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Volumn 266, Issue 2, 1999, Pages 616-623

Purification, cDNA cloning and modification of a defensin from the coconut rhinoceros beetle, Oryctes rhinoceros

Author keywords

Antibacterial peptide; CDNA cloning; Gene expression; Oryctes rhinoceros; Synthetic oligopeptides

Indexed keywords

COMPLEMENTARY DNA; DEFENSIN; ALANINE; LIPOSOME; LYSINE; MESSENGER RNA; PEPTIDE;

EID: 0033485381     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1999.00906.x     Document Type: Article
Times cited : (56)

References (36)
  • 1
    • 0028933794 scopus 로고
    • Peptide antibiotics and their role in innate immunity
    • 1. Boman, H.G. (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, H.G.1
  • 2
    • 0027409883 scopus 로고
    • Purification, sequence and antibacterial activity of two novel sapecin homologues from Sarcophaga embryonic cells: Similarity of sapecin B to charybdotoxin
    • 2. Yamada, K. & Natori, S. (1993) Purification, sequence and antibacterial activity of two novel sapecin homologues from Sarcophaga embryonic cells: similarity of sapecin B to charybdotoxin. Biochem. J. 291, 275-279.
    • (1993) Biochem. J. , vol.291 , pp. 275-279
    • Yamada, K.1    Natori, S.2
  • 4
    • 0030523012 scopus 로고    scopus 로고
    • Effect of moricin, a novel antibacterial peptide of Bombyx mori (Lepidoptera: Bombycidae) on the growth of methicillin-resistant Staphylococcus aureus (MRSA)
    • 4. Hara, S., Asaoka, A. & Yamakawa, M. (1996) Effect of moricin, a novel antibacterial peptide of Bombyx mori (Lepidoptera: Bombycidae) on the growth of methicillin-resistant Staphylococcus aureus (MRSA). Appl. Entomol. Zool. 31, 465-466.
    • (1996) Appl. Entomol. Zool. , vol.31 , pp. 465-466
    • Hara, S.1    Asaoka, A.2    Yamakawa, M.3
  • 5
    • 0026570489 scopus 로고
    • Shortened cecropin A-melittin hybrids. Significant size reduction retains potent antibacterial activity
    • 5. Andreu, D., Ubach, J., Boman, A., Wahlin, B., Wade, D., Merrifield, R.B. & Boman, H.G. (1992) Shortened cecropin A-melittin hybrids. Significant size reduction retains potent antibacterial activity. FEBS Lett. 296, 190-194.
    • (1992) FEBS Lett. , vol.296 , pp. 190-194
    • Andreu, D.1    Ubach, J.2    Boman, A.3    Wahlin, B.4    Wade, D.5    Merrifield, R.B.6    Boman, H.G.7
  • 6
    • 0030071417 scopus 로고    scopus 로고
    • Structure-activity analysis of thanatin, a 21-residue inducible insect defense peptide with sequence homology to frog skin antimicrobial peptides
    • 6. Fehlbaum, P., Bulet, P., Chernysh, S., Briand, J.P., Roussel, J.P., Letellier, L., Hetru, C. & Hoffmann, J.A. (1996) Structure-activity analysis of thanatin, a 21-residue inducible insect defense peptide with sequence homology to frog skin antimicrobial peptides. Proc. Natl Acad. Sci. USA 93, 1221-1225.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 1221-1225
    • Fehlbaum, P.1    Bulet, P.2    Chernysh, S.3    Briand, J.P.4    Roussel, J.P.5    Letellier, L.6    Hetru, C.7    Hoffmann, J.A.8
  • 7
    • 0029891059 scopus 로고    scopus 로고
    • Covalent structure, synthesis, and structure-function studies of mesentericin Y 105 (37), a defensive peptide from gram-positive bacteria Leuconostoc mesenteroides
    • 7. Fleury, F., Dayem, M.A., Montagne, J.J., Chaboisseau, E., Le Caer, J.P., Nicholas, P. & Delfour, A. (1996) Covalent structure, synthesis, and structure-function studies of mesentericin Y 105 (37), a defensive peptide from gram-positive bacteria Leuconostoc mesenteroides. J. Biol. Chem. 271, 14421-14429.
