메뉴 건너뛰기




Volumn 69, Issue 1, 2005, Pages 92-98

Antimicrobial activity of conditioned medium fractions from Spodoptera frugiperda Sf9 and Trichoplusia ni Hi5 insect cells

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIA; BACTERIOLOGY; CELLS; DENSITY (OPTICAL); ESCHERICHIA COLI; GELS;

EID: 28344454084     PISSN: 01757598     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00253-005-1958-6     Document Type: Article
Times cited : (8)

References (24)
  • 1
    • 0033775891 scopus 로고    scopus 로고
    • Physiological functions of thioredoxin and thioredoxin reductase
    • Arnér ESJ, Holmgren A (2000) Physiological functions of thioredoxin and thioredoxin reductase. Eur J Biochem 267:6102-6109
    • (2000) Eur J Biochem , vol.267 , pp. 6102-6109
    • Arnér, E.S.J.1    Holmgren, A.2
  • 2
    • 9144248470 scopus 로고    scopus 로고
    • Detection and partial characterisation of two antibacterial factors from the excretions/secretions of the medicinal maggot Lucilia sericata and their activity against methicillin-resistant Staphylococcus aureus
    • Bexfield A, Nigam Y, Thomas S, Ratcliffe NA (2004) Detection and partial characterisation of two antibacterial factors from the excretions/secretions of the medicinal maggot Lucilia sericata and their activity against methicillin-resistant Staphylococcus aureus. Microbes Infect 6:1297-1304
    • (2004) Microbes Infect , vol.6 , pp. 1297-1304
    • Bexfield, A.1    Nigam, Y.2    Thomas, S.3    Ratcliffe, N.A.4
  • 3
    • 0034057767 scopus 로고    scopus 로고
    • Antibacterial properties and partial cDNA sequences of secropin-like antibacterial peptides from the common cutworm, Spodoptera litura
    • Choi CS, Lee IH, Kim E, Kim HR (2000) Antibacterial properties and partial cDNA sequences of secropin-like antibacterial peptides from the common cutworm, Spodoptera litura. Comp Biochem Physiol C Toxicol Pharmacol 125:287-297
    • (2000) Comp Biochem Physiol C Toxicol Pharmacol , vol.125 , pp. 287-297
    • Choi, C.S.1    Lee, I.H.2    Kim, E.3    Kim, H.R.4
  • 4
    • 0031913074 scopus 로고    scopus 로고
    • Cystine/cysteine metabolism in cultured Sf9 cells: Influence of cell physiology on biosynthesis, amino acid uptake and growth
    • Doverskog M, Han L, Häggström L (1998) Cystine/cysteine metabolism in cultured Sf9 cells: influence of cell physiology on biosynthesis, amino acid uptake and growth. Cytotechnology 26:91-102
    • (1998) Cytotechnology , vol.26 , pp. 91-102
    • Doverskog, M.1    Han, L.2    Häggström, L.3
  • 5
    • 0034283216 scopus 로고    scopus 로고
    • The roles of cationic antimicrobial peptides in innate host defences
    • Hancock REW, Diamond G (2000) The roles of cationic antimicrobial peptides in innate host defences. Trends Microbiol 8:402-410
    • (2000) Trends Microbiol , vol.8 , pp. 402-410
    • Hancock, R.E.W.1    Diamond, G.2
  • 8
  • 9
    • 0030087789 scopus 로고    scopus 로고
    • PCR differential display of immune gene expression in Trichoplusia ni
    • Kang D, Liu G, Gunne H, Steiner H (1996) PCR differential display of immune gene expression in Trichoplusia ni. Insect Biochem Mol Biol 26:177-184
    • (1996) Insect Biochem Mol Biol , vol.26 , pp. 177-184
    • Kang, D.1    Liu, G.2    Gunne, H.3    Steiner, H.4
  • 11
    • 0034665099 scopus 로고    scopus 로고
    • Pepsin-mediated processing of the cytoplasmic histone H2A to strong antimicrobial peptide buforin I
