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Volumn 144, Issue 2, 2006, Pages 199-205

Characterization and cDNA cloning of hinnavin II, a cecropin family antibacterial peptide from the cabbage butterfly, Artogeia rapae

Author keywords

5 rapid amplification of cDNA ends (RACE); Antibacterial peptide; Artogeia rapae; Cecropin; Hinnavin II; Hinnavin II gene; Insect immunity; MALDI MS

Indexed keywords

ANTIINFECTIVE AGENT; CECROPIN; COMPLEMENTARY DNA; HINNAVIN II; LYSOZYME; UNCLASSIFIED DRUG;

EID: 33646526755     PISSN: 10964959     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cbpb.2006.02.010     Document Type: Article
Times cited : (24)

References (38)
  • 1
    • 0037362455 scopus 로고    scopus 로고
    • Ascaris nematodes from pig and human make three antibacterial peptides: isolation of cecropin P1 and two ASABF peptides
    • Andersson M., Boman A., and Boman H.G. Ascaris nematodes from pig and human make three antibacterial peptides: isolation of cecropin P1 and two ASABF peptides. Cell. Mol. Life Sci. 60 (2003) 599-606
    • (2003) Cell. Mol. Life Sci. , vol.60 , pp. 599-606
    • Andersson, M.1    Boman, A.2    Boman, H.G.3
  • 2
    • 0031592754 scopus 로고    scopus 로고
    • Hinnavin II, an antibacterial peptide from cabbage butterfly, Artogeia rapae
    • Bang I.S., Son S.Y., and Yoe S.M. Hinnavin II, an antibacterial peptide from cabbage butterfly, Artogeia rapae. Mol. Cells 7 (1997) 509-513
    • (1997) Mol. Cells , vol.7 , pp. 509-513
    • Bang, I.S.1    Son, S.Y.2    Yoe, S.M.3
  • 3
    • 0002905116 scopus 로고
    • Cecropins: antibacterial peptides from insects and pigs
    • Hoffmann J.A., Janeway C.A., and Natori S. (Eds), R.G. Landes & Company
    • Boman H.G. Cecropins: antibacterial peptides from insects and pigs. In: Hoffmann J.A., Janeway C.A., and Natori S. (Eds). Phylogenetic Perspectives in Immunity: The Insect Host Defense (1994), R.G. Landes & Company 43-65
    • (1994) Phylogenetic Perspectives in Immunity: The Insect Host Defense , pp. 43-65
    • Boman, H.G.1
  • 8
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein dye binding
    • Bradford M. A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein dye binding. Anal. Biochem. 72 (1976) 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.1
  • 10
    • 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. C 125 (2000) 287-297
    • (2000) Comp. Biochem. Physiol. 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
  • 11
    • 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
  • 12
    • 0001999318 scopus 로고
    • Fate of bacteria injected into naive and immunized larvae of the tobacco hornworm Manduca sexta
    • Dunn P.E., and Drake D.R. Fate of bacteria injected into naive and immunized larvae of the tobacco hornworm Manduca sexta. J. Invertebr. Pathol. 41 (1983) 77-85
    • (1983) J. Invertebr. Pathol. , vol.41 , pp. 77-85
    • Dunn, P.E.1    Drake, D.R.2
  • 13
    • 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
  • 15
    • 0027968068 scopus 로고
    • Clustal W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Higgins D., Thompson J., Gibson T., 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 (1994) 4673-4680
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Higgins, D.1    Thompson, J.2    Gibson, T.3    Thompson, J.D.4    Higgins, D.G.5    Gibson, T.J.6
  • 16
    • 0018820115 scopus 로고
    • Insect immunity: purification and properties of three inducible bacterial proteins from hemolymph of immunized pupae of Hyalophora cecropia