    • (1996) J. Biol. Chem. , vol.271 , pp. 14421-14429
    • Fleury, F.1    Dayem, M.A.2    Montagne, J.J.3    Chaboisseau, E.4    Le Caer, J.P.5    Nicholas, P.6    Delfour, A.7
  • 8
    • 0029947232 scopus 로고    scopus 로고
    • A class of highly potent antibacterial peptides derived from paradaxin, a pore-forming peptide isolated from Moses sole fish Pardachirus marmoratus
    • 8. Oren, Z. & Shai, Y. (1996) A class of highly potent antibacterial peptides derived from paradaxin, a pore-forming peptide isolated from Moses sole fish Pardachirus marmoratus. Eur. J. Biochem. 237, 303-310.
    • (1996) Eur. J. Biochem. , vol.237 , pp. 303-310
    • Oren, Z.1    Shai, Y.2
  • 9
    • 0025761657 scopus 로고
    • Cytolytic pore-forming proteins and peptides: Is there a common structural motif?
    • 9. Ojcius, D.M. & Young, J.D. (1991) Cytolytic pore-forming proteins and peptides: is there a common structural motif? Trends. Biochem. Sci. 16, 225-229.
    • (1991) Trends. Biochem. Sci. , vol.16 , pp. 225-229
    • Ojcius, D.M.1    Young, J.D.2
  • 10
    • 0027043261 scopus 로고
    • Design of model amphipathic peptides having potent antimicrobial activities
    • 10. Blondelle, S.E. & Houghten, R.A. (1992) Design of model amphipathic peptides having potent antimicrobial activities. Biochemistry 31, 12688-12694.
    • (1992) Biochemistry , vol.31 , pp. 12688-12694
    • Blondelle, S.E.1    Houghten, R.A.2
  • 11
    • 0028299333 scopus 로고
    • Characterization of the antimicrobial peptide derived from sapecin B, an antibacterial protein of Sarcophaga peregrina (flesh fly)
    • 11. Yamada, K. & Natori, S. (1994) Characterization of the antimicrobial peptide derived from sapecin B, an antibacterial protein of Sarcophaga peregrina (flesh fly). Biochem. J. 298, 623-628.
    • (1994) Biochem. J. , vol.298 , pp. 623-628
    • Yamada, K.1    Natori, S.2
  • 12
    • 0028088351 scopus 로고
    • Novel synthetic antimicrobial peptides effective against methicillin-resistant Staphylococcus aureus
    • 12. Alvarez-Bravo, J., Kurata, S. & Natori, S. (1994) Novel synthetic antimicrobial peptides effective against methicillin-resistant Staphylococcus aureus. Biochem. J. 302, 535-538.
    • (1994) Biochem. J. , vol.302 , pp. 535-538
    • Alvarez-Bravo, J.1    Kurata, S.2    Natori, S.3
  • 14
    • 0032528858 scopus 로고    scopus 로고
    • Identification and characterization of the antimicrobial peptide corresponding to C-terminal β-sheet domain to tenecin 1, an antibacterial protein of larvae of Tenebrio molitor
    • 14. Lee, K.H., Hong, S.Y., Oh, J.E., Kwon, M., Yoon, J.H., Lee, J., Lee, B.L. & Moon, H.M. (1998) Identification and characterization of the antimicrobial peptide corresponding to C-terminal β-sheet domain to tenecin 1, an antibacterial protein of larvae of Tenebrio molitor. Biochem. J. 334, 99-105.
    • (1998) Biochem. J. , vol.334 , pp. 99-105
    • Lee, K.H.1    Hong, S.Y.2    Oh, J.E.3    Kwon, M.4    Yoon, J.H.5    Lee, J.6    Lee, B.L.7    Moon, H.M.8
  • 15
    • 0033557958 scopus 로고    scopus 로고
    • Synthesis and characterization of bactericidal oligopeptides designed on the basis of an insect antibacterial peptide
    • 15. Saido-Sakanaka, H., Ishibashi, J., Sagisaka, A., Momotani, E. & Yamakawa, M. (1999) Synthesis and characterization of bactericidal oligopeptides designed on the basis of an insect antibacterial peptide. Biochem. J. 338, 29-33.
