메뉴 건너뛰기




Volumn 27, Issue 3, 2003, Pages 207-215

Identification of immunorelevant genes from greater wax moth (Galleria mellonella) by a subtractive hybridization approach

Author keywords

Galleria mellonella; Gloverin; Innate immunity; Lipopolysaccharide; Peptidoglycan recognition protein; Real time PCR; Subtractive hybridization; Toxin 2

Indexed keywords

BACTERIUM LIPOPOLYSACCHARIDE; COMPLEMENTARY DNA; DEFENSIN; GLOVERIN; PEPTIDOGLYCAN; PROTEIN; RNA BINDING PROTEIN; TOXIN; TOXIN 2; TRANSFERRIN; TYROSINE 3 MONOOXYGENASE; UNCLASSIFIED DRUG;

EID: 0037363719     PISSN: 0145305X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0145-305X(02)00097-6     Document Type: Article
Times cited : (97)

References (43)
  • 2
    • 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 H.G. Insect immunity. Attacins, a family of antibacterial proteins from Hyalophora cecropia. EMBO J. 2:(4):1983;571-576.
    • (1983) EMBO J , vol.2 , Issue.4 , pp. 571-576
    • Hultmark, D.1    Engström, A.2    Andersson, K.3    Steiner, H.4    Bennich, H.5    Boman, H.G.6
  • 3
    • 0025693237 scopus 로고
    • Hemolin: An insect-immune protein belonging to the immunoglobulin superfamily
    • Sun S.C., Lindström I., Boman H.G., Faye I., Schmidt O. Hemolin: an insect-immune protein belonging to the immunoglobulin superfamily. Science. 250:(4988):1990;1729-1732.
    • (1990) Science , vol.250 , Issue.4988 , pp. 1729-1732
    • Sun, S.C.1    Lindström, I.2    Boman, H.G.3    Faye, I.4    Schmidt, O.5
  • 4
    • 0028249835 scopus 로고
    • Isolation and characterization of a hemocyte aggregation inhibitor from hemolymph of Manduca sexta larvae
    • Kanost M.R., Zepp M.K., Ladendorff N.E., Andersson L.A. Isolation and characterization of a hemocyte aggregation inhibitor from hemolymph of Manduca sexta larvae. Arch Insect Biochem Physiol. 27:(2):1994;123-136.
    • (1994) Arch Insect Biochem Physiol , vol.27 , Issue.2 , pp. 123-136
    • Kanost, M.R.1    Zepp, M.K.2    Ladendorff, N.E.3    Andersson, L.A.4
  • 5
    • 0026556546 scopus 로고
    • Antibacterial activity inducible in the haemolymph of the silkworm, Bombyx mori, by injection of formalin-treated Escherichia coli K-12 during the fifth larval instar and pharate adult development
    • Sumida M., Ichimori H., Johchi S., Takaoka A., Yuhki T., Mori H., Matsubara F. Antibacterial activity inducible in the haemolymph of the silkworm, Bombyx mori, by injection of formalin-treated Escherichia coli K-12 during the fifth larval instar and pharate adult development. Comp Biochem Physiol B. 101:(1-2):1992;165-171.
    • (1992) Comp Biochem Physiol B , vol.101 , Issue.1-2 , pp. 165-171
    • Sumida, M.1    Ichimori, H.2    Johchi, S.3    Takaoka, A.4    Yuhki, T.5    Mori, H.6    Matsubara, F.7
  • 6
    • 0028349720 scopus 로고
    • Gallysin-1, an antibacterial protein isolated from hemolymph of Galleria mellonella
    • Phipps D.J., Chadwick J.S., Aston W.P. Gallysin-1, an antibacterial protein isolated from hemolymph of Galleria mellonella. Dev Comp Immunol. 18:(1):1994;13-23.
    • (1994) Dev Comp Immunol , vol.18 , Issue.1 , pp. 13-23
    • Phipps, D.J.1    Chadwick, J.S.2    Aston, W.P.3
  • 7
    • 0021201002 scopus 로고
    • The in vitro generation of an antibacterial activity from the fat body and hemolymph of non-immunized larvae of Galleria mellonella
    • De Verno P.J., Chadwick J.S., Aston W.P., Dunphy G.B. The in vitro generation of an antibacterial activity from the fat body and hemolymph of non-immunized larvae of Galleria mellonella. Dev Comp Immunol. 8:(3):1984;537-546.
