메뉴 건너뛰기




Volumn 1, Issue 3, 2010, Pages 206-214

Coevolution between pathogen-derived proteinases and proteinase inhibitors of host insects

Author keywords

Coevolution; Innate immunity; Insects; Microbes; Proteinase inhibitors; Proteinases; Virulence

Indexed keywords

CECROPIN; PROTEINASE; SERINE PROTEINASE INHIBITOR; THERMOLYSIN;

EID: 77955746836     PISSN: 21505594     EISSN: 21505608     Source Type: Journal    
DOI: 10.4161/viru.1.3.12072     Document Type: Article
Times cited : (82)

References (90)
  • 1
    • 0000371962 scopus 로고
    • When is it coevolution?
    • Janzen D. When is it coevolution? Evol 1980; 34:611-612.
    • (1980) Evol , vol.34 , pp. 611-612
    • Janzen, D.1
  • 2
    • 34547613760 scopus 로고    scopus 로고
    • Exploiting amoeboid and non-vertebrate animal model systems to study virulence of human pathogenic fungi
    • Mylonakis E, Casadevall A, Ausubel FM. Exploiting amoeboid and non-vertebrate animal model systems to study virulence of human pathogenic fungi. PLoS Pathog 2007; 3:101.
    • (2007) PLoS Pathog , vol.3 , pp. 101
    • Mylonakis, E.1    Casadevall, A.2    Ausubel, F.M.3
  • 3
    • 45849135594 scopus 로고    scopus 로고
    • Natural selection on the Drosophila antiomicrobial immune system
    • Lazzaro BP. Natural selection on the Drosophila antiomicrobial immune system. Curr Opin Microbiol 2008; 11:284-289.
    • (2008) Curr Opin Microbiol , vol.11 , pp. 284-289
    • Lazzaro, B.P.1
  • 4
    • 0032965861 scopus 로고    scopus 로고
    • Parasitic fungi and their interactions with the insect immune system
    • Vilcinskas A, Götz P. Parasitic fungi and their interactions with the insect immune system. Adv Parasitol 1999; 43:267-313.
    • (1999) Adv Parasitol , vol.43 , pp. 267-313
    • Vilcinskas, A.1    Götz, P.2
  • 5
    • 33645876474 scopus 로고    scopus 로고
    • The regulation of pathogenicity and mutualism in Photorhabdus
    • Joyce SA, Watson RJ, Clarke DJ. The regulation of pathogenicity and mutualism in Photorhabdus. Curr Opin Micrbiol 2006; 9:127-132.
    • (2006) Curr Opin Micrbiol , vol.9 , pp. 127-132
    • Joyce, S.A.1    Watson, R.J.2    Clarke, D.J.3
  • 6
    • 41449117022 scopus 로고    scopus 로고
    • Comparative analysis of the Photorhabdus luminescens and Yersinia enterocolitica genomes: Uncovering candidate genes involved in insect pathogenesis
    • Heermann R, Fuchs TM. Comparative analysis of the Photorhabdus luminescens and Yersinia enterocolitica genomes: uncovering candidate genes involved in insect pathogenesis. BMC Genomics 2008; 9:40.
    • (2008) BMC Genomics , vol.9 , pp. 40
    • Heermann, R.1    Fuchs, T.M.2
  • 7
    • 44849124539 scopus 로고    scopus 로고
    • Photorhabdus luminescens gene induced upon insect infection
    • Münch A, Stingl L, Jung K, Heermann R. Photorhabdus luminescens gene induced upon insect infection. BMC Genomics 2008; 9:229.
    • (2008) BMC Genomics , vol.9 , pp. 229
    • Münch, A.1    Stingl, L.2    Jung, K.3    Heermann, R.4
  • 8
    • 33748502140 scopus 로고    scopus 로고
    • Developing insects as models for current and emerging human pathogens
    • Scully L, Bidochka M. Developing insects as models for current and emerging human pathogens. FEMS Microbiol Lett 2006; 263:1-9.
    • (2006) FEMS Microbiol Lett , vol.263 , pp. 1-9
    • Scully, L.1    Bidochka, M.2
  • 10
    • 33746287716 scopus 로고    scopus 로고
    • Using non-mammalian hosts to study fungal virulence and host defense
    • Fuchs B, Mylonakis E. Using non-mammalian hosts to study fungal virulence and host defense. Curr Opin Microbiol 2006; 9:346-351.
    • (2006) Curr Opin Microbiol , vol.9 , pp. 346-351
    • Fuchs, B.1    Mylonakis, E.2
  • 11
    • 72149130268 scopus 로고    scopus 로고
    • Comparative analysis of the virulence of invertebrate and mammalian pathogenic bacteria in the oral insect infection model Galleria mellonella
    • Fedhila S, Buisson C, Dussurget O, Serror P, Glomski IJ, Liehl P, et al. Comparative analysis of the virulence of invertebrate and mammalian pathogenic bacteria in the oral insect infection model Galleria mellonella. J Invertebr Pathol 2010; 103:24-29.
    • (2010) J Invertebr Pathol , vol.103 , pp. 24-29
    • Fedhila, S.1    Buisson, C.2    Dussurget, O.3    Serror, P.4    Glomski, I.J.5    Liehl, P.6
  • 13
    • 0037165196 scopus 로고    scopus 로고
    • Antimicrobial peptides of multicellular organisms
    • Zasloff M. Antimicrobial peptides of multicellular organisms. Nature 2002; 415:389-395.