    • Kim HS, Yoon H, Minn Il, Park CB, Lee WT, Zasloff M, Kim SC (2000) Pepsin-mediated processing of the cytoplasmic histone H2A to strong antimicrobial peptide buforin I. J Immunol 165:3268-3274
    • (2000) J Immunol , vol.165 , pp. 3268-3274
    • Kim, H.S.1    Yoon, H.2    Minn, Il.3    Park, C.B.4    Lee, W.T.5    Zasloff, M.6    Kim, S.C.7
  • 12
    • 0035853022 scopus 로고    scopus 로고
    • The antimibacterial pyrrhocoricin inhibits the ATPase action of DnaK and prevents chaperon-assisted protein folding
    • Kragol G, Lovas S, Varadi G, Condie BA, Hoffman R, Otvos L (2001) The antimibacterial pyrrhocoricin inhibits the ATPase action of DnaK and prevents chaperon-assisted protein folding. Biochemistry 40:3016-3026
    • (2001) Biochemistry , vol.40 , pp. 3016-3026
    • Kragol, G.1    Lovas, S.2    Varadi, G.3    Condie, B.A.4    Hoffman, R.5    Otvos, L.6
  • 13
    • 0036015622 scopus 로고    scopus 로고
    • Trichoplusia ni gloverin, an inducable immune gene encoding an antibacterial insect protein
    • Lundström A, Liu G, Kang D, Berzins K, Steiner H (2002) Trichoplusia ni gloverin, an inducable immune gene encoding an antibacterial insect protein. Insect Biochem Mol Biol 32:795-801
    • (2002) Insect Biochem Mol Biol , vol.32 , pp. 795-801
    • Lundström, A.1    Liu, G.2    Kang, D.3    Berzins, K.4    Steiner, H.5
  • 14
    • 3042743487 scopus 로고    scopus 로고
    • Effects of the antimicrobial peptide temporin L on cell morphology, membrane permeability and viability of Escherichia coli
    • Mangoni ML, Papo N, Barra D, Simmaco M, Bozzi A, Di Giulio A, Rinaldi AC (2004) Effects of the antimicrobial peptide temporin L on cell morphology, membrane permeability and viability of Escherichia coli. Biochem J 380:859-865
    • (2004) Biochem J , vol.380 , pp. 859-865
    • Mangoni, M.L.1    Papo, N.2    Barra, D.3    Simmaco, M.4    Bozzi, A.5    Di Giulio, A.6    Rinaldi, A.C.7
  • 15
    • 3042781052 scopus 로고    scopus 로고
    • Antimicrobial peptides: A natural alternative to chemical antibiotics and a potential for applied biotechnology
    • Marshall SH, Arenas G (2003) Antimicrobial peptides: a natural alternative to chemical antibiotics and a potential for applied biotechnology. Electron J Biotechnol 6:2
    • (2003) Electron J Biotechnol , vol.6 , pp. 2
    • Marshall, S.H.1    Arenas, G.2
  • 16
    • 3543110792 scopus 로고    scopus 로고
    • Recombinant expression and enzymatic characterization of PttCel9A, a KOR homologue from Populus tremula x tremuloides
    • Master E, Rudsander UJ, Zhou W, Henriksson H, Divne C, Denman S, Wilson DB, Teeri TT (2004) Recombinant expression and enzymatic characterization of PttCel9A, a KOR homologue from Populus tremula x tremuloides. Biochemistry 43:10080-10089
    • (2004) Biochemistry , vol.43 , pp. 10080-10089
    • Master, E.1    Rudsander, U.J.2    Zhou, W.3    Henriksson, H.4    Divne, C.5    Denman, S.6    Wilson, D.B.7    Teeri, T.T.8
  • 17
    • 0023664635 scopus 로고
    • Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes
    • Matsudaira P (1987) Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes. J Biol Chem 262:10035-10038
    • (1987) J Biol Chem , vol.262 , pp. 10035-10038
    • Matsudaira, P.1
  • 18
    • 3042554233 scopus 로고    scopus 로고