    • (1999) Biochem. J. , vol.338 , pp. 29-33
    • Saido-Sakanaka, H.1    Ishibashi, J.2    Sagisaka, A.3    Momotani, E.4    Yamakawa, M.5
  • 16
    • 0020366780 scopus 로고
    • Insect immunity: Isolation and structure of cecropin D and four minor antibacterial components from cecropia pupae
    • 16. Hultmark, D., Engström, A., Bennich, H., Kapur, R. & Boman, H.G. (1982) Insect immunity: isolation and structure of cecropin D and four minor antibacterial components from cecropia pupae. Eur. J. Biochem. 127, 207-217.
    • (1982) Eur. J. Biochem. , vol.127 , pp. 207-217
    • Hultmark, D.1    Engström, A.2    Bennich, H.3    Kapur, R.4    Boman, H.G.5
  • 17
    • 0029923481 scopus 로고    scopus 로고
    • High and low annealing temperatures increase both specificity and yield in touchdown and stepdown PCR
    • 17. Hecker, K.H. & Roux, K.H. (1996) High and low annealing temperatures increase both specificity and yield in touchdown and stepdown PCR. Biotechniques 20, 478-485.
    • (1996) Biotechniques , vol.20 , pp. 478-485
    • Hecker, K.H.1    Roux, K.H.2
  • 18
    • 0032080273 scopus 로고    scopus 로고
    • Molecular cloning and nucleotide sequence of a cytochrome P450 cDNA from a pyrethroid-resistant mosquito, Culex quinquefasciatus Say
    • 18. Kasai, S., Shono, T. & Yamakawa, M. (1998) Molecular cloning and nucleotide sequence of a cytochrome P450 cDNA from a pyrethroid-resistant mosquito, Culex quinquefasciatus Say. Insect Mol. Biol. 7, 185-190.
    • (1998) Insect Mol. Biol. , vol.7 , pp. 185-190
    • Kasai, S.1    Shono, T.2    Yamakawa, M.3
  • 19
    • 0009507733 scopus 로고
    • Characterization of the antibacterial protein of Sarcophaga peregrina (flesh fly)
    • 19. Yamada, K. & Natori, S. (1994) Characterization of the antibacterial protein of Sarcophaga peregrina (flesh fly). Biochem. J. 298, 1476-1478.
    • (1994) Biochem. J. , vol.298 , pp. 1476-1478
    • Yamada, K.1    Natori, S.2
  • 20
    • 49749180322 scopus 로고
    • A simplified spectro-metric determination of ester groups in lipids
    • 20. Snyder, F. & Stephens, N. (1959) A simplified spectro-metric determination of ester groups in lipids. Biochim. Biophys. Acta 34, 244-245.
    • (1959) Biochim. Biophys. Acta , vol.34 , pp. 244-245
    • Snyder, F.1    Stephens, N.2
  • 21
    • 0025752824 scopus 로고
    • A lipopolysaccharide (LPS)-resistant mutant isolated from a macrophage like cell line, J774.1, exhibits an altered activated-macrophage phenotype in response to LPS
    • 21. Amano, F. & Akamatsu, Y. (1991) A lipopolysaccharide (LPS)-resistant mutant isolated from a macrophage like cell line, J774.1, exhibits an altered activated-macrophage phenotype in response to LPS. Infect. Immun. 59, 2166-2174.
    • (1991) Infect. Immun. , vol.59 , pp. 2166-2174
    • Amano, F.1    Akamatsu, Y.2
  • 22
    • 0022577607 scopus 로고
    • A monosaccharide precursor of Escherichia coli lipid a has the ability to induce tumor-cytotoxic factor production by a murine macrophage-like cell line, J774.1
    • 22. Amano, F., Nishijima, M. & Akamatsu, Y. (1986) A monosaccharide precursor of Escherichia coli lipid A has the ability to induce tumor-cytotoxic factor production by a murine macrophage-like cell line, J774.1. J. Immunol. 136, 4122-4127.