    • (2002) Nature , vol.415 , pp. 389-395
    • Zasloff, M.1
  • 14
    • 1642545489 scopus 로고    scopus 로고
    • Menin. Anti-microbial peptides: From invertebrates to vertebrates
    • Bulet P, Stöcklin R, Menin. Anti-microbial peptides: from invertebrates to vertebrates. Immunol Rev 2004; 198:169-184.
    • (2004) Immunol Rev , vol.198 , pp. 169-184
    • Bulet, P.1    Stöcklin, R.2
  • 15
    • 34548045312 scopus 로고    scopus 로고
    • Unifying themes in host defence effector polypeptides
    • Yeman MR, Yount NY. Unifying themes in host defence effector polypeptides. Nature Rev Microbiol 2007; 5:727-740.
    • (2007) Nature Rev Microbiol , vol.5 , pp. 727-740
    • Yeman, M.R.1    Yount, N.Y.2
  • 16
    • 8444238186 scopus 로고    scopus 로고
    • Duplication and diversifying selection among termite antifungal peptides
    • Bulmer M, Crozier R. Duplication and diversifying selection among termite antifungal peptides. Mol Biol Evol 2004; 21:2256-2264.
    • (2004) Mol Biol Evol , vol.21 , pp. 2256-2264
    • Bulmer, M.1    Crozier, R.2
  • 17
    • 33747347594 scopus 로고    scopus 로고
    • Functional divergence of six isoforms of antifungal peptide drosomycin in Drosophila melanogaster
    • Yang WY, Wen SY, Huang YD, Ye MQ, Deng XJ, Han D, et al. Functional divergence of six isoforms of antifungal peptide drosomycin in Drosophila melanogaster. Gene 2006; 379:26-32.
    • (2006) Gene , vol.379 , pp. 26-32
    • Yang, W.Y.1    Wen, S.Y.2    Huang, Y.D.3    Ye, M.Q.4    Deng, X.J.5    Han, D.6
  • 18
    • 33845673319 scopus 로고    scopus 로고
    • Evolutionary selective trends of insect/mosquito antimicrobial defensin peptides containing cysteine-stabilized α/β motifs
    • Dassanayake R, Gunawardene Y, Tobe S. Evolutionary selective trends of insect/mosquito antimicrobial defensin peptides containing cysteine-stabilized α/β motifs. Peptides 2007; 28:62-75.
    • (2007) Peptides , vol.28 , pp. 62-75
    • Dassanayake, R.1    Gunawardene, Y.2    Tobe, S.3
  • 19
    • 48249137383 scopus 로고    scopus 로고
    • Anti-fungal innate immunity in C. elegans is enhanced by evolutionary diversification of antimicrobial peptides
    • Pujol N, Zugasti O, Wong D, Couillault C, Kurz CL, Schulenburg H, Ewbank JJ. Anti-fungal innate immunity in C. elegans is enhanced by evolutionary diversification of antimicrobial peptides. PLoS Pathog 2008; 4:1000105.
    • (2008) PLoS Pathog , vol.4 , pp. 1000105
    • Pujol, N.1    Zugasti, O.2    Wong, D.3    Couillault, C.4    Kurz, C.L.5    Schulenburg, H.6    Ewbank, J.J.7
  • 20
    • 43549106617 scopus 로고    scopus 로고
    • Diversification and adaptive sequence evolution of Caenorhabditis lysozymes
    • Schulenburg H, Boehnisch C. Diversification and adaptive sequence evolution of Caenorhabditis lysozymes. BMC Evol Biol 2008; 8:114.
    • (2008) BMC Evol Biol , vol.8 , pp. 114
    • Schulenburg, H.1    Boehnisch, C.2
  • 21
    • 57149115580 scopus 로고    scopus 로고
    • Porcine host defense peptides: Expanding repertoire and functions
    • Sang Y, Blecha F. Porcine host defense peptides: expanding repertoire and functions. Dev Comp Immunol 2009; 33:334-343.
    • (2009) Dev Comp Immunol , vol.33 , pp. 334-343
    • Sang, Y.1    Blecha, F.2
  • 22
    • 42149112852 scopus 로고    scopus 로고
    • Drosophila innate immunity and response to fungal infections
    • Levitin A, Whiteway M. Drosophila innate immunity and response to fungal infections. Cell Microbiol 2008; 10:1021-1026.
    • (2008) Cell Microbiol , vol.10 , pp. 1021-1026
    • Levitin, A.1    Whiteway, M.2
  • 23
    • 61449163214 scopus 로고    scopus 로고
    • Corruption of innate immunity by bacterial proteases
    • Potempa J, Robert NP. Corruption of innate immunity by bacterial proteases. J Innate Immun 2009; 1:70-87.
    • (2009) J Innate Immun , vol.1 , pp. 70-87
    • Potempa, J.1    Robert, N.P.2
  • 24
    • 33646384915 scopus 로고    scopus 로고
    • Proteases and protease inhibitors: A balance of activities in host-pathogen interaction
    • Armstrong PB. Proteases and protease inhibitors: a balance of activities in host-pathogen interaction. Immunobiol 2006; 211:263-281.
    • (2006) Immunobiol , vol.211 , pp. 263-281
    • Armstrong, P.B.1
  • 25
    • 0036784566 scopus 로고    scopus 로고
    • Insect hemocytes and their role in immunity
    • Lavine MD, StrandMR. Insect hemocytes and their role in immunity. Insect Biochem Mol Biol 2002; 32:1295-1309.
    • (2002) Insect Biochem Mol Biol , vol.32 , pp. 1295-1309
    • Lavine, M.D.1    Strand, M.R.2
  • 26
    • 44649197623 scopus 로고    scopus 로고
    • The proPO-system: Pros and cons for its role in invertebrate immunity
    • Cerenius L, Lee BL, Söderhäll K. The proPO-system: pros and cons for its role in invertebrate immunity. Trends Immunol 2008; 29:263-271.
