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Volumn 29, Issue 10, 2005, Pages 853-864

Cloning, expression and phylogenetic analysis of Hemolin, from the Chinese oak silkmoth, Antheraea pernyi

Author keywords

Antheraea pernyi; Chinese oak silkmoth; Hemolin; Innate immunity; Sequence analysis; Structure prediction

Indexed keywords

HEMOLIN; IMMUNOGLOBULIN; PHOSPHATE; UNCLASSIFIED DRUG;

EID: 20644444569     PISSN: 0145305X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.dci.2005.02.003     Document Type: Article
Times cited : (26)

References (45)
  • 1
    • 0020355347 scopus 로고
    • Insect immunity: Isolation and structure of cecropins B and D from pupae of the Chinese oak silk moth, Antheraea pernyi
    • Z. Qu, H. Steiner, A. Engström, H. Bennich, and H.G. Boman Insect immunity: isolation and structure of cecropins B and D from pupae of the Chinese oak silk moth, Antheraea pernyi Eur J Biochem 127 1982 219 224
    • (1982) Eur J Biochem , vol.127 , pp. 219-224
    • Qu, Z.1    Steiner, H.2    Engström, A.3    Bennich, H.4    Boman, H.G.5
  • 2
    • 0023303089 scopus 로고
    • Purification of a lectin from the hemolymph of Chinese oak silkmoth (Antheraea pernyi) pupae
    • X.M. Qu, C.F. Zhang, H. Komano, and S. Natori Purification of a lectin from the hemolymph of Chinese oak silkmoth (Antheraea pernyi) pupae J Biochem (Tokyo) 101 1987 545 551
    • (1987) J Biochem (Tokyo) , vol.101 , pp. 545-551
    • Qu, X.M.1    Zhang, C.F.2    Komano, H.3    Natori, S.4
  • 3
    • 0028274277 scopus 로고
    • A new female-specific fat-body protein of Antheraea pernyi - Purification, immunological properties, developmental profile and synthesis
    • M.N. Yokoyama, Z. Kajiura, H. Arai, M. Nakagaki, and R. Takei A new female-specific fat-body protein of Antheraea pernyi - purification, immunological properties, developmental profile and synthesis Comp Biochem Physiol B Biochem Mol Biol 107 1994 381 388
    • (1994) Comp Biochem Physiol B Biochem Mol Biol , vol.107 , pp. 381-388
    • Yokoyama, M.N.1    Kajiura, Z.2    Arai, H.3    Nakagaki, M.4    Takei, R.5
  • 4
    • 0016589542 scopus 로고
    • Insect immunity II. Simultaneous induction of antibacterial activity and selective synthesis of some hemolymph proteins in diapausing pupae of Hyalophora cecropia and Samia cynthia
    • I. Faye, A. Pye, T. Rasmuson, H.G. Boman, and I.A. Boman Insect immunity II. Simultaneous induction of antibacterial activity and selective synthesis of some hemolymph proteins in diapausing pupae of Hyalophora cecropia and Samia cynthia Infect Immun 12 1975 1426 1438
    • (1975) Infect Immun , vol.12 , pp. 1426-1438
    • Faye, I.1    Pye, A.2    Rasmuson, T.3    Boman, H.G.4    Boman, I.A.5
  • 5
    • 0000394077 scopus 로고
    • Insect immunity - V. Purification and some properties of immune protein P4 from haemolymph of Hyalophora cecropia pupae
    • T. Rasmuson, and H.G. Boman Insect immunity - V. Purification and some properties of immune protein P4 from haemolymph of Hyalophora cecropia pupae Insect Biochem 17 1979 133 140
    • (1979) Insect Biochem , vol.17 , pp. 133-140
    • Rasmuson, T.1    Boman, H.G.2
  • 6
    • 0025523371 scopus 로고
    • Isolation and characterization of bacteria-induced protein P4 from hemolymph of Manduca sexta
    • N.E. Ladendorff, and M.R. Kanost Isolation and characterization of bacteria-induced protein P4 from hemolymph of Manduca sexta Arch Insect Biochem Physiol 15 1990 33 41
    • (1990) Arch Insect Biochem Physiol , vol.15 , pp. 33-41
