메뉴 건너뛰기




Volumn 101, Issue 4, 1998, Pages 298-315

Endogenous defense mechanisms of insects

Author keywords

Antimicrobial peptides; Encapsulation; Hemocytes; Parasitization; Phagocytosis

Indexed keywords


EID: 0040039872     PISSN: 09442006     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Review
Times cited : (31)

References (150)
  • 1
    • 0001730096 scopus 로고
    • Immunolocalization of prophenoloxidase among hemocytes of the silkworm, Bombyx mori
    • Ashida M, Ochiai M, Niki T (1988) Immunolocalization of prophenoloxidase among hemocytes of the silkworm, Bombyx mori. Tissue Cell 20: 599-610
    • (1988) Tissue Cell , vol.20 , pp. 599-610
    • Ashida, M.1    Ochiai, M.2    Niki, T.3
  • 2
    • 0000623354 scopus 로고
    • Octopamine and 5-hydroxytryptamine enhance the phagocytic and nodule formation activities of cockroach (Periplaneta americana) haemocytes
    • Baines D, DeSantis T, Downer RGH (1992) Octopamine and 5-hydroxytryptamine enhance the phagocytic and nodule formation activities of cockroach (Periplaneta americana) haemocytes. J Insect Physiol 38: 905-914
    • (1992) J Insect Physiol , vol.38 , pp. 905-914
    • Baines, D.1    DeSantis, T.2    Downer, R.G.H.3
  • 3
    • 15844393328 scopus 로고    scopus 로고
    • Characterization of a defense complex consisting of interleukin 1 and phenol oxidase from the hemolymph of the tobacco horn-worm, Manduca sexta
    • Beck G, Cardinale S, Wang L et al. (1996) Characterization of a defense complex consisting of interleukin 1 and phenol oxidase from the hemolymph of the tobacco horn-worm, Manduca sexta. J Biol Chem 271: 11035-11038
    • (1996) J Biol Chem , vol.271 , pp. 11035-11038
    • Beck, G.1    Cardinale, S.2    Wang, L.3
  • 4
    • 84930046886 scopus 로고    scopus 로고
    • Die geheimwaffe der Schlupfwespen
    • Beckage NE (1998) Die Geheimwaffe der Schlupfwespen. Spektrum der Wissenschaft 2: 78-85
    • (1998) Spektrum der Wissenschaft , vol.2 , pp. 78-85
    • Beckage, N.E.1
  • 5
    • 84930042392 scopus 로고    scopus 로고
    • Veränderung des Hämozytenbildes von Manduca sexta im Verlauf der Metamorphose
    • Beetz S, Trenczek T (1998) Veränderung des Hämozytenbildes von Manduca sexta im Verlauf der Metamorphose. Verh Dtsch Zool Ges 91: 19
    • (1998) Verh Dtsch Zool Ges , vol.91 , pp. 19
    • Beetz, S.1    Trenczek, T.2
  • 6
    • 0029730738 scopus 로고    scopus 로고
    • A conserved signalling pathway: The Drosophila Toll-dorsal pathway
    • Belvin MP, Andersson KV (1996) A conserved signalling pathway: The Drosophila Toll-dorsal pathway. Annu Rev Cell Dev Biol 12: 393-416
    • (1996) Annu Rev Cell Dev Biol , vol.12 , pp. 393-416
    • Belvin, M.P.1    Andersson, K.V.2
  • 7
    • 0029971979 scopus 로고    scopus 로고
    • Peptide antibiotics: Holy or heretic grails of innate immunity?
    • Boman HG (1996) Peptide antibiotics: Holy or heretic grails of innate immunity? Scand J Immunol 43: 475-482
    • (1996) Scand J Immunol , vol.43 , pp. 475-482
    • Boman, H.G.1
  • 8
    • 0040405541 scopus 로고
    • The fungal cell wall and its involvement in the pathogenic process in insect hosts
    • Latgé JP, Boucias DG (eds) Springer, Berlin Heidelberg
    • Boucias DG, Pendland JC (1991) The fungal cell wall and its involvement in the pathogenic process in insect hosts. In: Latgé JP, Boucias DG (eds) Fungal Cell Wall and Immune Response, 303-315, Springer, Berlin Heidelberg
    • (1991) Fungal Cell Wall and Immune Response , vol.303-315
    • Boucias, D.G.1    Pendland, J.C.2
  • 9
    • 0018172653 scopus 로고
    • A comparative ultrastructural study of blood cells from nine insect orders
    • Brehélin M, Zachary D, Hoffmann JA (1978) A comparative ultrastructural study of blood cells from nine insect orders. Cell Tissue Res 195: 45-57
    • (1978) Cell Tissue Res , vol.195 , pp. 45-57
    • Brehélin, M.1    Zachary, D.2    Hoffmann, J.A.3
  • 10
    • 0027311062 scopus 로고
    • Role of the integument in insect immunity: Epicuticular abrasion and induction of cecropin synthesis in cuticular epithelial cells
    • Brey PT, Lee W-J, Yamakawa M, Koizumi Y, Perrot S, François M, Ashida M (1993) Role of the integument in insect immunity: Epicuticular abrasion and induction of cecropin synthesis in cuticular epithelial cells. Proc Natl Acad Sci USA 90: 6275-6279
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 6275-6279
    • Brey, P.T.1    Lee, W.-J.2    Yamakawa, M.3    Koizumi, Y.4    Perrot, S.5    François, M.6    Ashida, M.7
  • 11
    • 0040523920 scopus 로고    scopus 로고
    • COST publication, Pathogenicity of Entomopathogenic Nematodes Versus Insect Defense Mechanisms: Impact on Selection of Virulent Strains, Ponta Delgada, Portugal
    • Bulet P, Hoffmann D, Hetru D (1996) Antimicrobial Peptides/Polypeptides from Insects: Biochemical Aspects. COST publication, Pathogenicity of Entomopathogenic Nematodes Versus Insect Defense Mechanisms: Impact on Selection of Virulent Strains, Ponta Delgada, Portugal
    • (1996) Antimicrobial Peptides/polypeptides from Insects: Biochemical Aspects
    • Bulet, P.1    Hoffmann, D.2    Hetru, D.3
  • 12
    • 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 ET, Bennich H (1991) Attacin, an antibacterial protein from Hyalophora cecropia, inhibits synthesis of outer membrane proteins in Escherichia coli by interfering with omp gene transcription. Infect Immun 59: 3040-3045
    • (1991) Infect Immun , vol.59 , pp. 3040-3045
    • Carlsson, A.1    Engström, P.2    Palva, E.T.3    Bennich, H.4
  • 13
    • 0029012670 scopus 로고
    • Lipopolysaccharide-stimulated exocytosis of non-self recognition protein from insect hemocytes depend on protein tyrosine phosphorylation
    • Charalambidis ND, Zervas CG, Lambropoulou M, Katsoris G, Marmaras VJ (1995) Lipopolysaccharide-stimulated exocytosis of non-self recognition protein from insect hemocytes depend on protein tyrosine phosphorylation. Eur J Cell Biol 67: 32-41
    • (1995) Eur J Cell Biol , vol.67 , pp. 32-41
    • Charalambidis, N.D.1    Zervas, C.G.2    Lambropoulou, M.3    Katsoris, G.4    Marmaras, V.J.5
  • 14
    • 84940910643 scopus 로고
    • Biochemical and molecular basis of mosquito susceptibility to plasmodium and filaroid nematodes
    • Beckage NE, Thompson SN, Federici BA (eds), Acad Press, San Diego
    • Christensen BM, Severson DW (1993) Biochemical and molecular basis of mosquito susceptibility to Plasmodium and filaroid nematodes. In: Beckage NE, Thompson SN, Federici BA (eds), Parasites and Pathogens of Insects, 245-266, Acad Press, San Diego
    • (1993) Parasites and Pathogens of Insects , vol.245-266
    • Christensen, B.M.1    Severson, D.W.2
  • 15
    • 0030760062 scopus 로고    scopus 로고
    • Isolation and identification of a plasmatocyte-spreading peptide from the hemolymph of the lepidopteran insect Pseudoplusia includens
    • Clark KD, Pech LL, Strand MR (1997) Isolation and identification of a plasmatocyte-spreading peptide from the hemolymph of the lepidopteran insect Pseudoplusia includens. J Biol Chem 272: 23440-23447
    • (1997) J Biol Chem , vol.272 , pp. 23440-23447
    • Clark, K.D.1    Pech, L.L.2    Strand, M.R.3
  • 16
    • 0027249384 scopus 로고
    • Insect defensins, an inducible antibacterial peptide, forms voltage-dependant channels in Micrococcus luteus