    • (2008) Trends Immunol , vol.29 , pp. 263-271
    • Cerenius, L.1    Lee, B.L.2    Söderhäll, K.3
  • 27
    • 53149116721 scopus 로고    scopus 로고
    • Host-derived extracellular nucleic acids enhance innate immune responses, induce coagulation and prolong survival upon infection in insects
    • Altincicek B, Stötzel S, Wygrecka M, Preissner K, Vilcinskas A. Host-derived extracellular nucleic acids enhance innate immune responses, induce coagulation and prolong survival upon infection in insects. J Immunol 2008; 181:2705-2712.
    • (2008) J Immunol , vol.181 , pp. 2705-2712
    • Altincicek, B.1    Stötzel, S.2    Wygrecka, M.3    Preissner, K.4    Vilcinskas, A.5
  • 28
    • 0017156997 scopus 로고
    • Studies on the insect bacteriolytic enzymes-II. Some physical and enzymatic properties of lysozme from haemolymph of Galleria mellonella
    • Powning RF, Davidson WJ. Studies on the insect bacteriolytic enzymes-II. Some physical and enzymatic properties of lysozme from haemolymph of Galleria mellonella. Comp Biochem Physiol 1976; 55:221-228.
    • (1976) Comp Biochem Physiol , vol.55 , pp. 221-228
    • Powning, R.F.1    Davidson, W.J.2
  • 29
    • 0036823772 scopus 로고    scopus 로고
    • Comparative study on characteristics of lysozymes from the hemolymph of three lepidopteran larvae, Galleria mellonella, Bombyx mori, Agrius convolvuli
    • Yu KH, Kim KN, Lee JH, LeeHS, Kim SH, Cho KY, et al. Comparative study on characteristics of lysozymes from the hemolymph of three lepidopteran larvae, Galleria mellonella, Bombyx mori, Agrius convolvuli. Dev Comp Immunol 2002; 26:707-713.
    • (2002) Dev Comp Immunol , vol.26 , pp. 707-713
    • Yu, K.H.1    Kim, K.N.2    Lee, J.H.3    Lee, H.S.4    Kim, S.H.5    Cho, K.Y.6
  • 30
    • 77955720027 scopus 로고
    • Lytic action of lysozyme on Candida albicans
    • Kamaya T. Lytic action of lysozyme on Candida albicans. Mycopathol Mycologia App 1970; 37:320-330.
    • (1970) Mycopathol Mycologia App , vol.37 , pp. 320-330
    • Kamaya, T.1
  • 31
    • 0016293172 scopus 로고
    • Inhibition by lysozyome on the growth of the sperule phase of Coccidoides immitis in vitro
    • Collins MS, Papagianis D. Inhibition by lysozyome on the growth of the sperule phase of Coccidoides immitis in vitro. Infect Immun 1974; 10:616-623.
    • (1974) Infect Immun , vol.10 , pp. 616-623
    • Collins, M.S.1    Papagianis, D.2
  • 32
    • 77649237880 scopus 로고    scopus 로고
    • Antimicrobial peptides: General overview and clinical implications in human health and disease
    • Guaní-Guerra E, Santos-Mendoza T, Lugo-Reyes SO, Terán LM. Antimicrobial peptides: General overview and clinical implications in human health and disease. Clin Immunol 2010; 135:1-11.
    • (2010) Clin Immunol , vol.135 , pp. 1-11
    • Guaní-Guerra, E.1    Santos-Mendoza, T.2    Lugo-Reyes, S.O.3    Terán, L.M.4
  • 34
    • 1642416091 scopus 로고    scopus 로고
    • Genetic basis of natural variation in D. melanogaster antibacterial immunity
    • Lazzaro BP, Sceurman BK, Clark AG. Genetic basis of natural variation in D. melanogaster antibacterial immunity. Science 2004; 303:1873-1876.
    • (2004) Science , vol.303 , pp. 1873-1876
    • Lazzaro, B.P.1    Sceurman, B.K.2    Clark, A.G.3
  • 35
    • 11344267777 scopus 로고    scopus 로고
    • Insect antimicrobial peptides: Structures, properties and gene regulation
    • Bulet P, Stöcklin R. Insect antimicrobial peptides: structures, properties and gene regulation. Protein Peptide Lett 2005; 12:3-11.
    • (2005) Protein Peptide Lett , vol.12 , pp. 3-11
    • Bulet, P.1    Stöcklin, R.2
  • 36
    • 85011940533 scopus 로고    scopus 로고
    • Purification, cDNA cloning and expression of an insect defensin from the great wax moth, Galleria mellonella
    • Lee YS, Yun EK, Jang WS, Kim I, Lee JH, et al. Purification, cDNA cloning and expression of an insect defensin from the great wax moth, Galleria mellonella. Insect Mol Biol 2004; 35:1335-1346.
    • (2004) Insect Mol Biol , vol.35 , pp. 1335-1346
    • Lee, Y.S.1    Yun, E.K.2    Jang, W.S.3    Kim, I.4    Lee, J.H.5
  • 37
    • 0042970579 scopus 로고    scopus 로고
    • Cloning and expression of gallerimycin, an antifungal peptide expressed in immune response by the greater wax moth, Galleria mellonella
    • Schuhmann B, Seitz V, Vilcinskas A, Podsiadlowski L. Cloning and expression of gallerimycin, an antifungal peptide expressed in immune response by the greater wax moth, Galleria mellonella. Arch Insect Biochem Physiol 2003; 53:125-133.