    • (1984) Dev Comp Immunol , vol.8 , Issue.3 , pp. 537-546
    • De Verno, P.J.1    Chadwick, J.S.2    Aston, W.P.3    Dunphy, G.B.4
  • 8
    • 0030806872 scopus 로고    scopus 로고
    • Characterization of hemolytic and cytotoxic Gallysins: A relationship with arylphorins
    • Beresford P.J., Basinski-Gray J.M., Chiu J.K., Chadwick J.S., Aston W.P. Characterization of hemolytic and cytotoxic Gallysins: a relationship with arylphorins. Dev Comp Immunol. 21:(3):1997;253-266.
    • (1997) Dev Comp Immunol , vol.21 , Issue.3 , pp. 253-266
    • Beresford, P.J.1    Basinski-Gray, J.M.2    Chiu, J.K.3    Chadwick, J.S.4    Aston, W.P.5
  • 9
    • 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. 255:(3):1998;535-543.
    • (1998) Eur J Biochem , vol.255 , Issue.3 , pp. 535-543
    • Wedde, M.1    Weise, C.2    Kopacek, P.3    Franke, P.4    Vilcinskas, A.5
  • 10
    • 0034069583 scopus 로고    scopus 로고
    • Isolation and characterization of novel inducible serine protease inhibitors from larval hemolymph of the greater wax moth Galleria mellonella
    • Frobius A.C., Kanost M.R., Gotz 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. 267:(7):2000;2046-2053.
    • (2000) Eur J Biochem , vol.267 , Issue.7 , pp. 2046-2053
    • Frobius, A.C.1    Kanost, M.R.2    Gotz, P.3    Vilcinskas, A.4
  • 11
    • 0029556818 scopus 로고
    • The prophenoloxidase from the wax moth Galleria mellonella: Purification and characterization of the proenzyme
    • Kopacek P., Weise C., Götz P. The prophenoloxidase from the wax moth Galleria mellonella: purification and characterization of the proenzyme. Insect Biochem Mol Biol. 25:(10):1995;1081-1091.
    • (1995) Insect Biochem Mol Biol , vol.25 , Issue.10 , pp. 1081-1091
    • Kopacek, P.1    Weise, C.2    Götz, P.3
  • 13
    • 0030586931 scopus 로고    scopus 로고
    • Equalizing cDNA subtraction based on selective suppression of polymerase chain reaction: Cloning of Jurkat cell transcripts induced by phytohemaglutinin and phorbol 12-myristate 13-acetate
    • Gurskaya N.G., Diatchenko L., Chenchik A., Siebert P.D., Khaspekov G.L., Lukyanov K.A., Vagner L.L., Ermolaeva O.D., Lukyanov S.A., Sverdlov E.D. Equalizing cDNA subtraction based on selective suppression of polymerase chain reaction: cloning of Jurkat cell transcripts induced by phytohemaglutinin and phorbol 12-myristate 13-acetate. Anal Biochem. 240:(1):1996;90-97.
    • (1996) Anal Biochem , vol.240 , Issue.1 , pp. 90-97
    • Gurskaya, N.G.1    Diatchenko, L.2    Chenchik, A.3    Siebert, P.D.4    Khaspekov, G.L.5    Lukyanov, K.A.6    Vagner, L.L.7    Ermolaeva, O.D.8    Lukyanov, S.A.9    Sverdlov, E.D.10
  • 14
    • 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., Göetz P. Inhibition of phagocytic activity of plasmatocytes isolated from Galleria mellonella by entomogenous fungi and their secondary metabolites. J Ins Physiol. 43:1997;475-483.
    • (1997) J Ins Physiol , vol.43 , pp. 475-483
    • Vilcinskas, A.1    Matha, V.2    Göetz, P.3
  • 15
    • 0032091098 scopus 로고    scopus 로고
    • Quantification of low-copy transcripts by continuous SYBR Green I monitoring during amplification
    • See also p. 960 and 962
    • Morrison T.B., Weis J.J., Wittwer C.T. Quantification of low-copy transcripts by continuous SYBR Green I monitoring during amplification. Biotechniques. 24:(6):1998;954-958. See also p. 960 and 962.
    • (1998) Biotechniques , vol.24 , Issue.6 , pp. 954-958
    • Morrison, T.B.1    Weis, J.J.2    Wittwer, C.T.3
  • 16
    • 0026478996 scopus 로고
    • Mobilization of iron and iron-related proteins in rat spleen after intravenous injection of lipopolysaccharides (LPS)
    • Kumagai T., Awai M., Okada S. Mobilization of iron and iron-related proteins in rat spleen after intravenous injection of lipopolysaccharides (LPS). Pathol Res Pract. 188:(7):1992;931-941.
