메뉴 건너뛰기




Volumn 266, Issue 2, 1999, Pages 335-346

Recombinant expression and range of activity of penaeidins, antimicrobial peptides from penaeid shrimp

Author keywords

Activity spectrum; Antimicrobial peptides; Crustacean immunity; Heterologous expression; Saccharomyces cerevisiae

Indexed keywords

CYSTEINE; PROLINE; RECOMBINANT PROTEIN; ANTIINFECTIVE AGENT; COMPLEMENTARY DNA; PENAEIDIN 2; PENAEIDIN 3; PEPTIDE; PROTEIN;

EID: 0033485394     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1999.00855.x     Document Type: Article
Times cited : (171)

References (43)
  • 2
    • 0033067196 scopus 로고    scopus 로고
    • Antimicrobial peptides in mammalian and insect host defence
    • 2. Lehrer, R.I. & Ganz, T. (1999) Antimicrobial peptides in mammalian and insect host defence. Curr. Opin. Immunol. 11, 23-27.
    • (1999) Curr. Opin. Immunol. , vol.11 , pp. 23-27
    • Lehrer, R.I.1    Ganz, T.2
  • 3
    • 0029762649 scopus 로고    scopus 로고
    • Purification and characterization of a proline-rich antibacterial peptide, with sequence similarity to bactenecin-7, from the haemocytes of the shore crab, Carcinus maenas
    • 3. Schnapp, D., Kemp, G.D. & Smith, V.J. (1996) Purification and characterization of a proline-rich antibacterial peptide, with sequence similarity to bactenecin-7, from the haemocytes of the shore crab, Carcinus maenas. Eur. J. Biochem. 240, 532-539.
    • (1996) Eur. J. Biochem. , vol.240 , pp. 532-539
    • Schnapp, D.1    Kemp, G.D.2    Smith, V.J.3
  • 4
    • 0030692830 scopus 로고    scopus 로고
    • Penaeidins, a new family of antimicrobial peptides isolated from the shrimp Penaeus vannamei (Decapoda)
    • 4. Destoumieux, D., Bulet, P., Loew, D., van Dorsselaer, A., Rodriguez, J. & Bachère, E. (1997) Penaeidins, a new family of antimicrobial peptides isolated from the shrimp Penaeus vannamei (Decapoda). J. Biol. Chem. 272, 28398-28406.
    • (1997) J. Biol. Chem. , vol.272 , pp. 28398-28406
    • Destoumieux, D.1    Bulet, P.2    Loew, D.3    Van Dorsselaer, A.4    Rodriguez, J.5    Bachère, E.6
  • 5
    • 0003064891 scopus 로고    scopus 로고
    • Antimicrobial peptides from insects
    • (Brey, P.T. & Hultmark, D., eds) Chapman & Hall, London, UK.
    • 5. Hétru, C., Hoffmann, D. & Bulet, P. (1998) Antimicrobial peptides from insects. In Molecular Mechanisms of Immune Responses in Insects (Brey, P.T. & Hultmark, D., eds), pp. 40-66. Chapman & Hall, London, UK.
    • (1998) Molecular Mechanisms of Immune Responses in Insects , pp. 40-66
    • Hétru, C.1    Hoffmann, D.2    Bulet, P.3
  • 7
    • 0028304808 scopus 로고
    • Novel inducible antibacterial peptides from a hemipteran insect, the sap-sucking bug Pyrrhocoris apterus
    • 7. Cociancich, S., Dupont, A., Hegy, G., Lanot, R., Holder, F., Hétru, C., Hoffmann, J.A. & Bulet, P. (1994) Novel inducible antibacterial peptides from a hemipteran insect, the sap-sucking bug Pyrrhocoris apterus. 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    Hétru, C.6    Hoffmann, J.A.7    Bulet, P.8
  • 8
    • 0029051008 scopus 로고
    • A novel antibacterial peptide family isolated from the silkworm
    • 8. Hara, S. & Yamakawa, M. (1995) A novel antibacterial peptide family isolated from the silkworm. Bombyx mori. Biochem. J. 310, 651-656.
