메뉴 건너뛰기




Volumn 110, Issue 1, 2012, Pages 92-101

Inactivation of the budded virus of Autographa californica M nucleopolyhedrovirus by gloverin

Author keywords

AcMNPV; Antiviral; Autographa californica M nucleopolyhedrovirus; Baculovirus; Gloverin

Indexed keywords

ANTIVIRUS AGENT; GLOVERIN; PROTEIN;

EID: 84859759197     PISSN: 00222011     EISSN: 10960805     Source Type: Journal    
DOI: 10.1016/j.jip.2012.02.007     Document Type: Article
Times cited : (45)

References (47)
  • 1
    • 0037862882 scopus 로고    scopus 로고
    • Characterization of a recombinant immunomodulatory protein from the salivary glands of Dermacentor andersoni
    • Alarcon-Chaidez F.J., Müller-Doblies U.U., Wikel S. Characterization of a recombinant immunomodulatory protein from the salivary glands of Dermacentor andersoni. Parasite Immunol. 2003, 25(2):69-77.
    • (2003) Parasite Immunol. , vol.25 , Issue.2 , pp. 69-77
    • Alarcon-Chaidez, F.J.1    Müller-Doblies, U.U.2    Wikel, S.3
  • 2
    • 0343879238 scopus 로고
    • Assay of inorganic phosphate, total phosphate and phosphatases
    • In: Neufeld, E., Ginsburg, V. (Eds.)
    • Ames, B.N., 1966. Assay of inorganic phosphate, total phosphate and phosphatases. In: Neufeld, E., Ginsburg, V. (Eds.), Methods in enzymology. vol. VIII: Complex carbohydrates. pp. 115-118.
    • (1966) Methods in enzymology. Complex carbohydrates. , vol.8 , pp. 115-118
    • Ames, B.N.1
  • 3
    • 0030752238 scopus 로고    scopus 로고
    • Gloverin, an antibacterial protein from the immune hemolymph of Hyalophora pupae
    • Axen A., Carlsson A., Engström Å., Bennich H. Gloverin, an antibacterial protein from the immune hemolymph of Hyalophora pupae. Eur. J. Biochem. 1997, 247:614-619.
    • (1997) Eur. J. Biochem. , vol.247 , pp. 614-619
    • Axen, A.1    Carlsson, A.2    Engström, Å.3    Bennich, H.4
  • 4
    • 0026757345 scopus 로고
    • Baculovirus gp64 envelope glycoprotein is sufficient to mediate pH-dependent membrane fusion
    • Blissard G.W., Wenz J.R. Baculovirus gp64 envelope glycoprotein is sufficient to mediate pH-dependent membrane fusion. J. Virol. 1992, 66:6829-6835.
    • (1992) J. Virol. , vol.66 , pp. 6829-6835
    • Blissard, G.W.1    Wenz, J.R.2
  • 5
    • 70449658824 scopus 로고    scopus 로고
    • A peptidomics study reveals the impressive antimicrobial peptide arsenal of the wax moth Galleria mellonella
    • Brown S.E., Howard A., Kasprzak A.B., Gordon K.H., East P.D. A peptidomics study reveals the impressive antimicrobial peptide arsenal of the wax moth Galleria mellonella. Insect Biochem. Mol. Biol. 2009, 39(11):792-800.
    • (2009) Insect Biochem. Mol. Biol. , vol.39 , Issue.11 , pp. 792-800
    • Brown, S.E.1    Howard, A.2    Kasprzak, A.B.3    Gordon, K.H.4    East, P.D.5
  • 6
    • 0025886806 scopus 로고
    • Attacin, an antibacterial protein from Hyalophora cecropia, inhibits synthesis of outer membrane proteins in Escherichia coli by interfering with omp gene transcription
    • Carlsson A., Engström P., Palva E.T., Bennich H. Attacin, an antibacterial protein from Hyalophora cecropia, inhibits synthesis of outer membrane proteins in Escherichia coli by interfering with omp gene transcription. Infect Immun. 1991, 59:3040-3045.