    • Ladendorff, N.E.1    Kanost, M.R.2
  • 7
    • 0345055811 scopus 로고    scopus 로고
    • Isolation and characterization of immune-related genes from the fall webworm, Hyphantria cunea, using PCR-based differential display and subtractive cloning
    • S.W. Shin, S.-S. Park, D.-S. Park, M.G. Kim, S.C. Kim, and P.T. Brey Isolation and characterization of immune-related genes from the fall webworm, Hyphantria cunea, using PCR-based differential display and subtractive cloning Insect Biochem Mol Biol 28 1998 827 837
    • (1998) Insect Biochem Mol Biol , vol.28 , pp. 827-837
    • Shin, S.W.1    Park, S.-S.2    Park, D.-S.3    Kim, M.G.4    Kim, S.C.5    Brey, P.T.6
  • 8
    • 0036837105 scopus 로고    scopus 로고
    • Molecular characterization of the insect immune protein hemolin and its high induction during embryonic diapause in the gypsy moth, Lymantria dispar
    • K.-Y. Lee, F.M. Horodyski, A.P. Valaitis, and D.L. Denlinger Molecular characterization of the insect immune protein hemolin and its high induction during embryonic diapause in the gypsy moth, Lymantria dispar Insect Biochem Mol Biol 32 2002 1457 1467
    • (2002) Insect Biochem Mol Biol , vol.32 , pp. 1457-1467
    • Lee, K.-Y.1    Horodyski, F.M.2    Valaitis, A.P.3    Denlinger, D.L.4
  • 9
    • 0029022485 scopus 로고
    • Structure and expression of Hemolin, an insect member of the immunoglobulin gene superfamily
    • I. Lindström-Dinnetz, S.-C. Sun, and I. Faye Structure and expression of Hemolin, an insect member of the immunoglobulin gene superfamily Eur J Biochem 230 1995 920 925
    • (1995) Eur J Biochem , vol.230 , pp. 920-925
    • Lindström-Dinnetz, I.1    Sun, S.-C.2    Faye, I.3
  • 10
    • 0034235488 scopus 로고    scopus 로고
    • The insect immune protein hemolin is expressed during oogenesis and embryogenesis
    • R. Bettencourt, Y. Assefaw-Redda, and I. Faye The insect immune protein hemolin is expressed during oogenesis and embryogenesis Mech Dev 95 2000 301 304
    • (2000) Mech Dev , vol.95 , pp. 301-304
    • Bettencourt, R.1    Assefaw-Redda, Y.2    Faye, I.3
  • 11
    • 0035999907 scopus 로고    scopus 로고
    • Hemolin gene silencing by ds-RNA injected into Cecropia pupae is lethal to next generation embryos
    • R. Bettencourt, O. Terenius, and I. Faye Hemolin gene silencing by ds-RNA injected into Cecropia pupae is lethal to next generation embryos Insect Mol Biol 11 2002 267 271
    • (2002) Insect Mol Biol , vol.11 , pp. 267-271
    • Bettencourt, R.1    Terenius, O.2    Faye, I.3
  • 12
    • 1642504737 scopus 로고    scopus 로고
    • Innate immune responses of a lepidopteran insect, Manduca sexta
    • M.R. Kanost, H. Jiang, and X.Q. Yu Innate immune responses of a lepidopteran insect, Manduca sexta Immunol Rev 198 2004 97 105
    • (2004) Immunol Rev , vol.198 , pp. 97-105
    • Kanost, M.R.1    Jiang, H.2    Yu, X.Q.3
  • 13
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • J.D. Thompson, D.G. Higgins, and T.J. Gibson CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice Nucleic Acids Res 22 1994 4673 4680
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 15
    • 0014757386 scopus 로고
    • A general method applicable to the search for similarities in the amino acid sequence of two proteins
    • S.A. Needleman, and C.D. Wunsch A general method applicable to the search for similarities in the amino acid sequence of two proteins J Mol Biol 48 1970 443 453
    • (1970) J Mol Biol , vol.48 , pp. 443-453
    • Needleman, S.A.1    Wunsch, C.D.2
  • 16