    • (1995) Bombyx Mori. Biochem. J. , vol.310 , pp. 651-656
    • Hara, S.1    Yamakawa, M.2
  • 9
    • 0032513209 scopus 로고    scopus 로고
    • Isolation from an Ant Myrmecia gulosa of two inducible O-glycosylated proline-rich antibacterial peptides
    • 9. Mackintosh, J.A., Veal, D.A., Beattie, A.J. & Gooley, A.A. (1998) Isolation from an Ant Myrmecia gulosa of two inducible O-glycosylated proline-rich antibacterial peptides. J. Biol. Chem. 273, 6139-6143.
    • (1998) J. Biol. Chem. , vol.273 , pp. 6139-6143
    • Mackintosh, J.A.1    Veal, D.A.2    Beattie, A.J.3    Gooley, A.A.4
  • 12
    • 0030583613 scopus 로고    scopus 로고
    • Determination of the disulfide array of the first inducible antifungal peptide from insects: Drosomycin from Drosophila melanogaster
    • 12. Michaut, L., Fehlbaum, P., Moniatte, M., Van Dorsselaer, A., Reichhart, J.-M. & Bulet, P. (1996) Determination of the disulfide array of the first inducible antifungal peptide from insects: drosomycin from Drosophila melanogaster. FEBS Lett. 395, 6-10.
    • (1996) FEBS Lett. , vol.395 , pp. 6-10
    • Michaut, L.1    Fehlbaum, P.2    Moniatte, M.3    Van Dorsselaer, A.4    Reichhart, J.-M.5    Bulet, P.6
  • 13
    • 0026602004 scopus 로고
    • A new signal peptide useful for secretion of heterologous proteins from yeast and its application for synthesis of hirudin
    • 13. Achstetter, T., Nguyen-Juilleret, M., Findeli, A., Merkamm, M. & Lemoine, Y. (1992) A new signal peptide useful for secretion of heterologous proteins from yeast and its application for synthesis of hirudin. Gene 110, 25-31.
    • (1992) Gene , vol.110 , pp. 25-31
    • Achstetter, T.1    Nguyen-Juilleret, M.2    Findeli, A.3    Merkamm, M.4    Lemoine, Y.5
  • 14
    • 0030897065 scopus 로고    scopus 로고
    • Heterologous expression of human cholecystokinin in Saccharomyces cerevisiae. Evidence for a lysine-specific endopeptidase in the yeast secretory pathway
    • 14. Rourke, I.J., Johnsen, A.H., Din, N., Petersen, J.G.L. & Rehfeld, J.F. (1997) Heterologous expression of human cholecystokinin in Saccharomyces cerevisiae. Evidence for a lysine-specific endopeptidase in the yeast secretory pathway. J. Biol. Chem. 272, 9720-9727.
    • (1997) J. Biol. Chem. , vol.272 , pp. 9720-9727
    • Rourke, I.J.1    Johnsen, A.H.2    Din, N.3    Petersen, J.G.L.4    Rehfeld, J.F.5
  • 15
    • 0032521638 scopus 로고    scopus 로고
    • Expression, processing and secretion of a proteolytically-sensitive insect diuretic hormone by Saccharomyces cerevisiae requires the use of a yeast strain lacking genes encoding the Yap3 and Mkc7 endoproteases found in the secretory pathway
    • 15. Copley, K.S., Alm, S.M., Schooley, D.A. & Courchesne, W.E. (1998) Expression, processing and secretion of a proteolytically-sensitive insect diuretic hormone by Saccharomyces cerevisiae requires the use of a yeast strain lacking genes encoding the Yap3 and Mkc7 endoproteases found in the secretory pathway. Biochem. J. 330, 1333-1340.