    • Structural and biological characterization of two novel peptides from the venom of the neotropical social wasp Agelaia pallipes pallipes
    • Mendes MA, de Souza BM, Marques MR, Palma MS (2004) Structural and biological characterization of two novel peptides from the venom of the neotropical social wasp Agelaia pallipes pallipes. Toxicon 44:67-74
    • (2004) Toxicon , vol.44 , pp. 67-74
    • Mendes, M.A.1    De Souza, B.M.2    Marques, M.R.3    Palma, M.S.4
  • 19
    • 2342514277 scopus 로고    scopus 로고
    • Effects of antimicrobial peptides derived from the beetle Allomyrina dichotoma defensin on mouse peritoneal macrophages stimulated with lipopolysaccharide
    • Motobu M, Amer S, Yamada M, Nakamura K, Saido-Sakanaka H, Asaoka A, Yamakawa M, Hirota Y (2003) Effects of antimicrobial peptides derived from the beetle Allomyrina dichotoma defensin on mouse peritoneal macrophages stimulated with lipopolysaccharide. J Vet Med Sci 66:319-322
    • (2003) J Vet Med Sci , vol.66 , pp. 319-322
    • Motobu, M.1    Amer, S.2    Yamada, M.3    Nakamura, K.4    Saido-Sakanaka, H.5    Asaoka, A.6    Yamakawa, M.7    Hirota, Y.8
  • 20
    • 0032489294 scopus 로고    scopus 로고
    • Mechanism of action of the antimicrobial peptide buforin II: Buforin II kills microorganisms by penetrating the cell membrane and inhibiting cellular functions
    • Park CB, Kim HS, Kim SC (1998) Mechanism of action of the antimicrobial peptide buforin II: buforin II kills microorganisms by penetrating the cell membrane and inhibiting cellular functions. Biochem Biophys Res 244:253-257
    • (1998) Biochem Biophys Res , vol.244 , pp. 253-257
    • Park, C.B.1    Kim, H.S.2    Kim, S.C.3
  • 22
    • 10744231506 scopus 로고    scopus 로고
    • Characterization and transcriptional profiles of three Spodoptera frugiperda genes encoding cysteine-rich peptides. A new class of defensin-like genes from lepidopteran insects?
    • Volkoff A, Rocher J, d'Alencon E, Bouton M, Landais I, Quesada-Moraga E, Vey A, Fournier P, Mita K, Devauchelle G (2003) Characterization and transcriptional profiles of three Spodoptera frugiperda genes encoding cysteine-rich peptides. A new class of defensin-like genes from lepidopteran insects? Gene 319:43-53
    • (2003) Gene , vol.319 , pp. 43-53
    • Volkoff, A.1    Rocher, J.2    D'Alencon, E.3    Bouton, M.4    Landais, I.5    Quesada-Moraga, E.6    Vey, A.7    Fournier, P.8    Mita, K.9    Devauchelle, G.10
  • 23
    • 0036164391 scopus 로고    scopus 로고
    • Antibacterial peptides in stimulated human granulocytes. Characterization of ubiquinated histone H1A
    • Wang Y, Griffiths WJ, Jörnvall H, Agerberth B, Johansson J (2002) Antibacterial peptides in stimulated human granulocytes. Characterization of ubiquinated histone H1A. Eur J Biochem 269:512-518
    • (2002) Eur J Biochem , vol.269 , pp. 512-518
    • Wang, Y.1    Griffiths, W.J.2    Jörnvall, H.3    Agerberth, B.4    Johansson, J.5
  • 24
    • 0032567666 scopus 로고    scopus 로고
    • Expression of antimicrobial peptides has an antitumour effect in human cells
    • Winder D, Günzburg WH, Erfle V, Salmons B (1998) Expression of antimicrobial peptides has an antitumour effect in human cells. Biochem Bioph Res 242:608-612
    • (1998) Biochem Bioph Res , vol.242 , pp. 608-612
    • Winder, D.1    Günzburg, W.H.2    Erfle, V.3    Salmons, B.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.