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Volumn 148, Issue 4, 2007, Pages 417-425

Characterization and expression of a cecropin-like gene from Helicoverpa armigera

Author keywords

Cecropin; EMSA; Helicoverpa armigera; RT PCR; TAIL PCR

Indexed keywords

AMINO ACID; BLOOD CLOTTING FACTOR 10A; CECROPIN; GENOMIC DNA; GREEN FLUORESCENT PROTEIN; HACD PROTEIN; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; INSECT PROTEIN; INTERLEUKIN 6; NUCLEAR PROTEIN; PROTEIN; UNCLASSIFIED DRUG;

EID: 35648995342     PISSN: 10964959     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cbpb.2007.07.010     Document Type: Article
Times cited : (23)

References (35)
  • 2
    • 0028933794 scopus 로고
    • Peptide antibiotics and their role in innate immunity
    • Boman H.G. Peptide antibiotics and their role in innate immunity. Annu. Rev. Immunol. 13 (1995) 61-92
    • (1995) Annu. Rev. Immunol. , vol.13 , pp. 61-92
    • Boman, H.G.1
  • 3
    • 0036848010 scopus 로고    scopus 로고
    • Sequential activation of signaling pathways during innate immune responses in Drosophila
    • Boutros M., Agaisse H., and Perrimon N. Sequential activation of signaling pathways during innate immune responses in Drosophila. Dev. Cell. 3 (2002) 711-722
    • (2002) Dev. Cell. , vol.3 , pp. 711-722
    • Boutros, M.1    Agaisse, H.2    Perrimon, N.3
  • 5
    • 0034057767 scopus 로고    scopus 로고
    • Antibacterial properties and partial cDNA sequences of cecropin-like antibacterial peptides from the common cutworm, Spodoptera litura
    • Choi C.S., Lee I.H., Kim E., Kim S.I., and Kim H.R. Antibacterial properties and partial cDNA sequences of cecropin-like antibacterial peptides from the common cutworm, Spodoptera litura. Comp. Biochem. Physiol. Part C 125 (2000) 287-297
    • (2000) Comp. Biochem. Physiol. Part C , vol.125 , pp. 287-297
    • Choi, C.S.1    Lee, I.H.2    Kim, E.3    Kim, S.I.4    Kim, H.R.5
  • 6
    • 0024297452 scopus 로고
    • A family of bacteria-regulated, cecropin D-like peptides from Manduca sexta
    • Dickinson L., Russell V., and Dunn P.E. A family of bacteria-regulated, cecropin D-like peptides from Manduca sexta. J. Biol. Chem. 263 (1988) 19424-19429
    • (1988) J. Biol. Chem. , vol.263 , pp. 19424-19429
    • Dickinson, L.1    Russell, V.2    Dunn, P.E.3
  • 7
    • 0026047489 scopus 로고
    • The cecropin locus. Cloning and expression of a gene cluster encoding three antibacterial peptides in Hyalophora cecropia
    • Gudmundsson G.H., Lidholm D.A., Asling B., Gan R., and Boman H.G. The cecropin locus. Cloning and expression of a gene cluster encoding three antibacterial peptides in Hyalophora cecropia. J. Biol. Chem. 266 (1991) 11510-11517
    • (1991) J. Biol. Chem. , vol.266 , pp. 11510-11517
    • Gudmundsson, G.H.1    Lidholm, D.A.2    Asling, B.3    Gan, R.4    Boman, H.G.5
  • 8
    • 0029664501 scopus 로고    scopus 로고
    • Production in Escherichia of moricin, a novel type antibacterial peptide from the silkworm, Bombyx mori
    • Hara S., and Yamakawa M. Production in Escherichia of moricin, a novel type antibacterial peptide from the silkworm, Bombyx mori. Biochem. Biophys. Res. Commun. 220 (1996) 664-669
    • (1996) Biochem. Biophys. Res. Commun. , vol.220 , pp. 664-669
    • Hara, S.1    Yamakawa, M.2
  • 9
    • 0242581687 scopus 로고    scopus 로고
    • The immune response of Drosophila