    • Hultmark D., Steiner H., Rasmuson T., and Boman H.G. Insect immunity: purification and properties of three inducible bacterial proteins from hemolymph of immunized pupae of Hyalophora cecropia. Eur. J. Biochem. 106 (1980) 7-16
    • (1980) Eur. J. Biochem. , vol.106 , pp. 7-16
    • Hultmark, D.1    Steiner, H.2    Rasmuson, T.3    Boman, H.G.4
  • 17
    • 0020366780 scopus 로고
    • Insect immunity: isolation and structure of cecropin D and four minor antibacterial components from cecropia pupae
    • Hultmark D., Engstrom A., Bennich H., Kapur R., and Boman H.G. Insect immunity: isolation and structure of cecropin D and four minor antibacterial components from cecropia pupae. Eur. J. Biochem. 127 (1982) 207-217
    • (1982) Eur. J. Biochem. , vol.127 , pp. 207-217
    • Hultmark, D.1    Engstrom, A.2    Bennich, H.3    Kapur, R.4    Boman, H.G.5
  • 18
    • 0020686109 scopus 로고
    • Insect immunity: attacins, a family of antibacterial proteins from Hyalophora cecropia
    • Hultmark D., Engstrom A., Anderson K., Steiner H., Bennich H., and Boman H.G. Insect immunity: attacins, a family of antibacterial proteins from Hyalophora cecropia. EMBO J. 2 (1983) 571-576
    • (1983) EMBO J. , vol.2 , pp. 571-576
    • Hultmark, D.1    Engstrom, A.2    Anderson, K.3    Steiner, H.4    Bennich, H.5    Boman, H.G.6
  • 19
    • 0030087789 scopus 로고    scopus 로고
    • PCR differential display of immune gene expression in Trichoplusia ni
    • Kang D., Liu G., Gunne H., and Steiner H. PCR differential display of immune gene expression in Trichoplusia ni. Insect Biochem. Mol. Biol. 26 (1996) 177-184
    • (1996) Insect Biochem. Mol. Biol. , vol.26 , pp. 177-184
    • Kang, D.1    Liu, G.2    Gunne, H.3    Steiner, H.4
  • 20
    • 33646519353 scopus 로고    scopus 로고
    • Insect immune activation by recombinant apolipophorin-III and its application to pest control in Hyphantria cunea
    • Kang Y.J., Kim H.J., and Seo S.J. Insect immune activation by recombinant apolipophorin-III and its application to pest control in Hyphantria cunea. Korean J. Entomol. 33 (2003) 205-213
    • (2003) Korean J. Entomol. , vol.33 , pp. 205-213
    • Kang, Y.J.1    Kim, H.J.2    Seo, S.J.3
  • 21
    • 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
  • 22
    • 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
  • 23
    • 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., Kim M.K., Park D.S., Oh H.W., 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    Kim, M.K.3    Park, D.S.4    Oh, H.W.5    Park, H.Y.6
  • 24
    • 23944461543 scopus 로고    scopus 로고
    • Cecropin P1 and novel nematode cecropins: a bacteria-inducible antimicrobial peptide family in the nematode Ascaris suum
    • Pillai A., Ueno S., Zhang H., Lee J.M., and Kato Y. Cecropin P1 and novel nematode cecropins: a bacteria-inducible antimicrobial peptide family in the nematode Ascaris suum. Biochem. J. 390 (2005) 207-214
    • (2005) Biochem. J. , vol.390 , pp. 207-214
    • Pillai, A.1    Ueno, S.2    Zhang, H.3    Lee, J.M.4    Kato, Y.5
  • 26
    • 0020355347 scopus 로고
    • Insect immunity: isolation and structure of cecropins B and D from pupae of the Chinese oak silk moth, Antheraea pernyi
    • Qu Z., Steiner H., Engstrom A., Bennich H., and Boman H.G. Insect immunity: isolation and structure of cecropins B and D from pupae of the Chinese oak silk moth, Antheraea pernyi. Eur. J. Biochem. 127 (1982) 219-224
    • (1982) Eur. J. Biochem. , vol.127 , pp. 219-224
    • Qu, Z.1    Steiner, H.2    Engstrom, A.3    Bennich, H.4    Boman, H.G.5
