a novel class in the lysozyme family. Eur J Biochem 259 1-2 (1999) 456-461
    • (1999) Eur J Biochem , vol.259 , Issue.1-2 , pp. 456-461
    • Ito, Y.1    Yoshikawa, A.2    Hotani, T.3    Fukuda, S.4    Sugimura, K.5    Imoto, T.6
  • 33
    • 33748928226 scopus 로고    scopus 로고
    • Experimental verification of the crucial roles of Glu73 in the catalytic activity and structural stability of goose type lysozyme
    • Kawamura S., Ohno K., Ohkuma M., Chijiiwa Y., and Torikata T. Experimental verification of the crucial roles of Glu73 in the catalytic activity and structural stability of goose type lysozyme. J Biochem 140 1 (2006) 75-85
    • (2006) J Biochem , vol.140 , Issue.1 , pp. 75-85
    • Kawamura, S.1    Ohno, K.2    Ohkuma, M.3    Chijiiwa, Y.4    Torikata, T.5
  • 34
    • 1642439861 scopus 로고    scopus 로고
    • The lysozyme of the starfish Asterias rubens. A paradygmatic type i lysozyme
    • Bachali S., Bailly X., Jolles J., Jolles P., and Deutsch J.S. The lysozyme of the starfish Asterias rubens. A paradygmatic type i lysozyme. Eur J Biochem 271 2 (2004) 237-242
    • (2004) Eur J Biochem , vol.271 , Issue.2 , pp. 237-242
    • Bachali, S.1    Bailly, X.2    Jolles, J.3    Jolles, P.4    Deutsch, J.S.5
  • 36
    • 1642389872 scopus 로고    scopus 로고
    • Effect of experimental microbial challenge on the expression of defense molecules in Eisenia foetida earthworm
    • Köhlerova P., Beschin A., Šilerová M., De Baetselier P., and Bilej M. Effect of experimental microbial challenge on the expression of defense molecules in Eisenia foetida earthworm. Dev Comp Immunol 28 (2004) 701-711
    • (2004) Dev Comp Immunol , vol.28 , pp. 701-711
    • Köhlerova, P.1    Beschin, A.2    Šilerová, M.3    De Baetselier, P.4    Bilej, M.5


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