    • (1998) Biochem. J. , vol.330 , pp. 1333-1340
    • Copley, K.S.1    Alm, S.M.2    Schooley, D.A.3    Courchesne, W.E.4
  • 17
    • 0026562884 scopus 로고
    • Improved method for high efficiency transformation of intact yeast cells
    • 17. Gietz, D., St. Jean, A., Woods, J.R. & Schiestl, R.H. (1992) Improved method for high efficiency transformation of intact yeast cells. Nucleic Acids Res. 20, 1425.
    • (1992) Nucleic Acids Res. , vol.20 , pp. 1425
    • Gietz, D.1    St. Jean, A.2    Woods, J.R.3    Schiestl, R.H.4
  • 18
    • 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
    • 18. Fehlbaum, P., Bulet, P., Chernysh, S., Briand, J.P., Roussel, I.P., Letellier, L., Hétru, 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, I.P.5    Letellier, L.6    Hétru, C.7    Hoffmann, J.A.8
  • 19
    • 0028587829 scopus 로고
    • Insect Immunity. Septic injury of Drosophila induces the synthesis of a potent antifungal peptide with sequence homology to plant antifungal peptides
    • 19. Fehlbaum, P., Bulet, P., Michaut, L., Lagueux, M., Broekaert, W.F., Hétru, C. & Hoffman, J.A. (1994) Insect Immunity. Septic injury of Drosophila induces the synthesis of a potent antifungal peptide with sequence homology to plant antifungal peptides. J. Biol. Chem. 269, 33159-33163.
    • (1994) J. Biol. Chem. , vol.269 , pp. 33159-33163
    • Fehlbaum, P.1    Bulet, P.2    Michaut, L.3    Lagueux, M.4    Broekaert, W.F.5    Hétru, C.6    Hoffman, J.A.7
  • 20
    • 0027528472 scopus 로고
    • Functional and chemical characterization of hymenoptaecin, an antibacterial polypeptide that is infection-inducible in the honeybee (Apis mellifera)
    • 20. Casteels, P., Ampe, C., Jacobs, F. & Tempst, P. (1993) Functional and chemical characterization of hymenoptaecin, an antibacterial polypeptide that is infection-inducible in the honeybee (Apis mellifera). J. Biol. Chem. 268, 7044-7054.
    • (1993) J. Biol. Chem. , vol.268 , pp. 7044-7054
    • Casteels, P.1    Ampe, C.2    Jacobs, F.3    Tempst, P.4
  • 22
    • 0343554635 scopus 로고    scopus 로고
    • Recombinant expression of the antimicrobial peptide polyphemusin and its activity against the protozoan oyster pathogen Perkinsus marinus
    • 22. Pierce, J.C., Maloy, W.L., Salvador, L. & Dungan, C.F. (1997) Recombinant expression of the antimicrobial peptide polyphemusin and its activity against the protozoan oyster pathogen Perkinsus marinus. Mol. Mar. Biol. Technical 6, 248-259.
    • (1997) Mol. Mar. Biol. Technical , vol.6 , pp. 248-259
    • Pierce, J.C.1    Maloy, W.L.2    Salvador, L.3    Dungan, C.F.4
  • 23
    • 0023944202 scopus 로고
    • Effects on electrophoretic mobility and antibacterial spectrum of removal of two residues from synthetic sarcotoxin Ia and addition of the same residues to cecropin B
    • 23. Li, Z.Q., Merrifield, R.B., Boman, I.A. & Boman, H.G. (1988) Effects on electrophoretic mobility and antibacterial spectrum of removal of two residues from synthetic sarcotoxin Ia and addition of the same residues to cecropin B. FEBS Lett. 231, 299-302.