    • (2003) Arch Insect Biochem Physiol , vol.53 , pp. 125-133
    • Schuhmann, B.1    Seitz, V.2    Vilcinskas, A.3    Podsiadlowski, L.4
  • 38
    • 33746047082 scopus 로고    scopus 로고
    • Transgenic expression of gallerimycin, a novel antifungal insect defensin from the greater wax moth Galleria mellonella, confers resistance against pathogenic fungi in tobacco
    • Langen G, Imani B, Altinciek G, Kieseritzky G, Kogel KH, Vilcinskas A. Transgenic expression of gallerimycin, a novel antifungal insect defensin from the greater wax moth Galleria mellonella, confers resistance against pathogenic fungi in tobacco. Biol Chem 2006; 387:549-557.
    • (2006) Biol Chem , vol.387 , pp. 549-557
    • Langen, G.1    Imani, B.2    Altinciek, G.3    Kieseritzky, G.4    Kogel, K.H.5    Vilcinskas, A.6
  • 39
    • 0345724808 scopus 로고    scopus 로고
    • Arthropod and mollusk defensins-evolution by exon-shiffling
    • Froy O, Gurevitz M. Arthropod and mollusk defensins-evolution by exon-shiffling. Trends Genetics 2003; 19:684-687.
    • (2003) Trends Genetics , vol.19 , pp. 684-687
    • Froy, O.1    Gurevitz, M.2
  • 40
    • 0019386682 scopus 로고
    • Sequence and specificity of two antibacterial proteins involved in insect immunity
    • Steiner H, Hultmark D, Engstrom A, Bennich H, Boman HG. Sequence and specificity of two antibacterial proteins involved in insect immunity. Nature 1981; 292:246-248.
    • (1981) Nature , vol.292 , pp. 246-248
    • Steiner, H.1    Hultmark, D.2    Engstrom, A.3    Bennich, H.4    Boman, H.G.5
  • 41
    • 1242344146 scopus 로고    scopus 로고
    • Purification and cDNA cloning of a cecropin-like peptide from great wax moth, Galleria mellonella
    • Kim CH, Lee JH, Kim I, Seo SJ, Son SM, Lee KY, Lee IH. Purification and cDNA cloning of a cecropin-like peptide from great wax moth, Galleria mellonella. Mol Cells 2004; 17:262-266.
    • (2004) Mol Cells , vol.17 , pp. 262-266
    • Kim, C.H.1    Lee, J.H.2    Kim, I.3    Seo, S.J.4    Son, S.M.5    Lee, K.Y.6    Lee, I.H.7
  • 42
    • 0029609285 scopus 로고
    • Moricin, a novel type of antibacterial peptide isolated from the silkworm, Bombyx mori
    • Hara S, Yamakawa MA. Moricin, a novel type of antibacterial peptide isolated from the silkworm, Bombyx mori. J Biol Chem 1995; 270:29923-29927.
    • (1995) J Biol Chem , vol.270 , pp. 29923-29927
    • Hara, S.1    Yamakawa, M.A.2
  • 43
    • 38349052959 scopus 로고    scopus 로고
    • The discovery and analysis of a diverged family of novel antifungal moricin-like peptides in the wax moth Galleria mellonella
    • Brown S, Howard A, Kasprzak AB, Gordon K, East P. The discovery and analysis of a diverged family of novel antifungal moricin-like peptides in the wax moth Galleria mellonella. Insect Biochem Mol Biol 2008; 38:201-212.
    • (2008) Insect Biochem Mol Biol , vol.38 , pp. 201-212
    • Brown, S.1    Howard, A.2    Kasprzak, A.B.3    Gordon, K.4    East, P.5
  • 44
    • 33846794525 scopus 로고    scopus 로고
    • Purfication and characterization of eight peptides from Galleria mellonella immune hemolymph
    • Cytrynska M, Mak P, Zdybicka-Barabas A, Suder P, Jakubowicz T. Purfication and characterization of eight peptides from Galleria mellonella immune hemolymph. Peptides 2007; 28:533-546.
    • (2007) Peptides , vol.28 , pp. 533-546
    • Cytrynska, M.1    Mak, P.2    Zdybicka-Barabas, A.3    Suder, P.4    Jakubowicz, T.5
  • 45
    • 70449658824 scopus 로고    scopus 로고
    • A peptidomics study reveals the impressive antimicrobial peptide arsenal of the wax moth Galleria mellonella
    • Brown SE, Howard A, Kasprzak AB, Gordon KH, East PD. A peptidomics study reveals the impressive antimicrobial peptide arsenal of the wax moth Galleria mellonella. Insect Biochem Mol Biol 2009; 39:792-800.
    • (2009) Insect Biochem Mol Biol , vol.39 , pp. 792-800
    • Brown, S.E.1    Howard, A.2    Kasprzak, A.B.3    Gordon, K.H.4    East, P.D.5
  • 46
    • 0007555611 scopus 로고    scopus 로고
    • Effect of the entomopathogenic fungus Beauveria bassiana on humoral immune response of Galleria mellonella larvae (Lepidoptera: Pyralidae)
    • Vilcinskas A, Matha V. Effect of the entomopathogenic fungus Beauveria bassiana on humoral immune response of Galleria mellonella larvae (Lepidoptera: Pyralidae). Eur J Entomol 1997; 94:461-472.
    • (1997) Eur J Entomol , vol.94 , pp. 461-472
    • Vilcinskas, A.1    Matha, V.2
  • 47
    • 0030835341 scopus 로고    scopus 로고
    • Inhibition of phagocytic activity of plasmatocytes isolated from Galleria mellonella by entomogenous fungi and their secondary metabolites
    • Vilcinskas A, Matha V, Götz P. Inhibition of phagocytic activity of plasmatocytes isolated from Galleria mellonella by entomogenous fungi and their secondary metabolites. J Insect Physiol 1997; 43:475-483.