    • (1991) Infect Immun. , vol.59 , pp. 3040-3045
    • Carlsson, A.1    Engström, P.2    Palva, E.T.3    Bennich, H.4
  • 8
    • 84855853236 scopus 로고    scopus 로고
    • Purification and characterization of tenecin 4, a new anti-Gram-negative bacterial peptide, from the beetle Tenebrio molitor
    • Chae J.H., Kurokawa K., So Y.I., Hwang H.O., Kim M.S., Park J.W., Jo Y.H., Lee Y.S., Lee B.L. Purification and characterization of tenecin 4, a new anti-Gram-negative bacterial peptide, from the beetle Tenebrio molitor. Dev. Comp. Immunol. 2011, 36(3):540-546.
    • (2011) Dev. Comp. Immunol. , vol.36 , Issue.3 , pp. 540-546
    • Chae, J.H.1    Kurokawa, K.2    So, Y.I.3    Hwang, H.O.4    Kim, M.S.5    Park, J.W.6    Jo, Y.H.7    Lee, Y.S.8    Lee, B.L.9
  • 10
    • 0024040498 scopus 로고
    • Channel-forming properties of cecropins and related model compounds incorporated into planar lipid membranes
    • Christensen B., Fink J., Merrifield R.B., Mauzerall D. Channel-forming properties of cecropins and related model compounds incorporated into planar lipid membranes. PNAS 1988, 85(14):5072-5076.
    • (1988) PNAS , vol.85 , Issue.14 , pp. 5072-5076
    • Christensen, B.1    Fink, J.2    Merrifield, R.B.3    Mauzerall, D.4
  • 11
    • 0022977989 scopus 로고
    • Direct inactivation of viruses by human granulocyte defensins
    • Daher K.A., Selsted M.E., Lehrer R.I. Direct inactivation of viruses by human granulocyte defensins. J. Virol. 1986, 60(3):1068-1074.
    • (1986) J. Virol. , vol.60 , Issue.3 , pp. 1068-1074
    • Daher, K.A.1    Selsted, M.E.2    Lehrer, R.I.3
  • 12
    • 80052602353 scopus 로고    scopus 로고
    • Deep sequencing-based transcriptome analysis of Plutella xylostella larvae parasitized by Diadegma semiclausum
    • Etebari K., Palfreyman R.W., Schlipalius D., Nielsen L.K., Glatz R.V., Asgari S. Deep sequencing-based transcriptome analysis of Plutella xylostella larvae parasitized by Diadegma semiclausum. BMC Genomics 2011, 12:446.
    • (2011) BMC Genomics , vol.12 , pp. 446
    • Etebari, K.1    Palfreyman, R.W.2    Schlipalius, D.3    Nielsen, L.K.4    Glatz, R.V.5    Asgari, S.6
  • 13
    • 39049143349 scopus 로고    scopus 로고
    • Immune system responses and fitness costs associated with consumption of bacteria in larvae of Trichoplusia ni
    • Freitak D., Wheat C.W., Heckel D.G., Vogel H. Immune system responses and fitness costs associated with consumption of bacteria in larvae of Trichoplusia ni. BMC Biology 2007, 5(1):56.
    • (2007) BMC Biology , vol.5 , Issue.1 , pp. 56
    • Freitak, D.1    Wheat, C.W.2    Heckel, D.G.3    Vogel, H.4
  • 14
    • 0141799911 scopus 로고    scopus 로고
    • Defensins: antimicrobial peptides of innate immunity
    • Ganz T. Defensins: antimicrobial peptides of innate immunity. Nat. Rev. Immunol. 2003, 3(9):710-720.
    • (2003) Nat. Rev. Immunol. , vol.3 , Issue.9 , pp. 710-720
    • Ganz, T.1
  • 15
    • 0037042209 scopus 로고    scopus 로고
    • Solution structure of moricin, an antibacterial peptide, isolated from the silkworm Bombyx mori
    • Hemmi H., Ishibashi J., Hara S., Yamakawa M. Solution structure of moricin, an antibacterial peptide, isolated from the silkworm Bombyx mori. FEBS Letters 2002, 518(1-3):33-38.