    • Cociancich S, Ghazi A, Hetru C, Hoffmann JA, Letellier L (1993) Insect defensins, an inducible antibacterial peptide, forms voltage-dependant 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    Hetru, C.3    Hoffmann, J.A.4    Letellier, L.5
  • 17
    • 0028304808 scopus 로고
    • Novel inducible antibacterial peptides from a hemipteran insect, the sap-sucking bug Pyrrhocoris apterus
    • Cociancich S, Dupont A, Hegy G, Lanot R, Holder F, Hetru C, Hoffmann JA, 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    Hetru, C.6    Hoffmann, J.A.7    Bulet, P.8
  • 18
    • 0000527403 scopus 로고
    • Lipophorin inhibits the adhesion of cockroach (Periplaneta americana) haemocytes in vitro
    • Coodin S, Caveney S (1992) Lipophorin inhibits the adhesion of cockroach (Periplaneta americana) haemocytes in vitro. J Insect Physiol 38: 853-862
    • (1992) J Insect Physiol , vol.38 , pp. 853-862
    • Coodin, S.1    Caveney, S.2
  • 19
    • 0031009383 scopus 로고    scopus 로고
    • Lipopolysaccharide interaction with hemolin, an insect member of the Ig-superfamily
    • Daffre S, Faye I (1997) Lipopolysaccharide interaction with hemolin, an insect member of the Ig-superfamily. FEBS Lett 408: 127-130
    • (1997) FEBS Lett , vol.408 , pp. 127-130
    • Daffre, S.1    Faye, I.2
  • 20
    • 0000946914 scopus 로고
    • Molecular mimicry: Antigen sharing by a parasite and host and its consequences
    • Damian RT (1964) Molecular mimicry: Antigen sharing by a parasite and host and its consequences. Am Nat 98: 129-149
    • (1964) Am Nat , vol.98 , pp. 129-149
    • Damian, R.T.1
  • 21
    • 0001103441 scopus 로고
    • Passive evasion by eggs of braconid parasitoid Cardiochiles nigriceps of encapsulation in vitro by haemocytes of host Heliothis viriscens. Possible role for fibrous layer in immunity
    • Davies DH, Vinson SB (1986) Passive evasion by eggs of braconid parasitoid Cardiochiles nigriceps of encapsulation in vitro by haemocytes of host Heliothis viriscens. Possible role for fibrous layer in immunity. J Insect Physiol 32: 1003-1010
    • (1986) J Insect Physiol , vol.32 , pp. 1003-1010
    • Davies, D.H.1    Vinson, S.B.2
  • 22
    • 0024297452 scopus 로고
    • A family of bacteria-regulated, cecropin D-like peptides from Manduca sexta
    • Dickinson L, Russell V (1988) A family of bacteria-regulated, cecropin D-like peptides from Manduca sexta. J Biol Chem 263: 19424-19429
    • (1988) J Biol Chem , vol.263 , pp. 19424-19429
    • Dickinson, L.1    Russell, V.2
  • 24
    • 0030867913 scopus 로고    scopus 로고
    • Molecular immune responses of the mosquito Anopheles gambiae to bacteria and malaria parasites
    • Dimopoulos G, Richman A, Müller H-M, Kafatos F (1997) Molecular immune responses of the mosquito Anopheles gambiae to bacteria and malaria parasites. Proc Natl Acad Sci USA 94: 11508-11513
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 11508-11513
    • Dimopoulos, G.1    Richman, A.2    Müller, H.-M.3    Kafatos, F.4
  • 25
    • 0021866578 scopus 로고
    • Soluble peptidoglycan fragments stimulate antibacterial protein synthesis by fat body from larvae of Manduca sexta
    • Dunn PE, Dai W, Kanost MR, Geng C (1985) Soluble peptidoglycan fragments stimulate antibacterial protein synthesis by fat body from larvae of Manduca sexta. Dev Comp Immunol 9: 559-568
    • (1985) Dev Comp Immunol , vol.9 , pp. 559-568
    • Dunn, P.E.1    Dai, W.2    Kanost, M.R.3    Geng, C.4
  • 26
    • 0008971194 scopus 로고
    • Insect antibacterial proteins
    • Warr GW, Cohen N (eds), CRC Press
    • Dunn PE (1991) Insect antibacterial proteins. In: Warr GW, Cohen N (eds), Phylogeny of Immune Functions 19-44. CRC Press
    • (1991) Phylogeny of Immune Functions , vol.19-44
    • Dunn, P.E.1
  • 27
    • 0027947846 scopus 로고
    • Octopamine, a modulator of the haemocytic nodulation response of non-immune Galleria mellonella larvae
    • Dunphy GB, Downer RGH (1994) Octopamine, a modulator of the haemocytic nodulation response of non-immune Galleria mellonella larvae. J Insect Physiol 40: 267-272
    • (1994) J Insect Physiol , vol.40 , pp. 267-272
    • Dunphy, G.B.1    Downer, R.G.H.2
  • 28
    • 0031252949 scopus 로고    scopus 로고
    • Haemolymph proteins of larvae of Galleria mellonella detoxify endotoxins of the insect pathogenic bacteria Xenorhabdus nematophilus (Enterobacteriaceae)
    • Dunphy G, Halwani A (1997) Haemolymph proteins of larvae of Galleria mellonella detoxify endotoxins of the insect pathogenic bacteria Xenorhabdus nematophilus (Enterobacteriaceae). J Insect Physiol 43: 1023-1029
    • (1997) J Insect Physiol , vol.43 , pp. 1023-1029
    • Dunphy, G.1    Halwani, A.2
  • 29
    • 0003150156 scopus 로고
    • The insect immune proteins and the regulation of their genes
    • Beckage NE, Thompson SN, Frederici BA (eds), Acad. Press, San Diego
    • Faye I, Hultmark D (1993) The insect immune proteins and the regulation of their genes. In: Beckage NE, Thompson SN, Frederici BA (eds), Parasites and Pathogens of Insects, 25-54, Acad. Press, San Diego
    • (1993) Parasites and Pathogens of Insects , vol.25-54
    • Faye, I.1    Hultmark, D.2
  • 30
    • 0002749058 scopus 로고    scopus 로고
    • Function and regulation of hemolin
    • Brey PT, Hultmark D (eds), Chapman & Hall, London
    • Faye I, Kanost M (1997) Function and regulation of hemolin. In: Brey PT, Hultmark D (eds), Molecular Mechanisms of Immune Responses in Insects, 173-188, Chapman & Hall, London
    • (1997) Molecular Mechanisms of Immune Responses in Insects , vol.173-188
    • Faye, I.1    Kanost, M.2
  • 31
    • 0030831201 scopus 로고    scopus 로고
    • Seeking wisdom in innate immunity
    • Fearon DT (1997) Seeking wisdom in innate immunity. Nature 388: 323-324
    • (1997) Nature , vol.388 , pp. 323-324
    • Fearon, D.T.1
  • 32
    • 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
    • Fehlbaum P, Bulet P, Chernysh S, Briand J-P, Roussel J-P et al (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
  • 33
    • 0028587829 scopus 로고
    • Insect immunity. Septic injury of drosophila induces the synthesis of a potent antifungal peptide with sequence homology to antifungal peptides
    • Fehlbaum P, Bulet P, Michaut L, Lagueux M, Broekaert WF et al (1994) Insect Immunity. Septic injury of Drosophila induces the synthesis of a potent antifungal peptide with sequence homology to 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
  • 35
    • 0031057840 scopus 로고    scopus 로고
    • The plasma protein scolexin from Manduca sexta is induced by baculovirus infection and other immune challenges
    • Finnerty CM, Granados RR (1997) The plasma protein scolexin from Manduca sexta is induced by baculovirus infection and other immune challenges. Insect Biochem Molec Biol 27: 1-7
    • (1997) Insect Biochem Molec Biol , vol.27 , pp. 1-7
    • Finnerty, C.M.1    Granados, R.R.2
  • 36
    • 0030152160 scopus 로고    scopus 로고
    • Croquemort, a novel Drosophila hemocyte/macrophage receptor that recognizes apoptotic cells
    • Franc NC, Dimarcg J-L, Lagueux M, Hoffmann JA, Ezekowitz RAB (1996) Croquemort, a novel Drosophila hemocyte/macrophage receptor that recognizes apoptotic cells. Immunity 4: 431-443
    • (1996) Immunity , vol.4 , pp. 431-443
    • Franc, N.C.1    Dimarcg, J.-L.2    Lagueux, M.3    Hoffmann, J.A.4    Ezekowitz, R.A.B.5
  • 37
    • 0029823028 scopus 로고    scopus 로고