    • (1986) J. Immunol. , vol.136 , pp. 4122-4127
    • Amano, F.1    Nishijima, M.2    Akamatsu, Y.3
  • 23
    • 0028069819 scopus 로고
    • Purification and molecular cloning of cDNA for an inducible antibacterial protein from larvae of the coleopteran, Tenebrio molitor
    • 23. Moon, H.J., Lee, S.Y., Kurata, S., Natori, S. & Lee, B.L. (1994) Purification and molecular cloning of cDNA for an inducible antibacterial protein from larvae of the coleopteran, Tenebrio molitor. J. Biochem. 116, 53-58.
    • (1994) J. Biochem. , vol.116 , pp. 53-58
    • Moon, H.J.1    Lee, S.Y.2    Kurata, S.3    Natori, S.4    Lee, B.L.5
  • 24
    • 0026329268 scopus 로고
    • Insect immunity. Isolation from a coleopteran insect of a novel inducible antibacterial peptide and of new members of the insect defensin family
    • 24. Bulet, P., Cociancich, S., Dimarcq, J.L., Lambert, J., Reichhart, J.M., Hoffmann, D., Hetru, C. & Hoffmann, J.A. (1991) Insect immunity. Isolation from a coleopteran insect of a novel inducible antibacterial peptide and of new members of the insect defensin family. J. Biol. Chem. 266, 24520-24525.
    • (1991) J. Biol. Chem. , vol.266 , pp. 24520-24525
    • Bulet, P.1    Cociancich, S.2    Dimarcq, J.L.3    Lambert, J.4    Reichhart, J.M.5    Hoffmann, D.6    Hetru, C.7    Hoffmann, J.A.8
  • 25
    • 0025311318 scopus 로고
    • A potent antibacterial protein in royal jelly. Purification and determination of the primary structure of royalisin
    • 25. Fujiwara, S., Imai, J., Yaeshima, T., Kawashima, T. & Kobayashi, K. (1990) A potent antibacterial protein in royal jelly. Purification and determination of the primary structure of royalisin. J. Biol. Chem. 265, 11333-11337.
    • (1990) J. Biol. Chem. , vol.265 , pp. 11333-11337
    • Fujiwara, S.1    Imai, J.2    Yaeshima, T.3    Kawashima, T.4    Kobayashi, K.5
  • 26
    • 0028304808 scopus 로고
    • Novel inducible antibacterial peptide from a hemipteran insect, the sap sucking-bug Pyrrhocoris aptarus
    • 26. Cociancich, S., Dupont, A., Hegy, G., Lanot, R., Holder, F., Hetru, C., Hoffmann, J.A. & Bulet, P. (1994) Novel inducible antibacterial peptide from a hemipteran insect, the sap sucking-bug Pyrrhocoris aptarus. Biochem. J. 300, 567-575.
    • (1994) Biochem. J. , vol.300 , pp. 567-575
    • Cociancich, S.1    Dupont, A.2    Hegy, G.3    Lanot, R.4    Holder, F.5    Hetru, C.6    Hoffmann, J.A.7    Bulet, P.8
  • 27
    • 0024289191 scopus 로고
    • Molecular cloning of the sapecin gene during the development of Sarcophaga peregrina
    • 27. Matsuyama, K. & Natori, S. (1988) Molecular cloning of the sapecin gene during the development of Sarcophaga peregrina. J. Biol. Chem. 263, 17117-17121.
    • (1988) J. Biol. Chem. , vol.263 , pp. 17117-17121
    • Matsuyama, K.1    Natori, S.2
  • 28
    • 0028208333 scopus 로고
    • Characterization and transcriptional profiles of a Drosophila gene encoding an insect defensin: A study in insect immunity
    • 28. Dimarcq, J.L., Hoffmann, D., Meister, M., Bulet, P., Lanot, R., Reichhart, J.M. & Hoffmann, J.A. (1994) Characterization and transcriptional profiles of a Drosophila gene encoding an insect defensin: a study in insect immunity. Eur. J. Biochem. 221, 201-209.
    • (1994) Eur. J. Biochem. , vol.221 , pp. 201-209
    • Dimarcq, J.L.1    Hoffmann, D.2    Meister, M.3    Bulet, P.4    Lanot, R.5    Reichhart, J.M.6    Hoffmann, J.A.7
  • 29
    • 0026738576 scopus 로고
    • Insect defensin: Inducible antibacterial peptides
    • 29. Hoffmann, J.A. & Hetru, C. (1992) Insect defensin: inducible antibacterial peptides. Immunol. Today 13, 411-415.