    • (2002) FEBS Letters , vol.518 , Issue.1-3 , pp. 33-38
    • Hemmi, H.1    Ishibashi, J.2    Hara, S.3    Yamakawa, M.4
  • 16
    • 77949538431 scopus 로고    scopus 로고
    • A genome-wide survey for host response of silkworm, bombyx mori during pathogen bacillus bombyseptieus infection
    • Huang L., Cheng T., Xu P., Cheng D., Fang T., Xia Q. A genome-wide survey for host response of silkworm, bombyx mori during pathogen bacillus bombyseptieus infection. PloS one 2009, 4(12):e8098.
    • (2009) PloS one , vol.4 , Issue.12
    • Huang, L.1    Cheng, T.2    Xu, P.3    Cheng, D.4    Fang, T.5    Xia, Q.6
  • 17
    • 0020686109 scopus 로고
    • Insect immunity. Attacins, a family of antibacterial proteins from Hyalophora cecropia
    • Hultmark D., Engström å., Andersson K., Steiner H., Bennich H., Boman H.G. Insect immunity. Attacins, a family of antibacterial proteins from Hyalophora cecropia. EMBO Journal 1983, 2(4):571-576.
    • (1983) EMBO Journal , vol.2 , Issue.4 , pp. 571-576
    • Hultmark, D.1    Engström, Å.2    Andersson, K.3    Steiner, H.4    Bennich, H.5    Boman, H.G.6
  • 19
    • 53549088587 scopus 로고    scopus 로고
    • The postfusion structure of baculovirus gp64 supports a unified view of viral fusion machines
    • Kadlec J., Loureiro S., Abrescia N.G.A., Stuart D.I., Jones I.M. The postfusion structure of baculovirus gp64 supports a unified view of viral fusion machines. Nat. Struct. Mol. Biol. 2008, 15(10):1024-1030.
    • (2008) Nat. Struct. Mol. Biol. , vol.15 , Issue.10 , pp. 1024-1030
    • Kadlec, J.1    Loureiro, S.2    Abrescia, N.G.A.3    Stuart, D.I.4    Jones, I.M.5
  • 21
    • 71749109184 scopus 로고    scopus 로고
    • Acquisition of chemiluminescent signals from immunoblots with a digital single-lens reflex camera
    • Khoury M., Parker I., Aswad D.W. Acquisition of chemiluminescent signals from immunoblots with a digital single-lens reflex camera. Analyt. Biochem. 2010, 397:129-131.
    • (2010) Analyt. Biochem. , vol.397 , pp. 129-131
    • Khoury, M.1    Parker, I.2    Aswad, D.W.3
  • 22
    • 27744608414 scopus 로고    scopus 로고
    • Immune challenge differentially affects transcript abundance of three antimicrobial peptides in hemocytes from the moth Pseudoplusia includens
    • Lavine M.D., Chen G., Strand M.R. Immune challenge differentially affects transcript abundance of three antimicrobial peptides in hemocytes from the moth Pseudoplusia includens. Insect Biochem. Mol. Biol. 2005, 35(12):1335-1346.
    • (2005) Insect Biochem. Mol. Biol. , vol.35 , Issue.12 , pp. 1335-1346
    • Lavine, M.D.1    Chen, G.2    Strand, M.R.3
  • 23
    • 0034708353 scopus 로고    scopus 로고
    • Trichoplusia ni Lebocin, an inducible immune gene with a downstream insertion element
    • Liu G., Kang D., Steiner H. Trichoplusia ni Lebocin, an inducible immune gene with a downstream insertion element. Biochem. Biophys. Res. Commun. 2000, 269(3):803-807.
    • (2000) Biochem. Biophys. Res. Commun. , vol.269 , Issue.3 , pp. 803-807
    • Liu, G.1    Kang, D.2    Steiner, H.3
  • 24
    • 0036015622 scopus 로고    scopus 로고
    • Trichoplusia ni gloverin, an inducible immune gene encoding an antibacterial insect protein
    • Lundström A., Liu G., Kang D., Berzins K., Steiner H. Trichoplusia ni gloverin, an inducible immune gene encoding an antibacterial insect protein. Insect Biochem. Mol. Biol. 2002, 32(7):795-801.