    • (1988) FEBS Lett. , vol.231 , pp. 299-302
    • Li, Z.Q.1    Merrifield, R.B.2    Boman, I.A.3    Boman, H.G.4
  • 24
    • 0028095144 scopus 로고
    • Isolation and alpha-amidation of the non-amidated form of cecropin D from the larvae of Bombyx mori
    • 24. Kara, S., Taniai, K., Kato, Y. & Yamakawa, M. (1994) Isolation and alpha-amidation of the non-amidated form of cecropin D from the larvae of Bombyx mori. Comp. Biochem. Physiol. 108B, 303-308.
    • (1994) Comp. Biochem. Physiol. , vol.108 B , pp. 303-308
    • Kara, S.1    Taniai, K.2    Kato, Y.3    Yamakawa, M.4
  • 25
    • 0024996989 scopus 로고
    • Characterization of O-glycosylation sites in recombinant B-chain of platelet-derived growth factor expressed in yeast using liquid secondary ion mass spectrometry, tandem mass spectrometry and Edman sequence analysis
    • 25. Settineri, C.A., Medzihradszky, K.F., Masiarz, F.R., Burlingame, A.L., Chu, C. & George-Nascimiento, C. (1990) Characterization of O-glycosylation sites in recombinant B-chain of platelet-derived growth factor expressed in yeast using liquid secondary ion mass spectrometry, tandem mass spectrometry and Edman sequence analysis. Biomed. Environ. Mass Spectrom. 19, 665-676.
    • (1990) Biomed. Environ. Mass Spectrom. , vol.19 , pp. 665-676
    • Settineri, C.A.1    Medzihradszky, K.F.2    Masiarz, F.R.3    Burlingame, A.L.4    Chu, C.5    George-Nascimiento, C.6
  • 26
    • 0032056345 scopus 로고    scopus 로고
    • Identification of Man alpha-1-3 Man alpha-1-2 Man and Man-linked phosphate on O-mannosylated recombinant leech-derived tryptase inhibitor produced by Saccharomyces cerevisiae and determination of the solution conformation of the mannosylated polypeptide
    • 26. Bergwerff, A.A., Stark, W., Fendrich, G., Knecht, R., Blommers, M.J., Maerki, W., Kragten, E.A. & van Oostrum, J. (1998) Identification of Man alpha-1-3 Man alpha-1-2 Man and Man-linked phosphate on O-mannosylated recombinant leech-derived tryptase inhibitor produced by Saccharomyces cerevisiae and determination of the solution conformation of the mannosylated polypeptide. Eur. J. Biochem. 253, 560-575.
    • (1998) Eur. J. Biochem. , vol.253 , pp. 560-575
    • Bergwerff, A.A.1    Stark, W.2    Fendrich, G.3    Knecht, R.4    Blommers, M.J.5    Maerki, W.6    Kragten, E.A.7    Van Oostrum, J.8
  • 27
    • 0029958897 scopus 로고    scopus 로고
    • Glycosylation of rat NGF receptor ectodomain in the yeast Saccharomyces cerevisiae
    • 27. Holkeri, H., Simonen, M., Pummi, T., Vihinen, H. & Makarow, M. (1996) Glycosylation of rat NGF receptor ectodomain in the yeast Saccharomyces cerevisiae. FEBS Lett. 383, 255-258.
    • (1996) FEBS Lett. , vol.383 , pp. 255-258
    • Holkeri, H.1    Simonen, M.2    Pummi, T.3    Vihinen, H.4    Makarow, M.5
  • 28
    • 0029929079 scopus 로고    scopus 로고
    • Enlarged scale chemical synthesis and range of activity of drosocin, an O-glycosylated antibacterial peptide of Drosophila
    • 28. Bulet, P., Urge, L., Ohresser, S., Hétru, C. & Otvos, L. (1996) Enlarged scale chemical synthesis and range of activity of drosocin, an O-glycosylated antibacterial peptide of Drosophila. Eur. J. Biochem. 238, 64-69.