    • (1997) J Insect Physiol , vol.43 , pp. 475-483
    • Vilcinskas, A.1    Matha, V.2    Götz, P.3
  • 48
    • 0031280505 scopus 로고    scopus 로고
    • Effects of the entomopathogenic fungus Metarhizium anisopliae and its secondary metabolites on morphology and cytoskeleton of plasmatocytes isolated from Galleria mellonella
    • Vilcinskas A, Matha V, Götz P. Effects of the entomopathogenic fungus Metarhizium anisopliae and its secondary metabolites on morphology and cytoskeleton of plasmatocytes isolated from Galleria mellonella. J Insect Physiol 1997; 43:1149-1159.
    • (1997) J Insect Physiol , vol.43 , pp. 1149-1159
    • Vilcinskas, A.1    Matha, V.2    Götz, P.3
  • 49
    • 34447624650 scopus 로고    scopus 로고
    • Fungal peptide destruxin A plays a specific role in suppressing the innate immune response in Drosophila melanogaster
    • Pal S, St. leger RJ, Wu LP. Fungal peptide destruxin A plays a specific role in suppressing the innate immune response in Drosophila melanogaster. J Biol Chem 2007; 282:8969-8977.
    • (2007) J Biol Chem , vol.282 , pp. 8969-8977
    • Pal, S.1    Leger, R.J.2    Wu, L.P.3
  • 50
    • 70349671455 scopus 로고    scopus 로고
    • Insect peptide metchnikowin confers on barley a selective capacity for resistance to ascomycota fungal pathogens
    • Rahnamaeian M, Langen G, Imani J, Altincicek B, von Wettstein D, Kogel KH, Vilcinskas A. Insect peptide metchnikowin confers on barley a selective capacity for resistance to ascomycota fungal pathogens. J Exp Bot 2009; 60:4105-4114.
    • (2009) J Exp Bot , vol.60 , pp. 4105-4114
    • Rahnamaeian, M.1    Langen, G.2    Imani, J.3    Altincicek, B.4    von Wettstein, D.5    Kogel, K.H.6    Vilcinskas, A.7
  • 51
    • 77953432815 scopus 로고    scopus 로고
    • Conidial surface proteins Metarhizium anisopliae: Source of activities related with toxic effects, host penetration and pathogenesis
    • Santi L, Beys de Silva WO, Berger M, Guimaraes JA, Schrank A, Vainstain MA. Conidial surface proteins Metarhizium anisopliae: source of activities related with toxic effects, host penetration and pathogenesis. Toxicon 2010; 55:874-880.
    • (2010) Toxicon , vol.55 , pp. 874-880
    • Santi, L.1    de Silva, B.W.O.2    Berger, M.3    Guimaraes, J.A.4    Schrank, A.5    Vainstain, M.A.6
  • 52
    • 0028141988 scopus 로고
    • Isoforms of the cuticle-degrading Pr1 proteinase and production of a metalloproteinase by Metarhizium anisopliae
    • St. Leger RJ, Bidochka MJ, Roberts DW. Isoforms of the cuticle-degrading Pr1 proteinase and production of a metalloproteinase by Metarhizium anisopliae. Arch Biochem Biophys 1994; 313:1-7.
    • (1994) Arch Biochem Biophys , vol.313 , pp. 1-7
    • Leger, R.J.1    Bidochka, M.J.2    Roberts, D.W.3
  • 53
    • 0031701527 scopus 로고    scopus 로고
    • Proteases released by entomopathogenic fungi impair phagocytic activity, attachment and spreading of plasmatocytes isolated from hemolymph of the greater wax moth Galleria mellonella
    • Griesch J, Vilcinskas A. Proteases released by entomopathogenic fungi impair phagocytic activity, attachment and spreading of plasmatocytes isolated from hemolymph of the greater wax moth Galleria mellonella. Biocontr Sci Techn 1998; 8:517-531.
    • (1998) Biocontr Sci Techn , vol.8 , pp. 517-531
    • Griesch, J.1    Vilcinskas, A.2
  • 54
    • 0033973889 scopus 로고    scopus 로고
    • Microbial metalloproteases and pathogenesis
    • Miyoshi S, Shinoda S. Microbial metalloproteases and pathogenesis. Microb Infect 2000; 2:91-98.
    • (2000) Microb Infect , vol.2 , pp. 91-98
    • Miyoshi, S.1    Shinoda, S.2
  • 55
    • 58149103584 scopus 로고    scopus 로고
    • The thermolysin family (M4) of enzymes: Therapeutic and biotechnological potential
    • Adekoya O, Sylte I. The thermolysin family (M4) of enzymes: therapeutic and biotechnological potential. Chem Biol Drug Des 2009; 73:7-16.
    • (2009) Chem Biol Drug Des , vol.73 , pp. 7-16
    • Adekoya, O.1    Sylte, I.2
  • 56
    • 38449113749 scopus 로고    scopus 로고
    • A metalloprotease secreted by the pathogen Photorhabdus luminescens induces melanization
    • Held KG, Larock CN, D Argenio DA, Berg CA, Collins CM. A metalloprotease secreted by the pathogen Photorhabdus luminescens induces melanization. Appl Env Microbiol 2007; 73:7622-7628.
    • (2007) Appl Env Microbiol , vol.73 , pp. 7622-7628
    • Held, K.G.1    Larock, C.N.2    Argenio, D.D.A.3    Berg, C.A.4    Collins, C.M.5
  • 57
    • 0032992544 scopus 로고    scopus 로고
    • Serine proteinase inhibitors in arthropod immunity
    • Kanost MR. Serine proteinase inhibitors in arthropod immunity. Dev Comp Immunol 1999; 23:291-301.
