메뉴 건너뛰기




Volumn 246, Issue 3, 1997, Pages 756-762

Sequence and expression of an Eisenia-fetida-derived cDNA clone that encodes the 40-kDa fetidin antibacterial protein

Author keywords

cDNA cloning; Gene expression; Peroxidase; Polymorphism

Indexed keywords

BACTERIAL PROTEIN; COMPLEMENTARY DNA; GLYCOPROTEIN; PEROXIDASE;

EID: 0030904254     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1997.00756.x     Document Type: Article
Times cited : (62)

References (40)
  • 1
    • 0026653625 scopus 로고
    • Les peptides antibactériens inductibles des insectes
    • Hoffmann, J. A., Dimarcq, J. L. & Bulet, P. (1992) Les peptides antibactériens inductibles des insectes, Med. Sci. 8, 432-439.
    • (1992) Med. Sci. , vol.8 , pp. 432-439
    • Hoffmann, J.A.1    Dimarcq, J.L.2    Bulet, P.3
  • 2
    • 0028933794 scopus 로고
    • Peptide antibiotics and their role in innate immunity
    • Boman, G. H. (1995) Peptide antibiotics and their role in innate immunity, Annu. Rev. Immunol. 13, 61-92.
    • (1995) Annu. Rev. Immunol. , vol.13 , pp. 61-92
    • Boman, G.H.1
  • 3
    • 0029842737 scopus 로고    scopus 로고
    • A member of the arthropod defensin family from edible Mediterranean mussels (Mytilus galloprovincialis)
    • Hubert, F., Noel, T. & Roch, P. (1996) A member of the arthropod defensin family from edible Mediterranean mussels (Mytilus galloprovincialis), Eur. J. Biol. 240, 302-306.
    • (1996) Eur. J. Biol. , vol.240 , pp. 302-306
    • Hubert, F.1    Noel, T.2    Roch, P.3
  • 5
    • 0025693237 scopus 로고
    • Hemolin: An insect immune protein belonging to the immunoglobulin superfamily
    • Sun, S. C., Lindström, I., Boman, H. G., Faye, I. & Schmidt, O. (1990) Hemolin: an insect immune protein belonging to the immunoglobulin superfamily, Science 250, 1729-1732.
    • (1990) Science , vol.250 , pp. 1729-1732
    • Sun, S.C.1    Lindström, I.2    Boman, H.G.3    Faye, I.4    Schmidt, O.5
  • 6
    • 0018820115 scopus 로고
    • Insect immunity: Purification and properties of three inducible bactericidal proteins from hemolymph of immunized pupae of Hyalophora cecropia
    • Hultmark, D., Steiner, H., Rasmuson, T. & Boman, H. G. (1980) Insect immunity: purification and properties of three inducible bactericidal proteins from hemolymph of immunized pupae of Hyalophora cecropia, Eur. J. Biochem. 106, 7-16.
    • (1980) Eur. J. Biochem. , vol.106 , pp. 7-16
    • Hultmark, D.1    Steiner, H.2    Rasmuson, T.3    Boman, H.G.4
  • 7
    • 0020355347 scopus 로고
    • Insect immunity: Isolation and structure of cecropins B and D from pupae of Chinese oak silk moth, Antheraea pernyi
    • Qu, X. M., Steiner, H., Engström, A., Bennich, H. & Boman, H. G. (1982) Insect immunity: isolation and structure of cecropins B and D from pupae of Chinese oak silk moth, Antheraea pernyi, Eur. J. Biochem. 127, 219-224.
    • (1982) Eur. J. Biochem. , vol.127 , pp. 219-224
    • Qu, X.M.1    Steiner, H.2    Engström, A.3    Bennich, H.4    Boman, H.G.5
  • 8
    • 0020686109 scopus 로고
    • Insect immunity: Attacins, a family of antibacterial proteins from Hyalophora cecropia
    • Hultmark, D., Engström, A., Anderson, K., Steiner, H., Bennich, H. & Boman, H. G. (1983) Insect immunity: attacins, a family of antibacterial proteins from Hyalophora cecropia, EMBO J. 2, 571-576.
    • (1983) EMBO J. , vol.2 , pp. 571-576
    • Hultmark, D.1    Engström, A.2    Anderson, K.3    Steiner, H.4    Bennich, H.5    Boman, H.G.6
  • 9
    • 0024286601 scopus 로고
    • Insect immunity. Purification and characterization of a family of novel inducible antibacterial proteins from immunized larvae of the dipteran Phormia terranovae and complete amino acid sequence of the predominant member, diptericin A