    • Induction of ACTH-and TNF-α-like molecules in the hemocytes of Calliphora vomitoria (Insecta, Diptera)
    • Franchini A, Miyan JA, Ottaviani E (1996) Induction of ACTH-and TNF-α-like molecules in the hemocytes of Calliphora vomitoria (Insecta, Diptera). Tissue Cell 28: 587-592
    • (1996) Tissue Cell , vol.28 , pp. 587-592
    • Franchini, A.1    Miyan, J.A.2    Ottaviani, E.3
  • 38
    • 23544476373 scopus 로고    scopus 로고
    • Haematopoetic disorders in invertebrates
    • Söderhäll K, Iwanaga S, Vasta G (eds), SOS Publication, New Haven
    • Gateff E (1996) Haematopoetic disorders in invertebrates. In: Söderhäll K, Iwanaga S, Vasta G (eds), New Directions in Invertebrate Immunology, 1-22, SOS Publication, New Haven
    • (1996) New Directions in Invertebrate Immunology , vol.1-22
    • Gateff, E.1
  • 40
    • 84968985856 scopus 로고
    • On the existence of immunity principles in insects
    • Glaser RW (1918) On the existence of immunity principles in insects. Psyche (Camb) 25: 39-46
    • (1918) Psyche (Camb) , vol.25 , pp. 39-46
    • Glaser, R.W.1
  • 41
    • 0030904372 scopus 로고    scopus 로고
    • The effects of protease inhibitors and sugars on the survival and development of the parasite Onchocerca ochengi in its natural intermediate host Simulium damnosums.l
    • Hagen HE, Kläger SL, Barrault DV, Ham PJ (1997a) The effects of protease inhibitors and sugars on the survival and development of the parasite Onchocerca ochengi in its natural intermediate host Simulium damnosums.l. Trop Med Int Health 2: 211-217
    • (1997) Trop Med Int Health , vol.2 , pp. 211-217
    • Hagen, H.E.1    Kläger, S.L.2    Barrault, D.V.3    Ham, P.J.4
  • 42
    • 0029558817 scopus 로고
    • Simulium damnosum s.l.: Identification of inducible serine proteases following an Onchocerca infection by differential display reverse transcription PCR
    • Hagen HE, Kläger SL, Chan V, Sakanari JA, McKerrow JH, Ham PJ (1995) Simulium damnosum s.l.: Identification of inducible serine proteases following an Onchocerca infection by differential display reverse transcription PCR. Exp Parasitol 81: 249-254
    • (1995) Exp Parasitol , vol.81 , pp. 249-254
    • Hagen, H.E.1    Kläger, S.L.2    Chan, V.3    Sakanari, J.A.4    McKerrow, J.H.5    Ham, P.J.6
  • 43
    • 0031194184 scopus 로고    scopus 로고
    • Simulium damnosum s.l.: Isolation and identification of prophenoloxidase following an infection with Onchocerca spp. Using targeted differential display
    • Hagen HE, Kläger SL, McKerrow JH, Ham PJ (1997b) Simulium damnosum s.l.: Isolation and identification of prophenoloxidase following an infection with Onchocerca spp. using targeted differential display. Exp Parasitol 86: 213-218
    • (1997) Exp Parasitol , vol.86 , pp. 213-218
    • Hagen, H.E.1    Kläger, S.L.2    McKerrow, J.H.3    Ham, P.J.4
  • 44
    • 0028938065 scopus 로고
    • Innate immunity of insects
    • Hoffmann JA (1995) Innate immunity of insects. Curr Opin Immunol 7: 4-10
    • (1995) Curr Opin Immunol , vol.7 , pp. 4-10
    • Hoffmann, J.A.1
  • 45
    • 0027318549 scopus 로고
    • Immune reactions in Drosophila and other insects: A model for innate immunity
    • Hultmark D (1993) Immune reactions in Drosophila and other insects: A model for innate immunity. Trends Genet 9: 178-183
    • (1993) Trends Genet , vol.9 , pp. 178-183
    • Hultmark, D.1
  • 46
    • 0028771840 scopus 로고
    • Ancient relationships
    • Hultmark D (1994) Ancient relationships. Nature 367: 116-117
    • (1994) Nature , vol.367 , pp. 116-117
    • Hultmark, D.1
  • 47
    • 0020686109 scopus 로고
    • Insect immunity: Attacins, a family of antibacterial proteins from Hyalophora cecropia
    • Hultmark D, Engström A, Andersson K, Steiner H, Bennich H, Boman HG (1983) Insect Immunity: Attacins, a family of antibacterial proteins from Hyalophora cecropia. EMBO J 2: 571-576
    • (1983) EMBO J , vol.2 , pp. 571-576
    • Hultmark, D.1    Engström, A.2    Andersson, K.3    Steiner, H.4    Bennich, H.5    Boman, H.G.6
  • 48
    • 0020366780 scopus 로고
    • Insect immunity: Isolation and structure of cecropin D and four minor antibacterial components from Cecropia pupae
    • Hultmark D, Kapur R, Boman HG, Engström A, Bennich H (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    Kapur, R.2    Boman, H.G.3    Engström, A.4    Bennich, H.5
  • 49
    • 84990431264 scopus 로고
    • An LPS-binding hemagglutinin in the midgut of Triatoma infestans: Partial characterization and tissue location
    • Hypsa V, Grubhoffer L (1995) An LPS-binding hemagglutinin in the midgut of Triatoma infestans: Partial characterization and tissue location. Arch Insect Biochem Physiol 28: 247-255
    • (1995) Arch Insect Biochem Physiol , vol.28 , pp. 247-255
    • Hypsa, V.1    Grubhoffer, L.2
  • 50
    • 0026791975 scopus 로고
    • The immune system evolved to discriminate infectious nonself from non-infectious self
    • Janeway CA, jr (1992) The immune system evolved to discriminate infectious nonself from non-infectious self. Immunol Today 13: 11-16
    • (1992) Immunol Today , vol.13 , pp. 11-16
    • Janeway C.A., Jr.1
  • 51
    • 0025295937 scopus 로고
    • Purification and characterization of lipopolysacharide-binding protein from hemolymph of American cockroach Periplaneta americana
    • Jomori T, Kubo T, Natori S (1990) Purification and characterization of lipopolysacharide-binding protein from hemolymph of American cockroach Periplaneta americana. Eur J Biochem 190: 201-206
    • (1990) Eur J Biochem , vol.190 , pp. 201-206
    • Jomori, T.1    Kubo, T.2    Natori, S.3
  • 52
    • 0025784020 scopus 로고
    • Molecular cloning of cDNA for lipopolysaccharide-binding protein from the hemolymph of the American cockroach, Periplaneta americana. Similarity of the protein with animal lectins and its acute phase expression
    • Jomori T, Natori S (1991) Molecular cloning of cDNA for lipopolysaccharide-binding protein from the hemolymph of the American cockroach, Periplaneta americana. Similarity of the protein with animal lectins and its acute phase expression. J Biol Chem 266: 13318-13323
    • (1991) J Biol Chem , vol.266 , pp. 13318-13323
    • Jomori, T.1    Natori, S.2
  • 53
    • 0028249835 scopus 로고
    • Isolation and characterization of a hemocyte aggregation inhibitor from hemolymph of Manduca sexta larvae
    • Kanost MR, Zepp MK, Ladendorff NE, Andersson LA (1994) Isolation and characterization of a hemocyte aggregation inhibitor from hemolymph of Manduca sexta larvae. Arch Insect Biochem Physiol 27: 123-136
    • (1994) Arch Insect Biochem Physiol , vol.27 , pp. 123-136
    • Kanost, M.R.1    Zepp, M.K.2    Ladendorff, N.E.3    Andersson, L.A.4
  • 54
    • 0002779670 scopus 로고    scopus 로고
    • Proteinase inhibitors in invertebrate immunity
    • Söderhäll K, Iwanaga S, Vasta G (eds), SOS Publication, New Haven
    • Kanost MR, Jiang H (1996) Proteinase inhibitors in invertebrate immunity. In: Söderhäll K, Iwanaga S, Vasta G (eds), New Directions in Invertebrate Immunology, 155-174, SOS Publication, New Haven
    • (1996) New Directions in Invertebrate Immunology , vol.155-174
    • Kanost, M.R.1    Jiang, H.2
  • 55
    • 0028448281 scopus 로고
    • Lipopolysaccharide-lipophorin complex formation in insect hemolymph: A common pathway of lipopolysaccharide detoxification both in insects and in mammals