    • (1996) Eur. J. Biochem. , vol.238 , pp. 64-69
    • Bulet, P.1    Urge, L.2    Ohresser, S.3    Hétru, C.4    Otvos, L.5
  • 29
    • 0029055842 scopus 로고
    • Insect immunity. The inducible antibacterial peptide diptericin carries two O-glycans necessary for biological activity
    • 29. Bulet, P., Hégy, G., Lambert, J., Van Dorsselaer, A., Hoffmann, J.A. & Hétru, C. (1995) Insect immunity. The inducible antibacterial peptide diptericin carries two O-glycans necessary for biological activity. Biochemistry 34, 7394-7400.
    • (1995) Biochemistry , vol.34 , pp. 7394-7400
    • Bulet, P.1    Hégy, G.2    Lambert, J.3    Van Dorsselaer, A.4    Hoffmann, J.A.5    Hétru, C.6
  • 30
    • 0033547753 scopus 로고    scopus 로고
    • Conformational studies by NMR of the antimicrobial peptide, drosocin and its non-glycosylated derivative: Effects of glycosylation on solution conformation
    • 30. McManus, A.M., Otvos, L. Jr, Hoffmann, R. & Craik, D.J. (1999) Conformational studies by NMR of the antimicrobial peptide, drosocin and its non-glycosylated derivative: effects of glycosylation on solution conformation. Biochemistry 38, 705-714.
    • (1999) Biochemistry , vol.38 , pp. 705-714
    • McManus, A.M.1    Otvos L., Jr.2    Hoffmann, R.3    Craik, D.J.4
  • 31
    • 0027988532 scopus 로고
    • The vertebrate peptide antibiotics dermaseptins have overlapping structural features but target specific microorganisms
    • 31. Mor, A., Hani, K. & Nicolas, P. (1994) The vertebrate peptide antibiotics dermaseptins have overlapping structural features but target specific microorganisms. J. Biol. Chem. 269, 31635-31641.
    • (1994) J. Biol. Chem. , vol.269 , pp. 31635-31641
    • Mor, A.1    Hani, K.2    Nicolas, P.3
  • 33
    • 0031934614 scopus 로고    scopus 로고
    • New types of clotting factors and defense molecules found in horseshoe crab hemolymph: Their structures and functions
    • 33. Iwanaga, S., Kawabata, S. & Muta, T. (1998) New types of clotting factors and defense molecules found in horseshoe crab hemolymph: their structures and functions. J. Biochem. (Tokyo) 123, 1-15.
    • (1998) J. Biochem. (Tokyo) , vol.123 , pp. 1-15
    • Iwanaga, S.1    Kawabata, S.2    Muta, T.3
  • 35
    • 0000888009 scopus 로고
    • Characterization and ecological implication of luminous Vibrio harveyi isolated from tiger shrimp (Penaeus monodon)
    • 35. Song, Y.L. & Lee, S.P. (1993) Characterization and ecological implication of luminous Vibrio harveyi isolated from tiger shrimp (Penaeus monodon). Bull Inst. Zool. 32, 217-220.
    • (1993) Bull Inst. Zool. , vol.32 , pp. 217-220
    • Song, Y.L.1    Lee, S.P.2
  • 36
    • 0028905203 scopus 로고
    • Interaction of the fragments characteristic of bactenecin 7 with phospholipid bilayers and their antimicrobial activity
    • 36. Tani, A., Lee, S., Oishi, O., Aoyagi, H. & Ohno, M. (1995) Interaction of the fragments characteristic of bactenecin 7 with phospholipid bilayers and their antimicrobial activity. J. Biochem. (Tokyo) 117, 560-565.