    • (1999) Dev Comp Immunol , vol.23 , pp. 291-301
    • Kanost, M.R.1
  • 58
    • 0034069583 scopus 로고    scopus 로고
    • Isolation and characterization of novel inducible serine protease inhibitors from larval hemolymph of the greater wax moth, Galleria mellonella
    • Fröbius A, Kanost M, Götz P, Vilcinskas A. Isolation and characterization of novel inducible serine protease inhibitors from larval hemolymph of the greater wax moth, Galleria mellonella. Eur J Biochem 2000; 267:2046-2053.
    • (2000) Eur J Biochem , vol.267 , pp. 2046-2053
    • Fröbius, A.1    Kanost, M.2    Götz, P.3    Vilcinskas, A.4
  • 59
    • 3242714188 scopus 로고    scopus 로고
    • A Kunitz type protease inhibitor related protein is synthesized in Drosophila prepupal salivary glands and released into the moulting fluid during pupation
    • Kress H, Jarrin A, Thüroff E, Saunders R, Weise C, Schmidtam Busch M, et al. A Kunitz type protease inhibitor related protein is synthesized in Drosophila prepupal salivary glands and released into the moulting fluid during pupation. Insect Biochem Mol Biol 2004; 34:855-869.
    • (2004) Insect Biochem Mol Biol , vol.34 , pp. 855-869
    • Kress, H.1    Jarrin, A.2    Thüroff, E.3    Saunders, R.4    Weise, C.5    Schmidtam, B.M.6
  • 60
    • 74449087251 scopus 로고    scopus 로고
    • Structure and function Kazal-type serine proteinase inhibitors
    • Rimphanitchayakit V, Tassanakajon A. Structure and function Kazal-type serine proteinase inhibitors. Dev Comp Immunol 2010; 34:377-386.
    • (2010) Dev Comp Immunol , vol.34 , pp. 377-386
    • Rimphanitchayakit, V.1    Tassanakajon, A.2
  • 61
    • 0036921508 scopus 로고    scopus 로고
    • Insect inhibitors of metalloproteinases
    • Vilcinskas A, Wedde M. Insect inhibitors of metalloproteinases. IUBMB Life 2002; 54:339-343.
    • (2002) IUBMB Life , vol.54 , pp. 339-343
    • Vilcinskas, A.1    Wedde, M.2
  • 62
    • 0032146755 scopus 로고    scopus 로고
    • Purification and characterization of an inducible metalloprotease inhibitor from the hemolymph of greater wax moth larvae, Galleria mellonella
    • Wedde M, Weise C, Kopacek P, Franke P, Vilcinskas A. Purification and characterization of an inducible metalloprotease inhibitor from the hemolymph of greater wax moth larvae, Galleria mellonella. Eur J Biochem 1998; 255:534-543.
    • (1998) Eur J Biochem , vol.255 , pp. 534-543
    • Wedde, M.1    Weise, C.2    Kopacek, P.3    Franke, P.4    Vilcinskas, A.5
  • 63
    • 4344590388 scopus 로고    scopus 로고
    • Cloning and expression of an inhibitor against microbial metalloproteinases from insects (IMPI) contributing to innate immunity
    • Clermont A, Wedde M, Seitz V, Podsiadlowski L, Hummel M, Vilcinskas A. Cloning and expression of an inhibitor against microbial metalloproteinases from insects (IMPI) contributing to innate immunity. Biochem J 2004; 382:315-322.
    • (2004) Biochem J , vol.382 , pp. 315-322
    • Clermont, A.1    Wedde, M.2    Seitz, V.3    Podsiadlowski, L.4    Hummel, M.5    Vilcinskas, A.6
  • 64
    • 1642464622 scopus 로고    scopus 로고
    • Evolutionary families of peptidase inhibitors
    • Rawlings ND, Tolle DP, Barret AJ. Evolutionary families of peptidase inhibitors. Biochem J 2004; 378:705-716.
    • (2004) Biochem J , vol.378 , pp. 705-716
    • Rawlings, N.D.1    Tolle, D.P.2    Barret, A.J.3
  • 65
    • 28044470978 scopus 로고    scopus 로고
    • Evolutionary mechanisms acting on proteinase inhibitor variability
    • Christeller J. Evolutionary mechanisms acting on proteinase inhibitor variability. FEBS J 2005; 272:5710-5722.
    • (2005) FEBS J , vol.272 , pp. 5710-5722
    • Christeller, J.1
  • 66
    • 33746294374 scopus 로고    scopus 로고
    • Metamorphosis and collagen-IV-fragments stimulate innate immune response in the greater wax moth Galleria mellonella
    • Altincicek B, Vilcinskas A. Metamorphosis and collagen-IV-fragments stimulate innate immune response in the greater wax moth Galleria mellonella. Dev Comp Immunol 2006; 30:1108-1118.
    • (2006) Dev Comp Immunol , vol.30 , pp. 1108-1118
    • Altincicek, B.1    Vilcinskas, A.2
  • 67
    • 33846173565 scopus 로고    scopus 로고
    • The insect metalloproteinase inhibitor gene of the lepidopteran Galleria mellonella encodes two distinct inhibitors
    • Wedde M, Weise C, Nuck C, Altincicek B, Vilcinskas A. The insect metalloproteinase inhibitor gene of the lepidopteran Galleria mellonella encodes two distinct inhibitors. Biol Chem 2007; 388:119-127.