    • (2002) Insect Biochem. Mol. Biol. , vol.32 , Issue.7 , pp. 795-801
    • Lundström, A.1    Liu, G.2    Kang, D.3    Berzins, K.4    Steiner, H.5
  • 25
    • 0028818140 scopus 로고
    • Kinetics of pore formation by an antimicrobial peptide, magainin 2, in phospholipid bilayers
    • Matsuzaki K., Murase O., Miyajima K. Kinetics of pore formation by an antimicrobial peptide, magainin 2, in phospholipid bilayers. Biochemistry 1995, 34(39):12553-12559.
    • (1995) Biochemistry , vol.34 , Issue.39 , pp. 12553-12559
    • Matsuzaki, K.1    Murase, O.2    Miyajima, K.3
  • 26
    • 0031846514 scopus 로고    scopus 로고
    • A gloverin-like antibacterial protein is synthesized in Helicoverpa armigera following bacterial challenge
    • Mackintosh J.A., Gooley A.A., Karuso P.H., Beattie A.J., Jardine D.R., Veal D.A. A gloverin-like antibacterial protein is synthesized in Helicoverpa armigera following bacterial challenge. Dev. Comp. Immunol. 1998, 22:387-399.
    • (1998) Dev. Comp. Immunol. , vol.22 , pp. 387-399
    • Mackintosh, J.A.1    Gooley, A.A.2    Karuso, P.H.3    Beattie, A.J.4    Jardine, D.R.5    Veal, D.A.6
  • 27
    • 0242494111 scopus 로고    scopus 로고
    • Stable expression of recombinant human alpha3/4 fucosyltransferase III in Spodoptera frugiperda Sf9 cells
    • Morais V.A., Costa J. Stable expression of recombinant human alpha3/4 fucosyltransferase III in Spodoptera frugiperda Sf9 cells. J. Biotech. 2003, 106(1):69-75.
    • (2003) J. Biotech. , vol.106 , Issue.1 , pp. 69-75
    • Morais, V.A.1    Costa, J.2
  • 28
    • 0347479229 scopus 로고    scopus 로고
    • Molecular basis of bacterial outer membrane permeability revisited
    • Nikaido H. Molecular basis of bacterial outer membrane permeability revisited. Micro. Mol. Biol. Rev. 2003, 67(4):593-656.
    • (2003) Micro. Mol. Biol. Rev. , vol.67 , Issue.4 , pp. 593-656
    • Nikaido, H.1
  • 29
    • 34548486254 scopus 로고    scopus 로고
    • Heterologous expression of wildtype and mutant myocilin in high five insect cells shows comparable effects to cultivated trabecular meshwork cells
    • Oezbey S., Stengel C., Schlötzer-Schrehardt U., Ekici A., Rautenstrauss B. Heterologous expression of wildtype and mutant myocilin in high five insect cells shows comparable effects to cultivated trabecular meshwork cells. Biomol. Eng. 2007, 24(3):313-317.
    • (2007) Biomol. Eng. , vol.24 , Issue.3 , pp. 313-317
    • Oezbey, S.1    Stengel, C.2    Schlötzer-Schrehardt, U.3    Ekici, A.4    Rautenstrauss, B.5
  • 30
    • 0028275743 scopus 로고
    • Induction of cecropin-like and attacin-like antibacterial but not antiviral activity in larvae
    • Ourth D.D., Lockey T.D., Renis H.E. Induction of cecropin-like and attacin-like antibacterial but not antiviral activity in larvae. Biochem. Biophys. Res. Commun. 1994, 200(1):35-44.