    • (1995) J. Biochem. (Tokyo) , vol.117 , pp. 560-565
    • Tani, A.1    Lee, S.2    Oishi, O.3    Aoyagi, H.4    Ohno, M.5
  • 37
    • 0033515629 scopus 로고    scopus 로고
    • Insect immunity. Isolation from the Lepidopteran Heliothis virescens of a novel insect defensin with potent antifungal activity
    • 37. Lamberty, M. (1999) Insect immunity. Isolation from the Lepidopteran Heliothis virescens of a novel insect defensin with potent antifungal activity. J. Biol. Chem. 274, 9320-9326.
    • (1999) J. Biol. Chem. , vol.274 , pp. 9320-9326
    • Lamberty, M.1
  • 38
    • 0032411402 scopus 로고    scopus 로고
    • Cysteine-rich antimicrobial peptides in invertebrates
    • 38. Dimarcq, J.-L., Bulet, P., Hétru, C. & Hoffmann, J.A. (1998) Cysteine-rich antimicrobial peptides in invertebrates. Biopolymers 47, 465-477.
    • (1998) Biopolymers , vol.47 , pp. 465-477
    • Dimarcq, J.-L.1    Bulet, P.2    Hétru, C.3    Hoffmann, J.A.4
  • 39
    • 84972222998 scopus 로고
    • Antibacterial activity in the haemocytes of the shore crab, Carcinus maenas
    • 39. Chisholm, J.R.S. & Smith, V.J. (1992) Antibacterial activity in the haemocytes of the shore crab, Carcinus maenas, J. Mar Biol. Assoc. UK. 72, 529-542.
    • (1992) J. Mar Biol. Assoc. UK. , vol.72 , pp. 529-542
    • Chisholm, J.R.S.1    Smith, V.J.2
  • 40
    • 0001147730 scopus 로고
    • Interaction of the pathogen Gaffkya homari with natural defense mechanisms of Homarus americanus
    • 40. Cornick, J.W. & Stewart, J.E. (1968) Interaction of the pathogen Gaffkya homari with natural defense mechanisms of Homarus americanus. J. Fish. Res. Board Can. 25, 695-709.
    • (1968) J. Fish. Res. Board Can. , vol.25 , pp. 695-709
    • Cornick, J.W.1    Stewart, J.E.2
  • 41
    • 0027249384 scopus 로고
    • Insect defensin, an inducible antibacterial peptide, forms voltage-dependent channels in Micrococcus luteus
    • 41. Cociancich, S., Ghazi, A., Hétru, C., Hoffmann, J.A. & Letellier, L. (1993) Insect defensin, an inducible antibacterial peptide, forms voltage-dependent channels in Micrococcus luteus. J. Biol. Chem. 268, 19239-19245.
    • (1993) J. Biol. Chem. , vol.268 , pp. 19239-19245
    • Cociancich, S.1    Ghazi, A.2    Hétru, C.3    Hoffmann, J.A.4    Letellier, L.5
  • 42
    • 0024454751 scopus 로고
    • Apidaecins: Antibacterial peptides from honeybees
    • 42. Casteels, P., Ampe, C., Jacobs, F., Vaeck, M. & Tempst, P. (1989) Apidaecins: antibacterial peptides from honeybees. EMBO J. 8, 2387-2391.
    • (1989) EMBO J. , vol.8 , pp. 2387-2391
    • Casteels, P.1    Ampe, C.2    Jacobs, F.3    Vaeck, M.4    Tempst, P.5
  • 43
    • 84989890786 scopus 로고
    • Fusarium moniliforme (Sheldon) isolated from gills of Kuruma prawn Penaeus japonicus (Bate) with black gill disease
    • 43. Rhoobunjongde, W., Hatai, K., Wada, S. & Kubota, S.S. (1991) Fusarium moniliforme (Sheldon) isolated from gills of Kuruma prawn Penaeus japonicus (Bate) with black gill disease. Nippon Suisan Gakkaishi 57, 629-635.
    • (1991) Nippon Suisan Gakkaishi , vol.57 , pp. 629-635
    • Rhoobunjongde, W.1    Hatai, K.2    Wada, S.3    Kubota, S.S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.