    • Hoffmann J.A. The immune response of Drosophila. Nature 426 (2003) 33-38
    • (2003) Nature , vol.426 , pp. 33-38
    • Hoffmann, J.A.1
  • 10
    • 0027318549 scopus 로고
    • Immune reactions in Drosophila and other insects: a model for innate immunity
    • Hultmark D. Immune reactions in Drosophila and other insects: a model for innate immunity. Trends Genet. 9 (1993) 178-183
    • (1993) Trends Genet. , vol.9 , pp. 178-183
    • Hultmark, D.1
  • 11
    • 33747804308 scopus 로고    scopus 로고
    • Expression and characterization of a housefly cecropin gene in the methylotrophic yeast, Pichia pastoris
    • Jin F., Xu X., Zhang W., and Gu D. Expression and characterization of a housefly cecropin gene in the methylotrophic yeast, Pichia pastoris. Protein Expr. Purif. 49 (2006) 39-46
    • (2006) Protein Expr. Purif. , vol.49 , pp. 39-46
    • Jin, F.1    Xu, X.2    Zhang, W.3    Gu, D.4
  • 12
    • 0030861832 scopus 로고    scopus 로고
    • Adjacent GATA and kappa B-like motifs regulate the expression of a Drosophila immune gene
    • Kadalayil L., Petersen U.M., and Engstrom Y. Adjacent GATA and kappa B-like motifs regulate the expression of a Drosophila immune gene. Nucleic. Acids. Res. 25 (1997) 1233-1239
    • (1997) Nucleic. Acids. Res. , vol.25 , pp. 1233-1239
    • Kadalayil, L.1    Petersen, U.M.2    Engstrom, Y.3
  • 13
    • 0034913274 scopus 로고    scopus 로고
    • Drosophila immunity: two paths to NF-kappaB
    • Khush R.S., Leulier F., and Lemaitre B. Drosophila immunity: two paths to NF-kappaB. Trends Immunol. 22 (2001) 260-264
    • (2001) Trends Immunol. , vol.22 , pp. 260-264
    • Khush, R.S.1    Leulier, F.2    Lemaitre, B.3
  • 15
    • 0025190557 scopus 로고
    • The cecropin locus in Drosophila; a compact gene cluster involved in the response to infection
    • Kylsten P., Samakovlis C., and Hultmark D. The cecropin locus in Drosophila; a compact gene cluster involved in the response to infection. EMBO. J. 9 (1990) 217-224
    • (1990) EMBO. J. , vol.9 , pp. 217-224
    • Kylsten, P.1    Samakovlis, C.2    Hultmark, D.3
  • 16
    • 27644525031 scopus 로고    scopus 로고
    • Molecular cloning and characterization of cecropin from the housefly (Musca domestica), and its expression in Escherichia coli
    • Liang Y., Wang J.X., Zhao X.F., Du X.J., and Xue J.F. Molecular cloning and characterization of cecropin from the housefly (Musca domestica), and its expression in Escherichia coli. Dev. Comp. Immunol. 30 (2006) 249-257
    • (2006) Dev. Comp. Immunol. , vol.30 , pp. 249-257
    • Liang, Y.1    Wang, J.X.2    Zhao, X.F.3    Du, X.J.4    Xue, J.F.5
  • 17
    • 0035118326 scopus 로고    scopus 로고
    • Innate immune response of Aedes aegypti
    • Lowenberger C. Innate immune response of Aedes aegypti. Insect Biochem. Mol. Biol. 31 (2001) 219-229
    • (2001) Insect Biochem. Mol. Biol. , vol.31 , pp. 219-229
    • Lowenberger, C.1
  • 18
    • 33746677487 scopus 로고    scopus 로고
    • A novel association between clustered NF-kappaB and C/EBP binding sites is required for immune regulation of mosquito Defensin genes
    • Meredith J.M., Munks R.J., Grail W., Hurd H., Eggleston P., and Lehane M.J. A novel association between clustered NF-kappaB and C/EBP binding sites is required for immune regulation of mosquito Defensin genes. Insect Mol. Biol. 15 (2006) 393-401