    • (2007) Biol Chem , vol.388 , pp. 119-127
    • Wedde, M.1    Weise, C.2    Nuck, C.3    Altincicek, B.4    Vilcinskas, A.5
  • 68
    • 37349016698 scopus 로고    scopus 로고
    • Identification of a lepidopteran matrix metalloproteinase with dual roles in metamorphosis and innate immunity
    • Altincicek B, Vilcinskas A. Identification of a lepidopteran matrix metalloproteinase with dual roles in metamorphosis and innate immunity. Dev Comp Immunol 2008; 32:400-409.
    • (2008) Dev Comp Immunol , vol.32 , pp. 400-409
    • Altincicek, B.1    Vilcinskas, A.2
  • 69
    • 72949111212 scopus 로고    scopus 로고
    • Identification of collagen IV derived danger/alarm signals in insect immunity by nanoLC-FTICR MS
    • Altincicek B, Berisha A, Mukherjee K, Spengler B, Römpp A, Vilcinskas A. Identification of collagen IV derived danger/alarm signals in insect immunity by nanoLC-FTICR MS. Biol Chem 2009; 390:1303-1311.
    • (2009) Biol Chem , vol.390 , pp. 1303-1311
    • Altincicek, B.1    Berisha, A.2    Mukherjee, K.3    Spengler, B.4    Römpp, A.5    Vilcinskas, A.6
  • 70
    • 33646230319 scopus 로고    scopus 로고
    • A collagenous protective coat enables Metarhizium anisopliae to evade insect immune responses
    • Wang C, St. Leger RJ. A collagenous protective coat enables Metarhizium anisopliae to evade insect immune responses. Proc Nat Acad Sci USA 2006; 103:6647-6652.
    • (2006) Proc Nat Acad Sci USA , vol.103 , pp. 6647-6652
    • Wang, C.1    Leger, R.J.2
  • 71
    • 45849137466 scopus 로고    scopus 로고
    • Evolution of pathogenicity in fungi
    • Humber RA. Evolution of pathogenicity in fungi. J Invertebr Path 2008; 98:262-266.
    • (2008) J Invertebr Path , vol.98 , pp. 262-266
    • Humber, R.A.1
  • 73
    • 8144231258 scopus 로고    scopus 로고
    • A phylogenomic approach to reconstructing the diversification of serine proteases in fungi
    • Hu G, St. Leger RJ. A phylogenomic approach to reconstructing the diversification of serine proteases in fungi. J Evol Biol 2004; 17:1204-1214.
    • (2004) J Evol Biol , vol.17 , pp. 1204-1214
    • Hu, G.1    Leger, R.J.2
  • 74
    • 1242341375 scopus 로고    scopus 로고
    • Multiplication of an ancestral gene encoding secreted fungalysin preceded species differentiation in the dermatophytes Trichophyton and Microsporum
    • Jousson O, Lechenne B, Bontems O, Capoccia S, Mignon B, Barblan J, et al. Multiplication of an ancestral gene encoding secreted fungalysin preceded species differentiation in the dermatophytes Trichophyton and Microsporum. Micorbiol 2004; 150:301-310.
    • (2004) Micorbiol , vol.150 , pp. 301-310
    • Jousson, O.1    Lechenne, B.2    Bontems, O.3    Capoccia, S.4    Mignon, B.5    Barblan, J.6
  • 75
    • 0348049996 scopus 로고    scopus 로고
    • Reconstructing the diversification of subtilisins in the pathogens fungus Metarhizium anisopliae
    • Bagga S, Hu G, Screen SE, St. Leger RJ. Reconstructing the diversification of subtilisins in the pathogens fungus Metarhizium anisopliae. Gene 2004; 324:159-169.
    • (2004) Gene , vol.324 , pp. 159-169
    • Bagga, S.1    Hu, G.2    Screen, S.E.3    Leger, R.J.4
  • 76
    • 34147162767 scopus 로고    scopus 로고
    • Hydrated conidia of Metarhizium anisopliae release a family of metalloproteases
    • Qazi SS, Khachatourians GG. Hydrated conidia of Metarhizium anisopliae release a family of metalloproteases. J Invertebr Pathol 2007; 95:48-59.
    • (2007) J Invertebr Pathol , vol.95 , pp. 48-59
    • Qazi, S.S.1    Khachatourians, G.G.2
  • 77
    • 66749153807 scopus 로고    scopus 로고
    • Comparative genomics using microarrays reveals divergence and loss of virulence-associated genes in host-specific strains of the insect pathogen Metarhizium anisopliae
    • Wang S, Leclerque A, Pava-Ripoll M, Fang W, St. Leger RJ. Comparative genomics using microarrays reveals divergence and loss of virulence-associated genes in host-specific strains of the insect pathogen Metarhizium anisopliae. Eukaryot Cell 2009; 8:888-898.
    • (2009) Eukaryot Cell , vol.8 , pp. 888-898
    • Wang, S.1    Leclerque, A.2    Pava-Ripoll, M.3    Fang, W.4    Leger, R.J.5
  • 78
    • 20544476855 scopus 로고    scopus 로고
    • Differential gene expression by Metarhizium anisopliae growing in root exudate and host (Manduca sexta) cuticle or hemolymph reveals mechanisms of physiological adaptation
    • Wang C, Hu G, St. Leger RJ. Differential gene expression by Metarhizium anisopliae growing in root exudate and host (Manduca sexta) cuticle or hemolymph reveals mechanisms of physiological adaptation. Fungal Genet Biol 2005; 42:704-718.
    • (2005) Fungal Genet Biol , vol.42 , pp. 704-718
    • Wang, C.1    Hu, G.2    Leger, R.J.3
  • 79
    • 12344261833 scopus 로고    scopus 로고
    • The relationship between domain duplication and recombination
    • Vogel C, Teichmann S, Pereira-Leal J. The relationship between domain duplication and recombination. J Mol Biol 2005; 346:355-365.