    • Dimarcq, J. L., Keppi, E., Dunbar, B., Lambert, J., Reichhart, J. M., Hoffmann, D., Rankine, S. M., Hergill, J. E. & Hoffmann, J. A. (1988) Insect immunity. Purification and characterization of a family of novel inducible antibacterial proteins from immunized larvae of the dipteran Phormia terranovae and complete amino acid sequence of the predominant member, diptericin A, Eur. J. Biochem. 171, 17-22.
    • (1988) Eur. J. Biochem. , vol.171 , pp. 17-22
    • Dimarcq, J.L.1    Keppi, E.2    Dunbar, B.3    Lambert, J.4    Reichhart, J.M.5    Hoffmann, D.6    Rankine, S.M.7    Hergill, J.E.8    Hoffmann, J.A.9
  • 11
    • 0030003347 scopus 로고    scopus 로고
    • Cloning of the gene encoding the antibacterial peptide drosocin involved in Drosophila immunity
    • Charlet, M., Lagueux, M., Reichhart, J. M., Hoffmann, D., Braun, A. & Meister, M. (1996) Cloning of the gene encoding the antibacterial peptide drosocin involved in Drosophila immunity, Eur. J. Biochem. 241, 699-706.
    • (1996) Eur. J. Biochem. , vol.241 , pp. 699-706
    • Charlet, M.1    Lagueux, M.2    Reichhart, J.M.3    Hoffmann, D.4    Braun, A.5    Meister, M.6
  • 12
    • 0014433658 scopus 로고
    • Aspects humoraux et cellulaires d'une immunité naturelle non spécifique chez l'oligochète Eisenia fetida (Sav)
    • Du Pasquier, L. & Duprat, P. (1968) Aspects humoraux et cellulaires d'une immunité naturelle non spécifique chez l'oligochète Eisenia fetida (Sav), C. R. Acad. Sci. Paris 266, 538-542.
    • (1968) C. R. Acad. Sci. Paris , vol.266 , pp. 538-542
    • Du Pasquier, L.1    Duprat, P.2
  • 13
    • 0000006406 scopus 로고
    • Protein analysis of earthworm coelomic fluid. 2. Isolation and biochemical characterization of the Eisenia fetida andrei factor (EFAF)
    • Roch, P., Valembois, P., Davant, N. & Lassègues, M. (1981) Protein analysis of earthworm coelomic fluid. 2. Isolation and biochemical characterization of the Eisenia fetida andrei factor (EFAF), Comp. Biochem. Physiol. B Comp. Biochem. 69, 829-836.
    • (1981) Comp. Biochem. Physiol. B Comp. Biochem. , vol.69 , pp. 829-836
    • Roch, P.1    Valembois, P.2    Davant, N.3    Lassègues, M.4
  • 14
    • 0018563587 scopus 로고
    • Protein analysis of earthworm coelomic fluid. 1. Polymorphic system of the natural hemolysin of Eisenia fetida andrei
    • Roch, P. (1979) Protein analysis of earthworm coelomic fluid. 1. Polymorphic system of the natural hemolysin of Eisenia fetida andrei, Dev. Comp. Immunol. 3, 599-608.
    • (1979) Dev. Comp. Immunol. , vol.3 , pp. 599-608
    • Roch, P.1
  • 15
    • 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., Lassègues, M. & Valembois, P. (1997) Purification, characterization and activities of two hemolytic and antibacterial proteins from coelomic fluid of the annelid Eisenia fetida andrei, Biochim. Biophys. Acta 1337, 123-132.
    • (1997) Biochim. Biophys. Acta , vol.1337 , pp. 123-132
    • Milochau, A.1    Lassègues, M.2    Valembois, P.3
  • 16
  • 17
    • 0002705972 scopus 로고
    • Simultaneous existence of hemolysis and hemagglutinins in the coelomic fluid and the cocoon albumen of the earthworm Eisenia fetida andrei
    • Valembois, P., Roch, P. & Lassègues, M. (1984) Simultaneous existence of hemolysis and hemagglutinins in the coelomic fluid and the cocoon albumen of the earthworm Eisenia fetida andrei, Comp. Biochem. Physiol. A Comp. Physiol. 78, 141-145.
    • (1984) Comp. Biochem. Physiol. A Comp. Physiol. , vol.78 , pp. 141-145
    • Valembois, P.1    Roch, P.2    Lassègues, M.3
  • 18
  • 19
    • 0012753229 scopus 로고
    • Hemolytic function of opsonizing proteins of earthworm's coelomic fluid