    • Kato Y, Motoi Y, Tanai K, Kadono-OkudaK, Hiramatsu M, Yamakawa M (1994) Lipopolysaccharide-lipophorin complex formation in insect hemolymph: A common pathway of lipopolysaccharide detoxification both in insects and in mammals. Insect Biochem Mol Biol 24: 547-555
    • (1994) Insect Biochem Mol Biol , vol.24 , pp. 547-555
    • Kato, Y.1    Motoi, Y.2    Tanai, K.3    Hiramatsu, M.4    Yamakawa, M.5
  • 56
    • 0028915696 scopus 로고
    • A serin protease zymogen in insect plasma. Purification and activation by microbial cell wall components
    • Katsumi Y, Kihara H, Ochiai M, Ashida M (1995) A serin protease zymogen in insect plasma. Purification and activation by microbial cell wall components. Eur J Biochem 228: 870-877
    • (1995) Eur J Biochem , vol.228 , pp. 870-877
    • Katsumi, Y.1    Kihara, H.2    Ochiai, M.3    Ashida, M.4
  • 57
    • 0027520138 scopus 로고
    • A novel role of periplaneta lectin as an opsonin to recognize 2-keto-3-deoxy-octonate residues of bacterial lipopolysaccharides
    • Kawasaki K, Kubo T, Natori S (1993) A novel role of Periplaneta lectin as an opsonin to recognize 2-keto-3-deoxy-octonate residues of bacterial lipopolysaccharides. Comp Biochem Physiol B 106: 675-680
    • (1993) Comp Biochem Physiol B , vol.106 , pp. 675-680
    • Kawasaki, K.1    Kubo, T.2    Natori, S.3
  • 59
    • 0039338871 scopus 로고
    • Presentation and characterization of a possible binding factor for LPS of E.coli in hemocytes
    • Klünner T, Preik-Steinhoff H, Trenczek T (1994) Presentation and characterization of a possible binding factor for LPS of E.coli in hemocytes. Verh Dtsch Zool Ges 87: 284
    • (1994) Verh Dtsch Zool Ges , vol.87 , pp. 284
    • Klünner, T.1    Preik-Steinhoff, H.2    Trenczek, T.3
  • 60
    • 0029134161 scopus 로고
    • Purification of a 200 kDa protein-binding protein from the fat body of Sarcophaga peregrina larvae
    • Kobayashi H, Kurata S, Natori S (1995) Purification of a 200 kDa protein-binding protein from the fat body of Sarcophaga peregrina larvae. Insect Biochem Mol Biol 25: 393-399
    • (1995) Insect Biochem Mol Biol , vol.25 , pp. 393-399
    • Kobayashi, H.1    Kurata, S.2    Natori, S.3
  • 62
    • 0025730806 scopus 로고
    • Participation of a 200-kda hemocyte membrane protein in the dissociation of the fat body at the metamorphosis of Sarcophaga
    • Kurata S, Kobayashi H, Natori S (1991) Participation of a 200-kDa hemocyte membrane protein in the dissociation of the fat body at the metamorphosis of Sarcophaga. Dev Biol 146: 179-185
    • (1991) Dev Biol , vol.146 , pp. 179-185
    • Kurata, S.1    Kobayashi, H.2    Natori, S.3
  • 63
    • 0026663222 scopus 로고
    • The 29-kDa hemocyte proteinase dissociates fat body at metamorphosis of Sarcophaga
    • Kurata S, Saito H, Natori S (1992) The 29-kDa hemocyte proteinase dissociates fat body at metamorphosis of Sarcophaga. Dev Biol 153: 115-121
    • (1992) Dev Biol , vol.153 , pp. 115-121
    • Kurata, S.1    Saito, H.2    Natori, S.3
  • 64
    • 0026524571 scopus 로고
    • The lysozyme locus in Drosophila melanogaster: Different genes are expressed in the midgut and salivary glands
    • Kylsten P, Kimbrell DA, Daffre S, Samakovlis C, Hultmark D (1992) The lysozyme locus in Drosophila melanogaster: Different genes are expressed in the midgut and salivary glands. Mol Gen Genetics 232: 335-343
    • (1992) Mol Gen Genetics , vol.232 , pp. 335-343
    • Kylsten, P.1    Kimbrell, D.A.2    Daffre, S.3    Samakovlis, C.4    Hultmark, D.5
  • 65
    • 0027195193 scopus 로고
    • In vivo distribution of the immune protein scolexin in bacteria-injected Manduca sexta larvae
    • Kyriakides TR, McKillip JL, Spence KD (1993) In vivo distribution of the immune protein scolexin in bacteria-injected Manduca sexta larvae. Tissue Cell 25: 423-434
    • (1993) Tissue Cell , vol.25 , pp. 423-434
    • Kyriakides, T.R.1    McKillip, J.L.2    Spence, K.D.3
  • 66
    • 0029176961 scopus 로고
    • Biochemical characterization, developmental expression, and induction of the immune protein scolexin from Manduca sexta
    • Kyriakides TR, McKillip JL, Spence KD (1995) Biochemical characterization, developmental expression, and induction of the immune protein scolexin from Manduca sexta. Arch Insect Biochem Physiol 29: 269-280
    • (1995) Arch Insect Biochem Physiol , vol.29 , pp. 269-280
    • Kyriakides, T.R.1    McKillip, J.L.2    Spence, K.D.3
  • 67
    • 77956763045 scopus 로고
    • Haemocyte behaviour
    • Lackie AM (1988) Haemocyte behaviour. Adv Insect Physiol 21: 85-178
    • (1988) Adv Insect Physiol , vol.21 , pp. 85-178
    • Lackie, A.M.1
  • 68
    • 0025523371 scopus 로고
    • Isolation and characterization of bacteria-induced protein p4 from hemolymph of Manduca sexta
    • Laclendorff NE, Kanost MR (1990) Isolation and characterization of bacteria-induced protein p4 from hemolymph of Manduca sexta. Arch Insect Biochem Physiol 15: 33-41
    • (1990) Arch Insect Biochem Physiol , vol.15 , pp. 33-41
    • Laclendorff, N.E.1    Kanost, M.R.2
  • 69
    • 0040523889 scopus 로고    scopus 로고
    • The effect of hemolymph plasma on the hemocyte behaviour and its possible role in the initial immune response of insects
    • Firenze
    • Lanz H, Trenczek T (1996) The effect of hemolymph plasma on the hemocyte behaviour and its possible role in the initial immune response of insects. Int Congress of Entomology, Firenze, 224
    • (1996) Int Congress of Entomology , pp. 224
    • Lanz, H.1    Trenczek, T.2
  • 70
    • 0029939163 scopus 로고    scopus 로고
    • Regulation of the immune response: The effect of hemolin on the cellular immune mechanisms
    • Lanz-Mendoza H, Bettencourt R, Fabbri M, Faye I (1996) Regulation of the immune response: The effect of hemolin on the cellular immune mechanisms. Cell Immunol 168: 47-54
    • (1996) Cell Immunol , vol.168 , pp. 47-54
    • Lanz-Mendoza, H.1    Bettencourt, R.2    Fabbri, M.3    Faye, I.4
  • 71
    • 0029074918 scopus 로고
    • Polydnaviruses: Potent mediators of host insect immune dysfunction
    • Lavine MD, Beckage NE (1995) Polydnaviruses: Potent mediators of host insect immune dysfunction. Parasitol Today 11: 368-378
    • (1995) Parasitol Today , vol.11 , pp. 368-378
    • Lavine, M.D.1    Beckage, N.E.2
  • 72
    • 0029846206 scopus 로고    scopus 로고
    • Purification and molecular cloning of an inducible gram-negative bacteria-binding protein from the silkworm, Bombyx mori
    • Lee WJ, Lee JD, Kravchenko VV, Ulevitch RJ, Brey P (1996) Purification and molecular cloning of an inducible gram-negative bacteria-binding protein from the silkworm, Bombyx mori. Proc Natl Acad Sci USA 93: 7888-7893
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 7888-7893
    • Lee, W.J.1    Lee, J.D.2    Kravchenko, V.V.3    Ulevitch, R.J.4    Brey, P.5
  • 73
    • 0030845264 scopus 로고    scopus 로고
    • Midgut-specific immune molecules are produced by the blood-sucking insect Stomoxys calcitrans
    • Lehane MJ, Wu D, Lehane SM (1997) Midgut-specific immune molecules are produced by the blood-sucking insect Stomoxys calcitrans. Proc Natl Acad Sci USA 94: 11502-11507
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 11502-11507
    • Lehane, M.J.1    Wu, D.2    Lehane, S.M.3
  • 75
    • 0030595339 scopus 로고    scopus 로고
    • The dorsoventral regulatory gene cassette spätzle/Toll/cactus controls the potent antifungal response in Drosophila adults