    • (1992) Pathol Res Pract , vol.188 , Issue.7 , pp. 931-941
    • Kumagai, T.1    Awai, M.2    Okada, S.3
  • 18
    • 0031046654 scopus 로고    scopus 로고
    • Antimicrobial peptides of leukocytes
    • Ganz T., Lehrer R.I. Antimicrobial peptides of leukocytes. Curr Opin Hematol. 4:(1):1997;53-58.
    • (1997) Curr Opin Hematol , vol.4 , Issue.1 , pp. 53-58
    • Ganz, T.1    Lehrer, R.I.2
  • 19
    • 0033771124 scopus 로고    scopus 로고
    • A masquerade-like serine proteinase homologue is necessary for phenoloxidase activity in the coleopteran insect, Holotrichia diomphalia larvae
    • Kwon T.H., Kim M.S., Choi H.W., Joo C.H., Cho M.Y., Lee B.L. A masquerade-like serine proteinase homologue is necessary for phenoloxidase activity in the coleopteran insect, Holotrichia diomphalia larvae. Eur J Biochem. 267:(20):2000;6188-6196.
    • (2000) Eur J Biochem , vol.267 , Issue.20 , pp. 6188-6196
    • Kwon, T.H.1    Kim, M.S.2    Choi, H.W.3    Joo, C.H.4    Cho, M.Y.5    Lee, B.L.6
  • 20
    • 0033975855 scopus 로고    scopus 로고
    • Cutting edge: Heat shock protein (HSP) 60 activates the innate immune response: CD14 is an essential receptor for HSP60 activation of mononuclear cells
    • Kol A., Lichtman A.H., Finberg R.W., Libby P., Kurt-Jones E.A. Cutting edge: heat shock protein (HSP) 60 activates the innate immune response: CD14 is an essential receptor for HSP60 activation of mononuclear cells. J Immunol. 164:(1):2000;13-17.
    • (2000) J Immunol , vol.164 , Issue.1 , pp. 13-17
    • Kol, A.1    Lichtman, A.H.2    Finberg, R.W.3    Libby, P.4    Kurt-Jones, E.A.5
  • 21
    • 0030752238 scopus 로고    scopus 로고
    • Gloverin, an antibacterial protein from the immune hemolymph of Hyalophora pupae
    • Axen A., Carlsson A., Engström A., Bennich H. Gloverin, an antibacterial protein from the immune hemolymph of Hyalophora pupae. Eur J Biochem. 247:(2):1997;614-619.
    • (1997) Eur J Biochem , vol.247 , Issue.2 , pp. 614-619
    • Axen, A.1    Carlsson, A.2    Engström, A.3    Bennich, H.4
  • 22
    • 0033597134 scopus 로고    scopus 로고
    • A pattern recognition protein for peptidoglycan. Cloning the cDNA and the gene of the silkworm, Bombyx mori
    • Ochiai M., Ashida M. A pattern recognition protein for peptidoglycan. Cloning the cDNA and the gene of the silkworm, Bombyx mori. J Biol Chem. 274:(17):1999;11854-11858.
    • (1999) J Biol Chem , vol.274 , Issue.17 , pp. 11854-11858
    • Ochiai, M.1    Ashida, M.2
  • 23
    • 0029884417 scopus 로고    scopus 로고
    • Purification of a peptidoglycan recognition protein from hemolymph of the silkworm, Bombyx mori
    • Yoshida H., Kinoshita K., Ashida M. Purification of a peptidoglycan recognition protein from hemolymph of the silkworm, Bombyx mori. J Biol Chem. 271:(23):1996;13854-13860.
    • (1996) J Biol Chem , vol.271 , Issue.23 , pp. 13854-13860
    • Yoshida, H.1    Kinoshita, K.2    Ashida, M.3
  • 24
    • 0022881454 scopus 로고
    • Beta-1,3-glucan receptor and peptidoglycan receptor are present as separate entities within insect prophenoloxidase activating system
    • Yoshida H., Ochiai M., Ashida M. Beta-1,3-glucan receptor and peptidoglycan receptor are present as separate entities within insect prophenoloxidase activating system. Biochem Biophys Res Commun. 141:(3):1986;1177-1184.
    • (1986) Biochem Biophys Res Commun , vol.141 , Issue.3 , pp. 1177-1184
    • Yoshida, H.1    Ochiai, M.2    Ashida, M.3
  • 25
    • 0032544089 scopus 로고    scopus 로고
    • A peptidoglycan recognition protein in innate immunity conserved from insects to humans
    • Kang D., Liu G., Lundström A., Gelius E., Steiner H. A peptidoglycan recognition protein in innate immunity conserved from insects to humans. Proc Natl Acad Sci USA. 95:(17):1998;10078-10082.