    • (2005) J Mol Biol , vol.346 , pp. 355-365
    • Vogel, C.1    Teichmann, S.2    Pereira-Leal, J.3
  • 81
    • 0034084470 scopus 로고    scopus 로고
    • Recognition and regulation of metalloproteinase activity in the hemolymph of Galleria mellonella: A new pathway mediating induction of humoral immune responses
    • Griesch J, Wedde M, Vilcinskas A. Recognition and regulation of metalloproteinase activity in the hemolymph of Galleria mellonella: A new pathway mediating induction of humoral immune responses. Insect Biochem Mol Biol 2000; 30:461-472.
    • (2000) Insect Biochem Mol Biol , vol.30 , pp. 461-472
    • Griesch, J.1    Wedde, M.2    Vilcinskas, A.3
  • 82
    • 33845974905 scopus 로고    scopus 로고
    • Microbial metalloproteinases mediate sensing of invading pathogens and activate innate immune responses in the lepidopteran model host Galleria mellonella
    • Altincicek B, Lindner M, Linder D, Preissner K, Vilcinskas A. Microbial metalloproteinases mediate sensing of invading pathogens and activate innate immune responses in the lepidopteran model host Galleria mellonella. Infect Immun 2007; 75:175-183.
    • (2007) Infect Immun , vol.75 , pp. 175-183
    • Altincicek, B.1    Lindner, M.2    Linder, D.3    Preissner, K.4    Vilcinskas, A.5
  • 83
    • 18044376633 scopus 로고    scopus 로고
    • Hemolymph coagulation and phenoloxidase in Drosophila larvae
    • Bidla G, Lindgren M, Theopold U, Dushay MS. Hemolymph coagulation and phenoloxidase in Drosophila larvae. Dev Comp Immunol 2005; 29:669-679
    • (2005) Dev Comp Immunol , vol.29 , pp. 669-679
    • Bidla, G.1    Lindgren, M.2    Theopold, U.3    Dushay, M.S.4
  • 84
    • 0029930574 scopus 로고    scopus 로고
    • Specific inhibition of mature fungal serine proteinase and metalloproteinase by their propeptides
    • Markaryan A, Lee JD, Sirakova TD, Kolattukudy PE. Specific inhibition of mature fungal serine proteinase and metalloproteinase by their propeptides. J Bacteriol 1996; 78:2211-2215.
    • (1996) J Bacteriol , vol.78 , pp. 2211-2215
    • Markaryan, A.1    Lee, J.D.2    Sirakova, T.D.3    Kolattukudy, P.E.4
  • 85
    • 33750002928 scopus 로고    scopus 로고
    • Expression of genes involved in germination, conidiogenesis and pathogenesis in Metarhizium anisopliae using quantitative real-time RT-PCR
    • Fang W, Bidochka MJ. Expression of genes involved in germination, conidiogenesis and pathogenesis in Metarhizium anisopliae using quantitative real-time RT-PCR. Mycol Res 2006; 110:1165-1171.
    • (2006) Mycol Res , vol.110 , pp. 1165-1171
    • Fang, W.1    Bidochka, M.J.2
  • 86
    • 68649091187 scopus 로고    scopus 로고
    • Identification of genes differentially expressed in vivo by Metarhrizium anisopliae in the hemolymph of Locusta migratoria using suppressionsubtractive hybridization
    • Zhang C, Xia Y. Identification of genes differentially expressed in vivo by Metarhrizium anisopliae in the hemolymph of Locusta migratoria using suppressionsubtractive hybridization. Curr Genet 2009; 55:399-407.
    • (2009) Curr Genet , vol.55 , pp. 399-407
    • Zhang, C.1    Xia, Y.2
  • 87
    • 38849084089 scopus 로고    scopus 로고
    • Mechanisms of pathogenesis and the evolution of parasite virulence
    • Frank SA, Schmid-Hempel P. Mechanisms of pathogenesis and the evolution of parasite virulence. J Evol Biol 2008; 21:396-404.
    • (2008) J Evol Biol , vol.21 , pp. 396-404
    • Frank, S.A.1    Schmid-Hempel, P.2
  • 88
    • 66749153807 scopus 로고    scopus 로고
    • Comparative genomics using microarrays reveals divergence and loss of virulence-associated genes in host-specific strains of the insect pathogen Metarhizium anisopliae
    • Wang S, Leclerque A, Pava-Ripoll M, Fang W, St. Leger RJ. Comparative genomics using microarrays reveals divergence and loss of virulence-associated genes in host-specific strains of the insect pathogen Metarhizium anisopliae. Eukaryotic Cell 2009; 8:888-898.
    • (2009) Eukaryotic Cell , vol.8 , pp. 888-898
    • Wang, S.1    Leclerque, A.2    Pava-Ripoll, M.3    Fang, W.4    Leger, R.J.5
  • 89
    • 43149085008 scopus 로고    scopus 로고
    • Identifying coevolving partners from paralogous gene families
    • Yeang CH. Identifying coevolving partners from paralogous gene families. Evolutionary Bioinf 2008; 4:97-107.
    • (2008) Evolutionary Bioinf , vol.4 , pp. 97-107
    • Yeang, C.H.1
  • 90
    • 21644432975 scopus 로고    scopus 로고
    • Computational aspects of host-parasite phylogenies
    • Stevens J. Computational aspects of host-parasite phylogenies.Briefings Bioinf 2004; 5:339-349.
    • (2004) Briefings Bioinf , vol.5 , pp. 339-349
    • Stevens, J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.