    • (1994) Biochem. Biophys. Res. Commun. , vol.200 , Issue.1 , pp. 35-44
    • Ourth, D.D.1    Lockey, T.D.2    Renis, H.E.3
  • 31
    • 69249137055 scopus 로고    scopus 로고
    • Characterizing vesicle leakage by fluorescent lifetime measurements
    • Patel H., Tscheka C., Heerklotz H. Characterizing vesicle leakage by fluorescent lifetime measurements. Soft Matter 2009, 5(15):2849-2851.
    • (2009) Soft Matter , vol.5 , Issue.15 , pp. 2849-2851
    • Patel, H.1    Tscheka, C.2    Heerklotz, H.3
  • 32
    • 78449236736 scopus 로고    scopus 로고
    • Antimicrobial peptides: primeval molecules or future drugs
    • Peters B.M., Shirtliff M.E., Jabra-Rizk M.A. Antimicrobial peptides: primeval molecules or future drugs. PLoS Pathogens 2010, 6(10):e1001067.
    • (2010) PLoS Pathogens , vol.6 , Issue.10
    • Peters, B.M.1    Shirtliff, M.E.2    Jabra-Rizk, M.A.3
  • 33
    • 0030068232 scopus 로고    scopus 로고
    • Outer membrane protein A of Escherichia coli contributes to invasion of brain microvascular endothelial cells
    • Prasadarao N.V., Wass C.A., Weiser J.N., Stins M.F., Huang S.H., Kim K.S. Outer membrane protein A of Escherichia coli contributes to invasion of brain microvascular endothelial cells. Infect. Immun. 1996, 64:146-153.
    • (1996) Infect. Immun. , vol.64 , pp. 146-153
    • Prasadarao, N.V.1    Wass, C.A.2    Weiser, J.N.3    Stins, M.F.4    Huang, S.H.5    Kim, K.S.6
  • 34
    • 0035830591 scopus 로고    scopus 로고
    • Cholesterol attenuates the interaction of the antimicrobial peptide gramicidin S with phospholipid bilayer membranes
    • Prenner E.J., Lewis R.N., Jelokhani-Niaraki M., Hodges R.S., McElhaney R.N. Cholesterol attenuates the interaction of the antimicrobial peptide gramicidin S with phospholipid bilayer membranes. Biochim. Biophys. Acta 2001, 1510(1-2):83-92.
    • (2001) Biochim. Biophys. Acta , vol.1510 , Issue.1-2 , pp. 83-92
    • Prenner, E.J.1    Lewis, R.N.2    Jelokhani-Niaraki, M.3    Hodges, R.S.4    McElhaney, R.N.5
  • 35
    • 62749182871 scopus 로고    scopus 로고
    • Generation and analysis of recombinant Bunyamwera orthobunyaviruses expressing V5 epitope-tagged L proteins
    • Shi X., Elliott R.M. Generation and analysis of recombinant Bunyamwera orthobunyaviruses expressing V5 epitope-tagged L proteins. J. Gen. Virol. 2009, 90(Pt 2):297-306.
    • (2009) J. Gen. Virol. , vol.90 , Issue.PART 2 , pp. 297-306
    • Shi, X.1    Elliott, R.M.2
  • 37
  • 38
    • 0018150270 scopus 로고
    • Cell envelope and shape of Escherichia coli: multiple mutants missing the outer membrane lipoprotein and other major outer membrane proteins
    • Sonntag I., Schwarz H., Hirota Y. Cell envelope and shape of Escherichia coli: multiple mutants missing the outer membrane lipoprotein and other major outer membrane proteins. J. Bacteriol. 1978, 136(1).
    • (1978) J. Bacteriol. , vol.136 , Issue.1
    • Sonntag, I.1    Schwarz, H.2    Hirota, Y.3
  • 39
    • 0025772724 scopus 로고
    • Identification of an epitope on the P and V proteins of simian virus 5 that distinguishes between two isolates with different biological characteristics
    • Southern J.A., Young D.F., Heaney F., Baumgärtner W.K., Randall R.E. Identification of an epitope on the P and V proteins of simian virus 5 that distinguishes between two isolates with different biological characteristics. J. Gen. Virol. 1991, 72(Pt 7):1551-1557.