    • (1992) Immunol. Today , vol.13 , pp. 411-415
    • Hoffmann, J.A.1    Hetru, C.2
  • 31
    • 0032145637 scopus 로고    scopus 로고
    • Isolation, cDNA cloning and gene expression of an antibacterial protein from larvae of the coconut rhinoceros beetle, Oryctes rhinoceros
    • 31. Yang, J., Yamamoto, M., Ishibashi, J., Tainiai, K. & Yamakawa, M. (1998) Isolation, cDNA cloning and gene expression of an antibacterial protein from larvae of the coconut rhinoceros beetle, Oryctes rhinoceros. Eur. J. Biochem. 255, 734-738.
    • (1998) Eur. J. Biochem. , vol.255 , pp. 734-738
    • Yang, J.1    Yamamoto, M.2    Ishibashi, J.3    Tainiai, K.4    Yamakawa, M.5
  • 32
    • 0025809272 scopus 로고
    • Organization and expression of the immunoresponsive lysozyme gene in the giant silk moth, Hyalophora cecropia
    • 32. Sun, S.-C, Isling, B. & Fage, I. (1991) Organization and expression of the immunoresponsive lysozyme gene in the giant silk moth, Hyalophora cecropia. J. Biol. Chem. 266, 6644-6649.
    • (1991) J. Biol. Chem. , vol.266 , pp. 6644-6649
    • Sun, S.-C.1    Isling, B.2    Fage, I.3
  • 33
    • 0029587068 scopus 로고
    • Parallel induction of cecropin and lysozyme in larvae of the silkworm, Bombyx mori
    • 33. Morishima, I., Horiba, T., Iketani, M., Nishioka, E. & Yamano, Y. (1995) Parallel induction of cecropin and lysozyme in larvae of the silkworm, Bombyx mori. Dev. Comp. Immunol. 19, 357-363.
    • (1995) Dev. Comp. Immunol. , vol.19 , pp. 357-363
    • Morishima, I.1    Horiba, T.2    Iketani, M.3    Nishioka, E.4    Yamano, Y.5
  • 34
    • 0030583546 scopus 로고    scopus 로고
    • Requirement for antibacterial and hemolytic activities in the bovine neutrophil derived 13-residue peptide indolicidin
    • 34. Subbalakshmi, C., Krishnakumari, V., Nagaraj, R. & Sitaram, N. (1996) Requirement for antibacterial and hemolytic activities in the bovine neutrophil derived 13-residue peptide indolicidin. FEBS Lett. 395, 48-52.
    • (1996) FEBS Lett. , vol.395 , pp. 48-52
    • Subbalakshmi, C.1    Krishnakumari, V.2    Nagaraj, R.3    Sitaram, N.4
  • 35
    • 0014899296 scopus 로고
    • Precise quantitative determination of human blood lipids by thin-layer and triethylaminoethylcellulose column chromatography. I. Erythrocyte lipids
    • 35. Turner, J.D. & Rouser, G. (1970) Precise quantitative determination of human blood lipids by thin-layer and triethylaminoethylcellulose column chromatography. I. Erythrocyte lipids. Anal. Biochem. 38, 423-436.
    • (1970) Anal. Biochem. , vol.38 , pp. 423-436
    • Turner, J.D.1    Rouser, G.2
  • 36
    • 0025916877 scopus 로고
    • Arg-X-Lys/Arg-Arg motif as a signal for precursor cleavage catalyzed by furin within the constitutive secretory pathway
    • 36. Hosaka, M., Nagahama, M., Kim, W.S., Watanabe, T., Hatsuzawa, K., Ikemizu, J., Murakami, K. & Nakayama, K. (1992) Arg-X-Lys/ Arg-Arg motif as a signal for precursor cleavage catalyzed by furin within the constitutive secretory pathway. J. Biol. Chem. 266, 12127-12130.
    • (1992) J. Biol. Chem. , vol.266 , pp. 12127-12130
    • Hosaka, M.1    Nagahama, M.2    Kim, W.S.3    Watanabe, T.4    Hatsuzawa, K.5    Ikemizu, J.6    Murakami, K.7    Nakayama, K.8


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