  • 28
    • 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
  • 29
    • 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
  • 30
    • 0034004954 scopus 로고    scopus 로고
    • Antibacterial and antimembrane activities of cecropin A in Escherichia coli
    • Silvestro L., Weiser J.N., and Axelsen P.H. Antibacterial and antimembrane activities of cecropin A in Escherichia coli. Antimicrob. Agents Chemother. 44 (2000) 602-607
    • (2000) Antimicrob. Agents Chemother. , vol.44 , pp. 602-607
    • Silvestro, L.1    Weiser, J.N.2    Axelsen, P.H.3
  • 31
    • 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
  • 32
    • 0026664785 scopus 로고
    • Isolation and nucleotide sequence of cecropin B cDNA clones from the silkworm, Bombyx mori
    • Taniai K., Kato Y., Hirochika H., and Yamakawa M. Isolation and nucleotide sequence of cecropin B cDNA clones from the silkworm, Bombyx mori. Biochim. Biophys. Acta 1132 (1992) 203-206
    • (1992) Biochim. Biophys. Acta , vol.1132 , pp. 203-206
    • Taniai, K.1    Kato, Y.2    Hirochika, H.3    Yamakawa, M.4
  • 33
    • 0023975852 scopus 로고
    • The structure of the gene for cecropin B, an antibacterial immune protein from Hyalophora cecropia
    • Xanthopoulos K.G., Lee J.Y., Gan R., Kockum K., Faye I., and Boman H.G. The structure of the gene for cecropin B, an antibacterial immune protein from Hyalophora cecropia. Eur. J. Biochem. 172 (1988) 371-376
    • (1988) Eur. J. Biochem. , vol.172 , pp. 371-376
    • Xanthopoulos, K.G.1    Lee, J.Y.2    Gan, R.3    Kockum, K.4    Faye, I.5    Boman, H.G.6
  • 34
    • 0028484005 scopus 로고
    • Cloning of cDNAs for cecropins A and B, and expression of the genes in the silkworm, Bombyx mori
    • Yamano Y., Matsumoto M., Inoue K., Kawabata T., and Morishima I. Cloning of cDNAs for cecropins A and B, and expression of the genes in the silkworm, Bombyx mori. Biosci. Biotechnol. Biochem. 58 (1994) 1476-1478
    • (1994) Biosci. Biotechnol. Biochem. , vol.58 , pp. 1476-1478
    • Yamano, Y.1    Matsumoto, M.2    Inoue, K.3    Kawabata, T.4    Morishima, I.5
  • 36
    • 0642334705 scopus 로고
    • Induction and purification of antibacterial proteins in larval haemolymph of cabbage butterfly, Artogeia rapae
    • Yoe S.M., Bang I.S., Chang B.S., and Cho E.J. Induction and purification of antibacterial proteins in larval haemolymph of cabbage butterfly, Artogeia rapae. Korean J. Zool. 38 (1995) 305-312
    • (1995) Korean J. Zool. , vol.38 , pp. 305-312
    • Yoe, S.M.1    Bang, I.S.2    Chang, B.S.3    Cho, E.J.4
  • 37
    • 0242428877 scopus 로고    scopus 로고
    • Purification and characterization of two lysozyme from larval haemolymph of cabbage butterfly, Artogeia rapae
    • Yoe S.M., Bang I.S., Kang C.S., and Kim H.J. Purification and characterization of two lysozyme from larval haemolymph of cabbage butterfly, Artogeia rapae. Mol. Cells 6 (1996) 609-614
    • (1996) Mol. Cells , vol.6 , pp. 609-614
    • Yoe, S.M.1    Bang, I.S.2    Kang, C.S.3    Kim, H.J.4
  • 38
    • 0030836343 scopus 로고    scopus 로고
    • cDNA cloning of three cecropin-like antimicrobial peptides (Styelins) from the tunicate, Styela clava
    • Zhao C., Liaw L., Lee I.H., and Lehrer R.I. cDNA cloning of three cecropin-like antimicrobial peptides (Styelins) from the tunicate, Styela clava. FEBS Lett. 412 (1997) 144-148
    • (1997) FEBS Lett. , vol.412 , pp. 144-148
    • Zhao, C.1    Liaw, L.2    Lee, I.H.3    Lehrer, R.I.4


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