    • Lemaitre B, Nicolas E, Michaut L, Reichhart J-M, Hoffmann JA (1996) The dorsoventral regulatory gene cassette spätzle/Toll/cactus controls the potent antifungal response in Drosophila adults. Cell 86: 973-883
    • (1996) Cell , vol.86 , pp. 973-1883
    • Lemaitre, B.1    Nicolas, E.2    Michaut, L.3    Reichhart, J.-M.4    Hoffmann, J.A.5
  • 76
    • 0031446642 scopus 로고    scopus 로고
    • Drosophila host defense: Differential induction of antimicrobial peptide genes after infection by various classes of microorganisms
    • Lemaitre B, Reichart JM, Hoffmann JA (1997) Drosophila host defense: Differential induction of antimicrobial peptide genes after infection by various classes of microorganisms. Proc Natl Acad Sci USA 94: 14614-14619
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 14614-14619
    • Lemaitre, B.1    Reichart, J.M.2    Hoffmann, J.A.3
  • 77
    • 0028884812 scopus 로고
    • Metchnikowin, a novel immune-inducible proline-rich peptide from Drosophila with antibacterial and antifugal properties
    • Levashina E, Ohresser S, Bulet P, Reichhart JM, Hetru C, Hoffmann JA (1995) Metchnikowin, a novel immune-inducible proline-rich peptide from Drosophila with antibacterial and antifugal properties. Eur J Biochem 233: 694-700
    • (1995) Eur J Biochem , vol.233 , pp. 694-700
    • Levashina, E.1    Ohresser, S.2    Bulet, P.3    Reichhart, J.M.4    Hetru, C.5    Hoffmann, J.A.6
  • 78
    • 0027631267 scopus 로고
    • Purification and primary structure of ceratotoxin A and B, two antibacterial peptides from the female reproductive accessory glands of the medfly Ceratitis capitata (Insecta: Diptera)
    • Marchini D, Giordano PC, Amons R, Bernini LF, Dallai R (1993) Purification and primary structure of ceratotoxin A and B, two antibacterial peptides from the female reproductive accessory glands of the medfly Ceratitis capitata (Insecta: Diptera). Insect Biochem Mol Biol 23: 591-598
    • (1993) Insect Biochem Mol Biol , vol.23 , pp. 591-598
    • Marchini, D.1    Giordano, P.C.2    Amons, R.3    Bernini, L.F.4    Dallai, R.5
  • 79
    • 84990462103 scopus 로고
    • Certain hemocyte proteins of the medfly, ceratitis capitata, are responsible for nonself recognition and immobilization of Escherichia coli in vitro
    • Marmaras VJ, Charalambidis ND (1992) Certain hemocyte proteins of the medfly, Ceratitis capitata, are responsible for nonself recognition and immobilization of Escherichia coli in vitro. Arch Insect Biochem Physiol 21: 281-288
    • (1992) Arch Insect Biochem Physiol , vol.21 , pp. 281-288
    • Marmaras, V.J.1    Charalambidis, N.D.2
  • 80
    • 0025252551 scopus 로고
    • Detection of β-1,3-glucan-specific lectin on the surface of plasmatocytes, immunocompetent cells of the great wax moth, Galleria mellonella L
    • Matha V, Grubhoffer L, Weyda F Hermanová L (1990) Detection of β-1,3-glucan-specific lectin on the surface of plasmatocytes, immunocompetent cells of the great wax moth, Galleria mellonella L. Cytobios 64: 35-42
    • (1990) Cytobios , vol.64 , pp. 35-42
    • Matha, V.1    Grubhoffer, L.2    Weyda, F.3    Hermanová, L.4
  • 81
    • 0026578564 scopus 로고
    • Functional studies on Calliphora vomitoria haemocytes subpopulation defined by lectin staining and density centrifugation
    • McKenzie ANJ, Preston TM (1992) Functional studies on Calliphora vomitoria haemocytes subpopulation defined by lectin staining and density centrifugation. Dev Comp Immunol 16: 19-30
    • (1992) Dev Comp Immunol , vol.16 , pp. 19-30
    • McKenzie, A.N.J.1    Preston, T.M.2
  • 82
    • 0030666222 scopus 로고    scopus 로고
    • Innate immunity: The virtues of a nonclonal system of recognition
    • Medzhitov R, Janeway CA, Jr. (1997) Innate immunity: The virtues of a nonclonal system of recognition. Cell 91: 295-298
    • (1997) Cell , vol.91 , pp. 295-298
    • Medzhitov, R.1    Janeway C.A., Jr.2
  • 83
    • 0031281940 scopus 로고    scopus 로고
    • Antimicrobial peptide defense in Drosophila
    • Meister M, Lemaitre B, Hoffmann JA (1997) Antimicrobial peptide defense in Drosophila. Bioessays 19: 1019-1026
    • (1997) Bioessays , vol.19 , pp. 1019-1026
    • Meister, M.1    Lemaitre, B.2    Hoffmann, J.A.3
  • 85
    • 0039338866 scopus 로고
    • Lysozym im humoralen Abwehrmechanismus spezifisch und unspezifisch immunisierter Insektenlarven
    • Mohrig W, Messner B (1967) Lysozym im humoralen Abwehrmechanismus spezifisch und unspezifisch immunisierter Insektenlarven. Biol Rundsch 5: 181-183
    • (1967) Biol Rundsch , vol.5 , pp. 181-183
    • Mohrig, W.1    Messner, B.2
  • 86
    • 0029587068 scopus 로고
    • Parallel induction of cecropin and lysozyme in larvae of the silkworm Bombyx mon
    • Morishima I, Horiba T, Iketani M, Nishioka E, Yamano Y (1995) Parallel induction of cecropin and lysozyme in larvae of the silkworm Bombyx mon. 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
  • 87
    • 0028385708 scopus 로고
    • Structure and induction of a lysozyme gene from the tobacco hornworm, Manduca sexta
    • Mulnix AB, Dünn PE (1994) Structure and induction of a lysozyme gene from the tobacco hornworm, Manduca sexta. Insect Biochem Mol Biol 24: 271-281
    • (1994) Insect Biochem Mol Biol , vol.24 , pp. 271-281
    • Mulnix, A.B.1    Dünn, P.E.2
  • 88
    • 0025601982 scopus 로고
    • Dual functions of insect immunity proteins in defence and development
    • Natori S (1990) Dual functions of insect immunity proteins in defence and development. Res Immunol 141: 938-939
    • (1990) Res Immunol , vol.141 , pp. 938-939
    • Natori, S.1
  • 89
    • 0002909243 scopus 로고    scopus 로고
    • Role of lectins in development and morphogenesis in insects
    • Söderhäll K, Iwanaga S, Vasta G (eds), SOS Publication, New Haven
    • Natori S, Kubo T (1996) Role of lectins in development and morphogenesis in insects. In: Söderhäll K, Iwanaga S, Vasta G (eds), New Directions in Invertebrate Immunology, 175-188, SOS Publication, New Haven
    • (1996) New Directions in Invertebrate Immunology , vol.175-188
    • Natori, S.1    Kubo, T.2
  • 91
    • 0024297132 scopus 로고
    • Purification of a β-1,3-glucan recognition protein in the prophenoloxidase activating system from hemolymph of the silkworm, Bombyx mori
    • Ochiai M, Ashida M (1988) Purification of a β-1,3-glucan recognition protein in the prophenoloxidase activating system from hemolymph of the silkworm, Bombyx mori. J Biol Chem 263: 12056-12062
    • (1988) J Biol Chem , vol.263 , pp. 12056-12062
    • Ochiai, M.1    Ashida, M.2
  • 93
    • 0029916999 scopus 로고    scopus 로고
    • Cavenger receptors in innate immunity
    • Pearson AM (1996) Cavenger receptors in innate immunity. Curr Opin Immunol 8: 20-28
    • (1996) Curr Opin Immunol , vol.8 , pp. 20-28
    • Pearson, A.M.1
  • 94
    • 0029038694 scopus 로고
    • Expression cloning of dSR-CI, a class C macrophage-specific scavenger receptor from Drosophila melanogaster
    • Pearson A, Lux A, Krieger M (1995) Expression cloning of dSR-CI, a class C macrophage-specific scavenger receptor from Drosophila melanogaster. Proc Natl Acad Sci USA 92: 4056-4060
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 4056-4060
    • Pearson, A.1    Lux, A.2    Krieger, M.3
  • 95
    • 0029107785 scopus 로고