    • (2006) Insect Mol. Biol. , vol.15 , pp. 393-401
    • Meredith, J.M.1    Munks, R.J.2    Grail, W.3    Hurd, H.4    Eggleston, P.5    Lehane, M.J.6
  • 19
    • 0025219035 scopus 로고
    • Isolation and structure of cecropins, inducible antibacterial peptides, from the silkworm, Bombyx mori
    • Morishima I., Suginaka S., Ueno T., and Hirano H. Isolation and structure of cecropins, inducible antibacterial peptides, from the silkworm, Bombyx mori. Comp. Biochem. Physiol. B 95 (1990) 551-554
    • (1990) Comp. Biochem. Physiol. B , vol.95 , pp. 551-554
    • Morishima, I.1    Suginaka, S.2    Ueno, T.3    Hirano, H.4
  • 20
    • 0029928757 scopus 로고    scopus 로고
    • The role of hemolymph coagulation in innate immunity
    • Muta T., and Iwanaga S. The role of hemolymph coagulation in innate immunity. Curr. Opin. Immunol. 8 (1996) 41-47
    • (1996) Curr. Opin. Immunol. , vol.8 , pp. 41-47
    • Muta, T.1    Iwanaga, S.2
  • 21
    • 2542523985 scopus 로고    scopus 로고
    • Effect of drastic sequence alteration and D-amino acid incorporation on the membrane binding behavior of lytic peptides
    • Papo N., and Shai Y. Effect of drastic sequence alteration and D-amino acid incorporation on the membrane binding behavior of lytic peptides. Biochemistry 43 (2004) 6393-6403
    • (2004) Biochemistry , vol.43 , pp. 6393-6403
    • Papo, N.1    Shai, Y.2
  • 22
    • 0031200945 scopus 로고    scopus 로고
    • Protein purification and cDNA cloning of a cecropin-like peptide from the larvae of fall webworm (Hyphantria cunea)
    • Park S.S., Shin S.W., Park D.S., Oh H.W., Boo K.S., and Park H.Y. Protein purification and cDNA cloning of a cecropin-like peptide from the larvae of fall webworm (Hyphantria cunea). Insect Biochem. Mol. Biol. 27 (1997) 711-720
    • (1997) Insect Biochem. Mol. Biol. , vol.27 , pp. 711-720
    • Park, S.S.1    Shin, S.W.2    Park, D.S.3    Oh, H.W.4    Boo, K.S.5    Park, H.Y.6
  • 23
    • 1042278915 scopus 로고    scopus 로고
    • The relationship between peptide structure and antibacterial activity
    • Powers J.P., and Hancock R.E. The relationship between peptide structure and antibacterial activity. Peptides 24 (2003) 1681-1691
    • (2003) Peptides , vol.24 , pp. 1681-1691
    • Powers, J.P.1    Hancock, R.E.2
  • 24
    • 2442573867 scopus 로고    scopus 로고
    • Characterization of a homologue of the Rel/NF-kB transcription factor from a beetle, Allomyrina dichotoma
    • Sagisaka A., Tanaka H., Furukawa S., and Yamakawa M. Characterization of a homologue of the Rel/NF-kB transcription factor from a beetle, Allomyrina dichotoma. Biochim. Biophys. Acta 1678 (2004) 85-93
    • (2004) Biochim. Biophys. Acta , vol.1678 , pp. 85-93
    • Sagisaka, A.1    Tanaka, H.2    Furukawa, S.3    Yamakawa, M.4
  • 26
    • 0035066909 scopus 로고    scopus 로고
    • Innate immunity and its evasion and suppression by hymenopteran endoparasitoids
    • Schmidt O., Theopold U., and Strand M. Innate immunity and its evasion and suppression by hymenopteran endoparasitoids. Bioessays 23 (2001) 344-351
    • (2001) Bioessays , vol.23 , pp. 344-351
    • Schmidt, O.1    Theopold, U.2    Strand, M.3
  • 27
    • 0032717886 scopus 로고    scopus 로고
    • Mechanism of the binding, insertion and destabilization of phospholipid bilayer membranes by alpha-helical antimicrobial and cell non-selective membrane-lytic peptides