    • Sinkora, M., Bilej, M., Tuckova, L. & Romanovsky, A. (1993) Hemolytic function of opsonizing proteins of earthworm's coelomic fluid, Cell Biol. Int. Rep. 14, 831-837.
    • (1993) Cell Biol. Int. Rep. , vol.14 , pp. 831-837
    • Sinkora, M.1    Bilej, M.2    Tuckova, L.3    Romanovsky, A.4
  • 20
    • 38249022982 scopus 로고
    • Antibacterial activity of Eisenia fetida andrei coelomic fluid: Specificity of the induced activity
    • Lassègues, M., Roch, P. & Valembois, P. (1989) Antibacterial activity of Eisenia fetida andrei coelomic fluid: specificity of the induced activity, J. Invertebr. Pathol. 54, 28-31.
    • (1989) J. Invertebr. Pathol. , vol.54 , pp. 28-31
    • Lassègues, M.1    Roch, P.2    Valembois, P.3
  • 21
    • 0025021320 scopus 로고
    • Antibacterial activity of Eisenia fetida andrei coelomic fluid: Transcription and translation regulation of lysozyme and proteins evidenced after bacterial infestation
    • Hirigoyenberry, F., Lassalle, F. & Lassègues, M. (1990) Antibacterial activity of Eisenia fetida andrei coelomic fluid: transcription and translation regulation of lysozyme and proteins evidenced after bacterial infestation, Comp. Biochem. Physiol. B Comp. Biochem. 95, 71-75.
    • (1990) Comp. Biochem. Physiol. B Comp. Biochem. , vol.95 , pp. 71-75
    • Hirigoyenberry, F.1    Lassalle, F.2    Lassègues, M.3
  • 22
    • 0018639079 scopus 로고
    • Isolation of biologically active ribonucleic acid from sources enriched in ribonuclease
    • Chirgwin, J. M., Przybyla, A. E., MacDonald, R. J. & Rutter, W. J. (1979) Isolation of biologically active ribonucleic acid from sources enriched in ribonuclease, Biochemistry 18, 5294-5299.
    • (1979) Biochemistry , vol.18 , pp. 5294-5299
    • Chirgwin, J.M.1    Przybyla, A.E.2    MacDonald, R.J.3    Rutter, W.J.4
  • 23
    • 0015356037 scopus 로고
    • Purification of biological active globin messenger RNA by chromatography on oligo-thymidilic acid-cellulose
    • Aviv, H. & Leder, P (1972) Purification of biological active globin messenger RNA by chromatography on oligo-thymidilic acid-cellulose, Proc. Natl Acad. Sci. USA 69, 1408-1412.
    • (1972) Proc. Natl Acad. Sci. USA , vol.69 , pp. 1408-1412
    • Aviv, H.1    Leder, P.2
  • 24
    • 0000182975 scopus 로고
    • XL1 Blue: A high efficiency plasmid transforming recA Escherichia coli strain with β-galactosidase selection
    • Bullock, W. O., Fernandez, J. M. & Short, J. M. (1987) XL1 Blue: A high efficiency plasmid transforming recA Escherichia coli strain with β-galactosidase selection, Biotechniques 5, 376.
    • (1987) Biotechniques , vol.5 , pp. 376
    • Bullock, W.O.1    Fernandez, J.M.2    Short, J.M.3
  • 25
    • 0002353530 scopus 로고
    • Antibacterial activity of Eisenia fetida andrei coelomic fluid: Immunological study of two major antibacterial proteins
    • Hirigoyenberry, F., Lassègues, M. & Roch, P. (1992) Antibacterial activity of Eisenia fetida andrei coelomic fluid: immunological study of two major antibacterial proteins, J. Invertebr. Pathol. 59, 69-74.
    • (1992) J. Invertebr. Pathol. , vol.59 , pp. 69-74
    • Hirigoyenberry, F.1    Lassègues, M.2    Roch, P.3
  • 28
    • 0022003140 scopus 로고
    • Deglycosylation of asparagine-linked glycans by peptide: N-glycosidase F
    • Tarentino, A. L. (1985) Deglycosylation of asparagine-linked glycans by peptide: N-glycosidase F, Biochemistry 24, 4665-4671.
    • (1985) Biochemistry , vol.24 , pp. 4665-4671
    • Tarentino, A.L.1
  • 30
    • 0014548372 scopus 로고
    • Glycoprotein staining following electrophoresis on acrylamide gels
    • Zacharius, R. M., Zell, T. E., Morrison, J. H. & Woddlock, J. J. (1969) Glycoprotein staining following electrophoresis on acrylamide gels, Anal. Biochem. 30, 148-152.