    • Encapsulation of foreign targets by hemocytes of the moth Pseudoplusia includens (Lepidoptera: Noctuidae) involves an RGD-dependent cell adhesion mechanism
    • Pech LL, Strand MR (1995) Encapsulation of foreign targets by hemocytes of the moth Pseudoplusia includens (Lepidoptera: Noctuidae) involves an RGD-dependent cell adhesion mechanism. J Insect Physiol 41: 481-488
    • (1995) J Insect Physiol , vol.41 , pp. 481-488
    • Pech, L.L.1    Strand, M.R.2
  • 96
    • 0029833464 scopus 로고    scopus 로고
    • Granular cells are required for encapsulation of foreign targets by insect haemocytes
    • Pech LL, Strand MR (1996) Granular cells are required for encapsulation of foreign targets by insect haemocytes. J Cell Sci 109: 2053-2060
    • (1996) J Cell Sci , vol.109 , pp. 2053-2060
    • Pech, L.L.1    Strand, M.R.2
  • 97
    • 0030037179 scopus 로고    scopus 로고
    • Phagocytosis of lectin-opsonized fungal cells and endocytosis of the ligand by insect Spodoptera exigua granular hemocytes: An ultrastructural and immuncytochemical study
    • Pendland JC, Boucias DG (1996) Phagocytosis of lectin-opsonized fungal cells and endocytosis of the ligand by insect Spodoptera exigua granular hemocytes: An ultrastructural and immuncytochemical study. Cell Tissue Res 285: 57-67
    • (1996) Cell Tissue Res , vol.285 , pp. 57-67
    • Pendland, J.C.1    Boucias, D.G.2
  • 98
    • 0019363489 scopus 로고
    • Lectins of distinct specificity in Rhodnius prolixus interact selectively with Trypanosoma cruzi
    • Pereira MEA, Andrade AFB, Ribeiro JMC (1981) Lectins of distinct specificity in Rhodnius prolixus interact selectively with Trypanosoma cruzi. Science 211: 597-600
    • (1981) Science , vol.211 , pp. 597-600
    • Pereira, M.E.A.1    Andrade, A.F.B.2    Ribeiro, J.M.C.3
  • 99
    • 0017156997 scopus 로고
    • Studies on insect bacteriolytic enzymes - II. Some physical and enzymatic properties of lysozyme from haemolymph of Galleria mellonella
    • Powning RF, Davidson WJ (1976) Studies on insect bacteriolytic enzymes - II. Some physical and enzymatic properties of lysozyme from haemolymph of Galleria mellonella. Comp Biochem Physiol 55: 221-228
    • (1976) Comp Biochem Physiol , vol.55 , pp. 221-228
    • Powning, R.F.1    Davidson, W.J.2
  • 100
    • 0000336925 scopus 로고
    • Isolation of a 90 kDa protein from haemocytes of Blaberus craniifer which has similar functional and immunological properties to the 76 KDa protein from crayfish haemocytes
    • Rantamäki J, Durrant H, Liang Z, Ratcliffe NA, Duvic B, Söderhäll K (1991) Isolation of a 90 kDa protein from haemocytes of Blaberus craniifer which has similar functional and immunological properties to the 76 KDa protein from crayfish haemocytes. J Insect Physiol 37: 627-634
    • (1991) J Insect Physiol , vol.37 , pp. 627-634
    • Rantamäki, J.1    Durrant, H.2    Liang, Z.3    Ratcliffe, N.A.4    Duvic, B.5    Söderhäll, K.6
  • 101
    • 0040523883 scopus 로고
    • Encapsulation reactions in vitro by haemocytes of Heliothis virescens
    • Ratner S, Vinson SB (1983) Encapsulation reactions in vitro by haemocytes of Heliothis virescens. J Insect Physiol 29: 855-863
    • (1983) J Insect Physiol , vol.29 , pp. 855-863
    • Ratner, S.1    Vinson, S.B.2
  • 102
    • 0000826497 scopus 로고
    • The circulatory system and associated cells and tissues
    • Ashburner M, Wright TRF (eds), Acad. Press, London, New York, San Francisco
    • Rizki TM (1978) The circulatory system and associated cells and tissues. In: Ashburner M, Wright TRF (eds), The Genetics and Biology of Drosophila, 397-452, Acad. Press, London, New York, San Francisco
    • (1978) The Genetics and Biology of Drosophila , vol.397-452
    • Rizki, T.M.1
  • 103
    • 4243888615 scopus 로고
    • The cellular defense in Drosophila melanogaster
    • Akai H et al (eds), Soc Insect Cells, Japan
    • Rizki TM, Rizki RM (1982) The cellular defense in Drosophila melanogaster. In: Akai H et al (eds), The Ultrastructure and Functioning of Insect Cells, 173-176, Soc Insect Cells, Japan
    • (1982) The Ultrastructure and Functioning of Insect Cells , vol.173-176
    • Rizki, T.M.1    Rizki, R.M.2
  • 104
    • 0000409768 scopus 로고
    • The cellular defense in Drosophila melanogaster
    • King RC, Akai H (eds), Plenum Press, New York
    • Rizki TM, Rizki RM (1984) The cellular defense in Drosophila melanogaster. In: King RC, Akai H (eds), Insect Ultrastructure 579-602, Plenum Press, New York
    • (1984) Insect Ultrastructure , vol.579-602
    • Rizki, T.M.1    Rizki, R.M.2
  • 105
    • 0028312279 scopus 로고
    • A fluorescence assay demonstrating stimulation of phagocytosis by haemolymph molecules of Galleria mellonella
    • Rohloff LH, Wiesner A, Götz P (1994) A fluorescence assay demonstrating stimulation of phagocytosis by haemolymph molecules of Galleria mellonella. J Insect Physiol 40: 1045-1049
    • (1994) J Insect Physiol , vol.40 , pp. 1045-1049
    • Rohloff, L.H.1    Wiesner, A.2    Götz, P.3
  • 106
    • 0345646454 scopus 로고    scopus 로고
    • In vivo regulation of tissue-specific and LPS-inducible expression of the Drosophila cecropin genes
    • Roos E, Björklund G, Engström Y (1998) In vivo regulation of tissue-specific and LPS-inducible expression of the Drosophila cecropin genes. Insect Biochem Molec Biol 7: 51-62
    • (1998) Insect Biochem Molec Biol , vol.7 , pp. 51-62
    • Roos, E.1    Björklund, G.2    Engström, Y.3
  • 107
    • 0028922245 scopus 로고
    • Signals from the IL-1 receptors homolog, Toll, can activate an immune response in a Drosophila hemocyte cell line
    • Rosetto M, Engström Y, Baldari CT, Telford JL, Hultmark D (1995) Signals from the IL-1 receptors homolog, Toll, can activate an immune response in a Drosophila hemocyte cell line. Biochem Biophys Res Commun 209: 111-116
    • (1995) Biochem Biophys Res Commun , vol.209 , pp. 111-116
    • Rosetto, M.1    Engström, Y.2    Baldari, C.T.3    Telford, J.L.4    Hultmark, D.5
  • 108
    • 0000659424 scopus 로고
    • Insects
    • Ratcliffe NA, Rowley AF (eds), Acad Press, London New York
    • Rowley AF, Ratcliffe NA (1981) Insects. In: Ratcliffe NA, Rowley AF (eds), Invertebrate Blood Cells, 421-488, Acad Press, London New York
    • (1981) Invertebrate Blood Cells , vol.421-488
    • Rowley, A.F.1    Ratcliffe, N.A.2
  • 109
    • 0041005766 scopus 로고
    • Lysozyme in the pericardial complex of Manduca sexta
    • Russell VW, Dunn PE (1990) Lysozyme in the pericardial complex of Manduca sexta. Insect Biochem 20: 501-509
    • (1990) Insect Biochem , vol.20 , pp. 501-509
    • Russell, V.W.1    Dunn, P.E.2
  • 110
    • 0026308226 scopus 로고
    • Lysozyme in the midgut of Manduca sexta during metamorphosis
    • Russell VW, Dunn PE (1991) Lysozyme in the midgut of Manduca sexta during metamorphosis. Arch Insect Biochem Physiol 17: 67-80
    • (1991) Arch Insect Biochem Physiol , vol.17 , pp. 67-80
    • Russell, V.W.1    Dunn, P.E.2
  • 111
    • 0030057057 scopus 로고    scopus 로고
    • Insect immunity: Early events in the encapsulation process of parasitoid (Leptopilina boulardi) eggs in resistant and susceptible strains of Drosophila
    • Russo J, Dupas S, Frey F, Carton Y, Brehelin M (1996) Insect immunity: Early events in the encapsulation process of parasitoid (Leptopilina boulardi) eggs in resistant and susceptible strains of Drosophila. Parasitol 112: 135-142