    • Shai Y. Mechanism of the binding, insertion and destabilization of phospholipid bilayer membranes by alpha-helical antimicrobial and cell non-selective membrane-lytic peptides. Biochim. Biophys. Acta 1462 (1999) 55-70
    • (1999) Biochim. Biophys. Acta , vol.1462 , pp. 55-70
    • Shai, Y.1
  • 28
    • 0034824597 scopus 로고    scopus 로고
    • From "carpet" mechanism to de-novo designed diastereomeric cell-selective antimicrobial peptides
    • Shai Y., and Oren Z. From "carpet" mechanism to de-novo designed diastereomeric cell-selective antimicrobial peptides. Peptides 22 (2001) 1629-1641
    • (2001) Peptides , vol.22 , pp. 1629-1641
    • Shai, Y.1    Oren, Z.2
  • 29
    • 0019386682 scopus 로고
    • Sequence and specificity of two antibacterial proteins involved in insect immunity
    • Steiner H., Hultmark D., Engstrom A., Bennich H., and Boman H.G. Sequence and specificity of two antibacterial proteins involved in insect immunity. Nature 292 (1981) 246-248
    • (1981) Nature , vol.292 , pp. 246-248
    • Steiner, H.1    Hultmark, D.2    Engstrom, A.3    Bennich, H.4    Boman, H.G.5
  • 30
    • 0023864293 scopus 로고
    • Binding and action of cecropin and cecropin analogues: antibacterial peptides from insects
    • Steiner H., Andreu D., and Merrifield R.B. Binding and action of cecropin and cecropin analogues: antibacterial peptides from insects. Biochim. Biophys. Acta 939 (1988) 260-266
    • (1988) Biochim. Biophys. Acta , vol.939 , pp. 260-266
    • Steiner, H.1    Andreu, D.2    Merrifield, R.B.3
  • 33
    • 0031991399 scopus 로고    scopus 로고
    • Structure of genes for cecropin A and an inducible nuclear protein that binds to the promoter region of the genes from the silkworm, Bombyx mori
    • Yamano Y., Matsumoto M., Sasahara K., Sakamoto E., and Morishima I. Structure of genes for cecropin A and an inducible nuclear protein that binds to the promoter region of the genes from the silkworm, Bombyx mori. Biosci. Biotechnol. Biochem. 62 (1998) 237-241
    • (1998) Biosci. Biotechnol. Biochem. , vol.62 , pp. 237-241
    • Yamano, Y.1    Matsumoto, M.2    Sasahara, K.3    Sakamoto, E.4    Morishima, I.5
  • 34
    • 33646526755 scopus 로고    scopus 로고
    • Characterization and cDNA cloning of hinnavin II, a cecropin family antibacterial peptide from the cabbage butterfly, Artogeia rapae
    • Yoe S.M., Kang C.S., Han S.S., and Bang I.S. Characterization and cDNA cloning of hinnavin II, a cecropin family antibacterial peptide from the cabbage butterfly, Artogeia rapae. Comp. Biochem. Physiol. B 144 (2006) 199-205
    • (2006) Comp. Biochem. Physiol. B , vol.144 , pp. 199-205
    • Yoe, S.M.1    Kang, C.S.2    Han, S.S.3    Bang, I.S.4
  • 35
    • 0032577940 scopus 로고    scopus 로고
    • Determinants of recombinant production of antimicrobial cationic peptides and creation of peptide variants in bacteria
    • Zhang L., Falla T., Wu M., Fidai S., Burian J., Kay W., and Hancock R.E. Determinants of recombinant production of antimicrobial cationic peptides and creation of peptide variants in bacteria. Biochem. Biophys. Res. Commun. 247 (1998) 674-680
    • (1998) Biochem. Biophys. Res. Commun. , vol.247 , pp. 674-680
    • Zhang, L.1    Falla, T.2    Wu, M.3    Fidai, S.4    Burian, J.5    Kay, W.6    Hancock, R.E.7


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