    • (1998) Proc Natl Acad Sci USA , vol.95 , Issue.17 , pp. 10078-10082
    • Kang, D.1    Liu, G.2    Lundström, A.3    Gelius, E.4    Steiner, H.5
  • 26
    • 0033168728 scopus 로고    scopus 로고
    • Cutting edge: Recognition of Gram-positive bacterial cell wall components by the innate immune system occurs via Toll-like receptor 2
    • Yoshimura A., Lien E., Ingalls R.R., Tuomanen E., Dziarski R., Golenbock D. Cutting edge: recognition of Gram-positive bacterial cell wall components by the innate immune system occurs via Toll-like receptor 2. J Immunol. 163:(1):1999;1-5.
    • (1999) J Immunol , vol.163 , Issue.1 , pp. 1-5
    • Yoshimura, A.1    Lien, E.2    Ingalls, R.R.3    Tuomanen, E.4    Dziarski, R.5    Golenbock, D.6
  • 27
    • 0034610370 scopus 로고    scopus 로고
    • A family of peptidoglycan recognition proteins in the fruit fly Drosophila melanogaster
    • Werner T., Liu G., Kang D., Ekengren S., Steiner H., Hultmark D. A family of peptidoglycan recognition proteins in the fruit fly Drosophila melanogaster. Proc Natl Acad Sci USA. 97:(25):2000;13772-13777.
    • (2000) Proc Natl Acad Sci USA , vol.97 , Issue.25 , pp. 13772-13777
    • Werner, T.1    Liu, G.2    Kang, D.3    Ekengren, S.4    Steiner, H.5    Hultmark, D.6
  • 28
    • 0027083267 scopus 로고
    • The Drosophila RNA-binding protein RBP1 is localized to transcriptionally active sites of chromosomes and shows a functional similarity to human splicing factor ASF/SF2
    • Kim Y.J., Zuo P., Manley J.L., Baker B.S. The Drosophila RNA-binding protein RBP1 is localized to transcriptionally active sites of chromosomes and shows a functional similarity to human splicing factor ASF/SF2. Genes Dev. 6:(12B):1992;2569-2579.
    • (1992) Genes Dev , vol.6 , Issue.12 B , pp. 2569-2579
    • Kim, Y.J.1    Zuo, P.2    Manley, J.L.3    Baker, B.S.4
  • 29
    • 0028034952 scopus 로고
    • A novel and major isoform of tyrosine hydroxylase in Drosophila is generated by alternative RNA processing
    • Birman S., Morgan B., Anzivino M., Hirsh J. A novel and major isoform of tyrosine hydroxylase in Drosophila is generated by alternative RNA processing. J Biol Chem. 269:(42):1994;26559-26567.
    • (1994) J Biol Chem , vol.269 , Issue.42 , pp. 26559-26567
    • Birman, S.1    Morgan, B.2    Anzivino, M.3    Hirsh, J.4
  • 30
    • 0024955886 scopus 로고
    • Approaching the asymptote? Evolution and revolution in immunology
    • Janeway C.A. Jr. Approaching the asymptote? Evolution and revolution in immunology. Cold Spring Harb Symp Quant Biol. 54:(Pt 1):1989;1-13.
    • (1989) Cold Spring Harb Symp Quant Biol , vol.54 , Issue.PART 1 , pp. 1-13
    • Janeway C.A., Jr.1
  • 31
    • 0032191163 scopus 로고    scopus 로고
    • Innate immune recognition and control of adaptive immune responses
    • Medzhitov R., Janeway C.A. Jr. Innate immune recognition and control of adaptive immune responses. Semin Immunol. 10:(5):1998;351-353.
    • (1998) Semin Immunol , vol.10 , Issue.5 , pp. 351-353
    • Medzhitov, R.1    Janeway C.A., Jr.2
  • 32
    • 0030831210 scopus 로고    scopus 로고
    • A human homologue of the Drosophila Toll protein signals activation of adaptive immunity
    • Medzhitov R., Preston-Hurlburt P., Janeway C.A. Jr. A human homologue of the Drosophila Toll protein signals activation of adaptive immunity. Nature. 388:(6640):1997;394-397.