    • (1996) Parasitol , vol.112 , pp. 135-142
    • Russo, J.1    Dupas, S.2    Frey, F.3    Carton, Y.4    Brehelin, M.5
  • 112
    • 0024600972 scopus 로고
    • Molecular cloning of complementary DNA for sarcocystain A and analysis of the expression of the sarcocystain A gene during development of Sarcophaga peregrina
    • Saito H, Suzuki T, Ueno K, Kubo T, Natori S (1989) Molecular cloning of complementary DNA for sarcocystain A and analysis of the expression of the sarcocystain A gene during development of Sarcophaga peregrina. Biochem 28: 1749-1755
    • (1989) Biochem , vol.28 , pp. 1749-1755
    • Saito, H.1    Suzuki, T.2    Ueno, K.3    Kubo, T.4    Natori, S.5
  • 113
    • 0025126215 scopus 로고
    • The immune response in Drosophila: Pattern of cecropin expression and biological activity
    • Samakovlis C, Kimbrell DA, Kylsten P, Engström Å, Hultmark D (1991) The immune response in Drosophila: Pattern of cecropin expression and biological activity. EMBO J 9: 2969-2976
    • (1991) EMBO J , vol.9 , pp. 2969-2976
    • Samakovlis, C.1    Kimbrell, D.A.2    Kylsten, P.3    Å, E.4    Hultmark, D.5
  • 114
    • 0025959246 scopus 로고
    • The andropin gene and its product, a male-specific antibacterial peptide in Drosophila melanogaster
    • Samakovlis C, Kylsten P, Kimbrell DA, Engström Y, Hultmark D (1991) The andropin gene and its product, a male-specific antibacterial peptide in Drosophila melanogaster. EMBO J 10: 163-169
    • (1991) EMBO J , vol.10 , pp. 163-169
    • Samakovlis, C.1    Kylsten, P.2    Kimbrell, D.A.3    Engström, Y.4    Hultmark, D.5
  • 115
    • 84990422041 scopus 로고
    • Viruslike particle proteins from a hymenopteran endoparasitoid are related to a protein component of the immune system in the lepidopteran host
    • Schmidt O, Andersson K, Will A, Schuchmann-Feddersen I (1990) Viruslike particle proteins from a hymenopteran endoparasitoid are related to a protein component of the immune system in the lepidopteran host. Arch Insect Biochem Physiol 13: 107-115
    • (1990) Arch Insect Biochem Physiol , vol.13 , pp. 107-115
    • Schmidt, O.1    Andersson, K.2    Will, A.3    Schuchmann-Feddersen, I.4
  • 116
    • 0001281441 scopus 로고
    • Immune defense and suppression in insects
    • Schmidt O, Theopold U (1991) Immune defense and suppression in insects. Bioessays 13: 343-346
    • (1991) Bioessays , vol.13 , pp. 343-346
    • Schmidt, O.1    Theopold, U.2
  • 117
    • 84985786412 scopus 로고
    • Ultrastructure and cytochemistry of the cell types in the larval hematopoetic organs and hemolymph of Drosophila melanogaster
    • Shrestha R, Gateff E (1982) Ultrastructure and cytochemistry of the cell types in the larval hematopoetic organs and hemolymph of Drosophila melanogaster. Dev Growth Differ 24: 65-82
    • (1982) Dev Growth Differ , vol.24 , pp. 65-82
    • Shrestha, R.1    Gateff, E.2
  • 118
    • 0002749939 scopus 로고    scopus 로고
    • The prophenoloxidase activating system in invertebrates
    • Söderhäll K, Iwanaga S, Vasta G (eds), SOS Publications, Fair Haven
    • Söderhäll K, Cerenius L, Johansson MW (1996) The prophenoloxidase activating system in invertebrates. In: Söderhäll K, Iwanaga S, Vasta G (eds), New Directions in Invertebrate Immunology 229-253. SOS Publications, Fair Haven
    • (1996) New Directions in Invertebrate Immunology , vol.229-253
    • Söderhäll, K.1    Cerenius, L.2    Johansson, M.W.3
  • 120
    • 0019386682 scopus 로고
    • Sequence and specificity of two antibacterial proteins involved in insect immunity
    • Steiner H, Hultmark D, Engström A, Bennich H, Boman HG (1981) Sequence and specificity of two antibacterial proteins involved in insect immunity. Nature 292: 246-248
    • (1981) Nature , vol.292 , pp. 246-248
    • Steiner, H.1    Hultmark, D.2    Engström, A.3    Bennich, H.4    Boman, H.G.5
  • 121
    • 0028110460 scopus 로고
    • Microplitis demolitor polydnavirus infects and expresses in specific morphotypes of Pseudoplusia includens haemocytes
    • Strand MR (1994) Microplitis demolitor polydnavirus infects and expresses in specific morphotypes of Pseudoplusia includens haemocytes. J Gen Virol 75: 3007-3020
    • (1994) J Gen Virol , vol.75 , pp. 3007-3020
    • Strand, M.R.1
  • 122
    • 0029110524 scopus 로고
    • Immunological basis for compatibility in parasitoid-host relationships
    • Strand MR, Pech LL (1995) Immunological basis for compatibility in parasitoid-host relationships. Annu Rev Entomol 40: 31-56
    • (1995) Annu Rev Entomol , vol.40 , pp. 31-56
    • Strand, M.R.1    Pech, L.L.2
  • 123
    • 0026669101 scopus 로고
    • Affinity purification and characterization of CIF, an insect immunoresponsive factor with NF-kappaB-like properties
    • Sun S-C, Faye I (1992) Affinity purification and characterization of CIF, an insect immunoresponsive factor with NF-kappaB-like properties. Comp Biochem Physiol B 103: 225-233
    • (1992) Comp Biochem Physiol B , vol.103 , pp. 225-233
    • Sun, S.-C.1    Faye, I.2
  • 124
    • 0025693237 scopus 로고
    • Hemolin: An insect-immune protein belonging to the immunoglobulin superfamily
    • Sun S-C, Lindström I, Boman HG, Faye I, Schmidt O (1990) Hemolin: An insect-immune protein belonging to the immunoglobulin superfamily. Science 250: 1729-1732
    • (1990) Science , vol.250 , pp. 1729-1732
    • Sun, S.-C.1    Lindström, I.2    Boman, H.G.3    Faye, I.4    Schmidt, O.5
  • 125
    • 0022432076 scopus 로고
    • Purification and characterization of an inhibitor of the cysteine protease from the hemolymph of Sarcophaga peregrina larvae
    • Suzuki T, Natori S (1985) Purification and characterization of an inhibitor of the cysteine protease from the hemolymph of Sarcophaga peregrina larvae. J Biol Chem 260: 5115-5120
    • (1985) J Biol Chem , vol.260 , pp. 5115-5120
    • Suzuki, T.1    Natori, S.2
  • 126
    • 0028365963 scopus 로고
    • Embryonic origin of hemocytes and their relationship to cell death in Drosophila
    • Tepass U, Fessler LI, Aziz A, Hartenstein V (1994) Embryonic origin of hemocytes and their relationship to cell death in Drosophila. Development 120: 1829-1837
    • (1994) Development , vol.120 , pp. 1829-1837
    • Tepass, U.1    Fessler, L.I.2    Aziz, A.3    Hartenstein, V.4
  • 127
    • 0028851344 scopus 로고
    • Calp A, a Drosphila Captain homology specifically expressed in the small set of nerves, midgut, and blood cells
    • Theopold U, Pinter M, DAffre S, Tryselius Y, Friedrich P, Nässel DR, Hultmark D (1995) Calp A, a Drosphila Captain homology specifically expressed in the small set of nerves, midgut, and blood cells. Mol Cell Biol 15: 824-834
    • (1995) Mol Cell Biol , vol.15 , pp. 824-834
    • Theopold, U.1    Pinter, M.2    Daffre, S.3    Tryselius, Y.4    Friedrich, P.5    Nässel, D.R.6    Hultmark, D.7
  • 129
    • 0031195062 scopus 로고    scopus 로고
    • Helix pomatia lectin and annexin V, two molecular probes for insect microparticles: Possible involvement in hemolymph coagulation
    • Theopold U, Schmidt O (1997) Helix pomatia lectin and annexin V, two molecular probes for insect microparticles: Possible involvement in hemolymph coagulation. J Insect Physiol 43: 667-674
    • (1997) J Insect Physiol , vol.43 , pp. 667-674
    • Theopold, U.1    Schmidt, O.2
  • 130
    • 84982040302 scopus 로고
    • Immunität bei Insekten?