    • (1991) J. Gen. Virol. , vol.72 , Issue.PART 7 , pp. 1551-1557
    • Southern, J.A.1    Young, D.F.2    Heaney, F.3    Baumgärtner, W.K.4    Randall, R.E.5
  • 42
    • 77953721392 scopus 로고    scopus 로고
    • Immune responses of Helicoverpa armigera to different kinds of pathogens
    • Wang Q., Liu Y., He H.J., Zhao X.F., Wang J.X. Immune responses of Helicoverpa armigera to different kinds of pathogens. BMC Immunology 2010, 11(1):9.
    • (2010) BMC Immunology , vol.11 , Issue.1 , pp. 9
    • Wang, Q.1    Liu, Y.2    He, H.J.3    Zhao, X.F.4    Wang, J.X.5
  • 43
    • 77953762782 scopus 로고    scopus 로고
    • Proteomics of the Autographa californica nucleopolyhedrovirus budded virions
    • Wang R., Deng F., Hou D., Zhao Y., Guo L., Wang H., Hu Z. Proteomics of the Autographa californica nucleopolyhedrovirus budded virions. J. Virol. 2010, 84(14):7233-7242.
    • (2010) J. Virol. , vol.84 , Issue.14 , pp. 7233-7242
    • Wang, R.1    Deng, F.2    Hou, D.3    Zhao, Y.4    Guo, L.5    Wang, H.6    Hu, Z.7
  • 44
    • 0027250356 scopus 로고
    • Storage protein uptake in Helicoverpa zea. Purification of the very high density lipoprotein receptor from perivisceral fat body
    • Wang Z., Haunerland N.H. Storage protein uptake in Helicoverpa zea. Purification of the very high density lipoprotein receptor from perivisceral fat body. J. Biol. Chem. 1993, 268(22):16673-16678.
    • (1993) J. Biol. Chem. , vol.268 , Issue.22 , pp. 16673-16678
    • Wang, Z.1    Haunerland, N.H.2
  • 45
    • 0028061984 scopus 로고
    • Interactions between human defensins and lipid bilayers: evidence for formation of multimeric pores
    • Wimley W.C., Selsted, Michael E., White S.H. Interactions between human defensins and lipid bilayers: evidence for formation of multimeric pores. Protein Sci. 1994, 3(9):1362-1373.
    • (1994) Protein Sci. , vol.3 , Issue.9 , pp. 1362-1373
    • Wimley, W.C.1    Selsted Michael, E.2    White, S.H.3
  • 46
    • 0001549579 scopus 로고
    • The chemistry of insect hemolymph; organic components of the hemolymph of the silkworm, Bombyx mori, and two other species
    • Wyatt G.R., Loughheed T.C., Wyatt S.S. The chemistry of insect hemolymph; organic components of the hemolymph of the silkworm, Bombyx mori, and two other species. J. Gen. Physiol. 1956, 39(6):853-868.
    • (1956) J. Gen. Physiol. , vol.39 , Issue.6 , pp. 853-868
    • Wyatt, G.R.1    Loughheed, T.C.2    Wyatt, S.S.3
  • 47
    • 61349125577 scopus 로고    scopus 로고
    • Comparative proteomic analysis between the domesticated silkworm (Bombyx mori) reared on fresh mulberry leaves and on artificial diet
    • Zhou Z.H., Yang H.J., Chen M., Lou C.F., Zhang Y.Z., Chen K.P., Wang Y., Yu M.L., Yu F., Li J.Y., Zhong B.X. Comparative proteomic analysis between the domesticated silkworm (Bombyx mori) reared on fresh mulberry leaves and on artificial diet. J. Proteome. Res. 2008, 7(12):5103-5111.
    • (2008) J. Proteome. Res. , vol.7 , Issue.12 , pp. 5103-5111
    • Zhou, Z.H.1    Yang, H.J.2    Chen, M.3    Lou, C.F.4    Zhang, Y.Z.5    Chen, K.P.6    Wang, Y.7    Yu, M.L.8    Yu, F.9    Li, J.Y.10    Zhong, B.X.11


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.