    • (1997) Nature , vol.388 , Issue.6640 , pp. 394-397
    • Medzhitov, R.1    Preston-Hurlburt, P.2    Janeway C.A., Jr.3
  • 33
    • 0027402608 scopus 로고
    • The development of awareness of iron-withholding defense
    • Weinberg E.D. The development of awareness of iron-withholding defense. Perspect Biol Med. 36:(2):1993;215-221.
    • (1993) Perspect Biol Med , vol.36 , Issue.2 , pp. 215-221
    • Weinberg, E.D.1
  • 35
    • 0032526266 scopus 로고    scopus 로고
    • Cobatoxins 1 and 2 from Centruroides noxius Hoffmann constitute a subfamily of potassium-channel-blocking scorpion toxins
    • Selisko B., Garcia C., Becerril B., Gomez-Lagunas F., Garay C., Possani L.D. Cobatoxins 1 and 2 from Centruroides noxius Hoffmann constitute a subfamily of potassium-channel-blocking scorpion toxins. Eur J Biochem. 254:(3):1998;468-479.
    • (1998) Eur J Biochem , vol.254 , Issue.3 , pp. 468-479
    • Selisko, B.1    Garcia, C.2    Becerril, B.3    Gomez-Lagunas, F.4    Garay, C.5    Possani, L.D.6
  • 36
    • 0028019507 scopus 로고
    • Novel K(+)-channel-blocking toxins from the venom of the scorpion Centruroides limpidus Karsch
    • Martin B.M., Ramirez A.N., Gurrola G.B., Nobile M., Prestipino G., Possani L.D. Novel K(+)-channel-blocking toxins from the venom of the scorpion Centruroides limpidus Karsch. Biochem J. 304:(Pt 1):1994;51-56.
    • (1994) Biochem J , vol.304 , Issue.PART 1 , pp. 51-56
    • Martin, B.M.1    Ramirez, A.N.2    Gurrola, G.B.3    Nobile, M.4    Prestipino, G.5    Possani, L.D.6
  • 37
    • 0028927315 scopus 로고
    • NMR sequential assignments and solution structure of chlorotoxin, a small scorpion toxin that blocks chloride channels
    • Lippens G., Najib J., Wodak S.J., Tartar A. NMR sequential assignments and solution structure of chlorotoxin, a small scorpion toxin that blocks chloride channels. Biochemistry. 34:(1):1995;13-21.
    • (1995) Biochemistry , vol.34 , Issue.1 , pp. 13-21
    • Lippens, G.1    Najib, J.2    Wodak, S.J.3    Tartar, A.4
  • 38
    • 0033789345 scopus 로고    scopus 로고
    • Evidence for the existence of insect defensin-like peptide in scorpion venom
    • Zhu S., Li W., Jiang D., Zeng X. Evidence for the existence of insect defensin-like peptide in scorpion venom. IUBMB Life. 50:(1):2000;57-61.
    • (2000) IUBMB Life , vol.50 , Issue.1 , pp. 57-61
    • Zhu, S.1    Li, W.2    Jiang, D.3    Zeng, X.4
  • 40
    • 0030750976 scopus 로고    scopus 로고
    • Solution structure of drosomycin, the first inducible antifungal protein from insects
    • Landon C., Sodano P., Hetru C., Hoffmann J., Ptak M. Solution structure of drosomycin, the first inducible antifungal protein from insects. Protein Sci. 6:(9):1997;1878-1884.
    • (1997) Protein Sci , vol.6 , Issue.9 , pp. 1878-1884
    • Landon, C.1    Sodano, P.2    Hetru, C.3    Hoffmann, J.4    Ptak, M.5
  • 41
    • 0026418431 scopus 로고
    • Refined structure of charybdotoxin: Common motifs in scorpion toxins and insect defensins
    • Bontems F., Roumestand C., Gilquin B., Menez A., Toma F. Refined structure of charybdotoxin: common motifs in scorpion toxins and insect defensins. Science. 254:(5037):1991;1521-1523.
    • (1991) Science , vol.254 , Issue.5037 , pp. 1521-1523
    • Bontems, F.1    Roumestand, C.2    Gilquin, B.3    Menez, A.4    Toma, F.5
  • 43
    • 0032411402 scopus 로고    scopus 로고
    • Cysteine-rich antimicrobial peptides in invertebrates
    • Dimarcq J.L., Bulet P., Hetru C., Hoffmann J. Cysteine-rich antimicrobial peptides in invertebrates. Biopolymers. 47:(6):1998;465-477.
    • (1998) Biopolymers , vol.47 , Issue.6 , pp. 465-477
    • Dimarcq, J.L.1    Bulet, P.2    Hetru, C.3    Hoffmann, J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.