    • Trenczek T (1992) Immunität bei Insekten? Biol uns Zeit 4: 212-217
    • (1992) Biol Uns Zeit , vol.4 , pp. 212-217
    • Trenczek, T.1
  • 131
    • 84930045722 scopus 로고
    • Antibacterial proteins synthesized by hemocytes of Hyalophora cecropia
    • Trenczek T, Bennich H (1988) Antibacterial proteins synthesized by hemocytes of Hyalophora cecropia. Sericologia, 28 (suppl): 16
    • (1988) Sericologia , vol.28 , Issue.SUPPL. , pp. 16
    • Trenczek, T.1    Bennich, H.2
  • 132
    • 84930045368 scopus 로고
    • The application of monoclonal antibodies to distinguish insect haemocyte types
    • Trenczek T, Bennich H (1991) The application of monoclonal antibodies to distinguish insect haemocyte types. Sericologica, 31 (suppl): 66
    • (1991) Sericologica , vol.31 , Issue.SUPPL. , pp. 66
    • Trenczek, T.1    Bennich, H.2
  • 133
    • 0000018838 scopus 로고
    • Synthesis of immune proteins in primary cultures of fat body from Hyalophora cecropia
    • Trenczek T, Faye I (1988) Synthesis of immune proteins in primary cultures of fat body from Hyalophora cecropia. Insect Biochem 18: 299-312
    • (1988) Insect Biochem , vol.18 , pp. 299-312
    • Trenczek, T.1    Faye, I.2
  • 135
    • 84930047009 scopus 로고
    • Vergleich der "immunproteine" zweier Lepidopterenarten (Hyalophora cecropia, Galleria mellonella) durch Western-Blot-Analysen
    • Trenczek T, Wiesner A (1993) Vergleich der "Immunproteine" zweier Lepidopterenarten (Hyalophora cecropia, Galleria mellonella) durch Western-Blot-Analysen. Verh. Dtsch. Zool. Ges. 86: 195
    • (1993) Verh. Dtsch. Zool. Ges. , vol.86 , pp. 195
    • Trenczek, T.1    Wiesner, A.2
  • 136
    • 23544467383 scopus 로고    scopus 로고
    • Production of monoclonal antibodies to study insect hemocytes
    • Wiesner A et al. (eds), SOS Publication, Fair Haven. Techn Fish Immun -SOS Publications, Vol Insects (In Press)
    • Trenczek T, Willott E, Kanost MR (1998) Production of monoclonal antibodies to study insect hemocytes. In: Wiesner A et al. (eds), Techniques in Insect Immunology 21-33 SOS Publication, Fair Haven. Techn Fish Immun -SOS Publications, Vol Insects (In Press)
    • (1998) Techniques in Insect Immunology , vol.21-33
    • Trenczek, T.1    Willott, E.2    Kanost, M.R.3
  • 137
    • 0026541180 scopus 로고
    • CecC, a cecropin gene expressed during metamorphosis in Drosophila pupae
    • Tryselius Y, Samakovlis C, Kimbrell DA, Hultmark D. (1992) CecC, a cecropin gene expressed during metamorphosis in Drosophila pupae. Eur J Biochem 204: 395-399
    • (1992) Eur J Biochem , vol.204 , pp. 395-399
    • Tryselius, Y.1    Samakovlis, C.2    Kimbrell, D.A.3    Hultmark, D.4
  • 138
    • 0002851286 scopus 로고
    • On the cytochemistry of the hemocytes of Galleria mellonella with special reference to polyphenoloxidase
    • Vercauteren R, Aerts F (1958) On the cytochemistry of the hemocytes of Galleria mellonella with special reference to polyphenoloxidase. Enzymologia 20: 167-172
    • (1958) Enzymologia , vol.20 , pp. 167-172
    • Vercauteren, R.1    Aerts, F.2
  • 139
    • 0002139258 scopus 로고    scopus 로고
    • Antimycotic activity of lysozyme and its contribution to antifungal humoral defence reactions in Galleria mellonella
    • Vilcinskas A, Matha V (1997) Antimycotic activity of lysozyme and its contribution to antifungal humoral defence reactions in Galleria mellonella. Anim Biol 6: 19-29
    • (1997) Anim Biol , vol.6 , pp. 19-29
    • Vilcinskas, A.1    Matha, V.2
  • 141
    • 84990440625 scopus 로고
    • How parasitoids deal with the immune system of their host: An overview
    • Vinson SB (1990) How parasitoids deal with the immune system of their host: An overview. Arch Insect Biochem Physiol 13: 3-27
    • (1990) Arch Insect Biochem Physiol , vol.13 , pp. 3-27
    • Vinson, S.B.1
  • 142
    • 0003165327 scopus 로고    scopus 로고
    • Factors mediating short-and long-term immune suppression in a parasitized insect
    • Webb BA, Luckhart S (1996) Factors mediating short-and long-term immune suppression in a parasitized insect. J Insect Physiol 42: 33-40
    • (1996) J Insect Physiol , vol.42 , pp. 33-40
    • Webb, B.A.1    Luckhart, S.2
  • 143
    • 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 (1998) Purification and characterization of an inducible metalloprotease inhibitor from the hemolymph of greater wax moth larvae, Galleria mellonella. Eur J Biochem 255: 535-543
    • (1998) Eur J Biochem , vol.255 , pp. 535-543
    • Wedde, M.1    Weise, C.2    Kopacek, P.3    Franke, P.4    Vilcinskas, A.5
  • 144
    • 84930043121 scopus 로고    scopus 로고
    • Identification of a hemocyte protein involved in encapsulation of foreign material in the tobacco hornworm Manduca sexta
    • Wiegand C, Gillespie JP, Wang Y, Willott E, Trenczek T, Kanost MR (1996) Identification of a hemocyte protein involved in encapsulation of foreign material in the tobacco hornworm Manduca sexta. Int Congr Entomol, Firenze: 223
    • (1996) Int Congr Entomol, Firenze , pp. 223
    • Wiegand, C.1    Gillespie, J.P.2    Wang, Y.3    Willott, E.4    Trenczek, T.5    Kanost, M.R.6
  • 145
    • 0030231346 scopus 로고    scopus 로고
    • A small phagocytosis stimulating factor is released by and acts on phagocytosing Galleria mellonella haemocytes in vitro
    • Wiesner A, Wittwer D, Götz P (1996) A small phagocytosis stimulating factor is released by and acts on phagocytosing Galleria mellonella haemocytes in vitro. J Insect Physiol 42: 829-835
    • (1996) J Insect Physiol , vol.42 , pp. 829-835
    • Wiesner, A.1    Wittwer, D.2    Götz, P.3
  • 146
    • 0030663332 scopus 로고    scopus 로고
    • The 18-wheeler mutation reveals complex antibacterial gene regulation in drosophila host defense
    • Williams MJ, Rodriguez A, Kimbrell DA, Eldon ED (1997) The 18-wheeler mutation reveals complex antibacterial gene regulation in Drosophila host defense. EMBO J 16: 6120-6130
    • (1997) EMBO J , vol.16 , pp. 6120-6130
    • Williams, M.J.1    Rodriguez, A.2    Kimbrell, D.A.3    Eldon, E.D.4
  • 147
    • 0032485392 scopus 로고    scopus 로고
    • Regulated nuclear import of rel proteins in the Drosophila immune response
    • Wu LP, Anderson KV (1998) Regulated nuclear import of Rel proteins in the Drosophila immune response. Nature 392: 93-97
    • (1998) Nature , vol.392 , pp. 93-97
    • Wu, L.P.1    Anderson, K.V.2
  • 149
    • 85007850845 scopus 로고
    • Phagocytic activities of haemocytes separated by two simple methods from larvae of two lepidopteran species, Agrotis segetum and Galleria mellonella
    • Yokoo S, Götz P, Tojo S (1995) Phagocytic activities of haemocytes separated by two simple methods from larvae of two lepidopteran species, Agrotis segetum and Galleria mellonella. Appl Entomol Zool 30: 343-350
    • (1995) Appl Entomol Zool , vol.30 , pp. 343-350
    • Yokoo, S.1    Götz, P.2    Tojo, S.3
  • 150
    • 0029884417 scopus 로고    scopus 로고
    • Purification of a peptidoglycan recognition protein from hemolymph of the silkworm, Bombyx mori
    • Yoshida H, Kinoshita K, Ashida M (1996) Purification of a peptidoglycan recognition protein from hemolymph of the silkworm, Bombyx mori. J Biol Chem 271: 13854-13860
    • (1996) J Biol Chem , vol.271 , pp. 13854-13860
    • Yoshida, H.1    Kinoshita, K.2    Ashida, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.