    • (1969) Anal. Biochem. , vol.30 , pp. 148-152
    • Zacharius, R.M.1    Zell, T.E.2    Morrison, J.H.3    Woddlock, J.J.4
  • 32
    • 0022427616 scopus 로고
    • Plant peroxidases: Their primary, secondary and tertiary structures, and relation to cytochrome c peroxidase
    • Welinder, K. G. (1985) Plant peroxidases: their primary, secondary and tertiary structures, and relation to cytochrome c peroxidase, Eur. J. Biochem. 151, 498-505.
    • (1985) Eur. J. Biochem. , vol.151 , pp. 498-505
    • Welinder, K.G.1
  • 33
    • 0029795495 scopus 로고    scopus 로고
    • A novel protein, lysenin, that causes contraction of the isolated rat aorta: Its purification from the coelomic fluid of the earthworm, Eisenia fetida
    • Sekizawa, Y., Hagiwara, K., Nakajima, T. & Kobayashi, H. (1996) A novel protein, lysenin, that causes contraction of the isolated rat aorta: its purification from the coelomic fluid of the earthworm, Eisenia fetida, Biomed. Res. 17, 197-203.
    • (1996) Biomed. Res. , vol.17 , pp. 197-203
    • Sekizawa, Y.1    Hagiwara, K.2    Nakajima, T.3    Kobayashi, H.4
  • 34
    • 0026021437 scopus 로고
    • Evidence and cellular localization of an oxidative activity in the coelomic fluid of the earthworm Eisenia fetida andrei
    • Valembois, P., Seymour, J. & Roch, P. (1991) Evidence and cellular localization of an oxidative activity in the coelomic fluid of the earthworm Eisenia fetida andrei, J. Invertebr. Pathol. 57, 177-183.
    • (1991) J. Invertebr. Pathol. , vol.57 , pp. 177-183
    • Valembois, P.1    Seymour, J.2    Roch, P.3
  • 35
    • 0028080849 scopus 로고
    • Carbohydrate moiety of peanut peroxidase necessary for enzyme activity
    • Van Huystee, R. B. & Wan, L. (1994) Carbohydrate moiety of peanut peroxidase necessary for enzyme activity, C. R. Acad. Sci. Paris 317, 789-794.
    • (1994) C. R. Acad. Sci. Paris , vol.317 , pp. 789-794
    • Van Huystee, R.B.1    Wan, L.2
  • 36
    • 0024294403 scopus 로고
    • Probing structure-function relations in heme-containing oxygenases and peroxidases
    • Dawson, J. H. (1988) Probing structure-function relations in heme-containing oxygenases and peroxidases, Science 240, 433-439.
    • (1988) Science , vol.240 , pp. 433-439
    • Dawson, J.H.1
  • 37
    • 0025188055 scopus 로고
    • Structural homology among the peroxidase enzyme family revealed by hydrophobic cluster analysis
    • Henrissat, B., Saloheimo, M., Lavaitte, M. & Knowles, J. K. C. (1990) Structural homology among the peroxidase enzyme family revealed by hydrophobic cluster analysis, Proteins 8, 251-257.
    • (1990) Proteins , vol.8 , pp. 251-257
    • Henrissat, B.1    Saloheimo, M.2    Lavaitte, M.3    Knowles, J.K.C.4
  • 39
    • 0025995263 scopus 로고
    • Bacterial catalase-peroxidases are gene duplicated members of the plant peroxidase superfamily
    • Welinder, K. G. (1991) Bacterial catalase-peroxidases are gene duplicated members of the plant peroxidase superfamily, Biochim. Biophys. Acta 1080, 215-220.
    • (1991) Biochim. Biophys. Acta , vol.1080 , pp. 215-220
    • Welinder, K.G.1
  • 40
    • 0024505540 scopus 로고
    • Peroxidases enhance macrophage-mediated cytotoxicity via induction of tumor necrosis factor
    • Lefkowitz, D. L., Mone, J., Mills, K., Hsieh, T. C. & Lefkowitz, S. (1989) Peroxidases enhance macrophage-mediated cytotoxicity via induction of tumor necrosis factor, Proc. Soc. Exp. Biol. Med. 190, 144-149.
    • (1989) Proc. Soc. Exp. Biol. Med. , vol.190 , pp. 144-149
    • Lefkowitz, D.L.1    Mone, J.2    Mills, K.3    Hsieh, T.C.4    Lefkowitz, S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.