    • 0029563023 scopus 로고
    • A method for estimating the numbers of synonymous and nonsynonymous substitutions per site
    • J.M. Comeron A method for estimating the numbers of synonymous and nonsynonymous substitutions per site J Mol Evol 41 1995 1152 1159
    • (1995) J Mol Evol , vol.41 , pp. 1152-1159
    • Comeron, J.M.1
  • 17
    • 0032825011 scopus 로고    scopus 로고
    • K-estimator: Calculation of the number of nucleotide substitutions per site and the confidence intervals
    • J.M. Comeron K-estimator: calculation of the number of nucleotide substitutions per site and the confidence intervals Bioinformatics 15 1999 763 764
    • (1999) Bioinformatics , vol.15 , pp. 763-764
    • Comeron, J.M.1
  • 18
    • 0043123048 scopus 로고    scopus 로고
    • Prediction of lipid posttranslational modifications and localization signals from protein sequences: Big-Pi, NMT and PTS1
    • F. Eisenhaber, B. Eisenhaber, W. Kubina, S. Maurer-Stroh, G. Neuberger, and G. Schneider Prediction of lipid posttranslational modifications and localization signals from protein sequences: big-Pi, NMT and PTS1 Nucleic Acids Res 31 2003 3631 3634
    • (2003) Nucleic Acids Res , vol.31 , pp. 3631-3634
    • Eisenhaber, F.1    Eisenhaber, B.2    Kubina, W.3    Maurer-Stroh, S.4    Neuberger, G.5    Schneider, G.6
  • 22
    • 15444381280 scopus 로고
    • Protein modeling by e-mail
    • M.C. Peitsch Protein modeling by e-mail Bio-Technology 13 1995 658 660
    • (1995) Bio-Technology , vol.13 , pp. 658-660
    • Peitsch, M.C.1
  • 23
    • 0042622380 scopus 로고    scopus 로고
    • SWISS-MODEL: An automated protein homology-modeling server
    • T. Schwede, J. Kopp, N. Guex, and M.C. Peitsch SWISS-MODEL: an automated protein homology-modeling server Nucleic Acids Res 31 2003 3381 3385
    • (2003) Nucleic Acids Res , vol.31 , pp. 3381-3385
    • Schwede, T.1    Kopp, J.2    Guex, N.3    Peitsch, M.C.4
  • 24
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling
    • N. Guex, and M.C. Peitsch SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling Electrophoresis 18 1997 2714 2723
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 25
    • 0026274750 scopus 로고
    • Bacteria induced protein P4 (hemolin) from Manduca sexta: A member of the immunoglobulin superfamily, which can inhibit hemocyte aggregation
    • N.E. Ladendorff, and M.R. Kanost Bacteria induced protein P4 (hemolin) from Manduca sexta: a member of the immunoglobulin superfamily, which can inhibit hemocyte aggregation Arch Insect Biochem Physiol 18 1991 285 300
    • (1991) Arch Insect Biochem Physiol , vol.18 , pp. 285-300
    • Ladendorff, N.E.1    Kanost, M.R.2
  • 26
    • 0032516658 scopus 로고    scopus 로고
    • Crystal structure of hemolin; A horseshoe shape with implication for homophilic adhesion
    • X.-D. Su, N.G. Gastinel, D.E. Vaughn, I. Faye, P. Poon, and P.J. Bjorkman Crystal structure of hemolin; a horseshoe shape with implication for homophilic adhesion Science 281 1998 991 995
    • (1998) Science , vol.281 , pp. 991-995
    • Su, X.-D.1    Gastinel, N.G.2    Vaughn, D.E.3    Faye, I.4    Poon, P.5    Bjorkman, P.J.6
  • 27
    • 0031009383 scopus 로고    scopus 로고
    • Lipopolysaccharide interaction with hemolin, an insect member of the Ig-superfamily
    • S. Daffre, and I. Faye Lipopolysaccharide interaction with hemolin, an insect member of the Ig-superfamily FEBS Lett 408 1997 127 130
    • (1997) FEBS Lett , vol.408 , pp. 127-130
    • Daffre, S.1    Faye, I.2
  • 28
    • 0031574364 scopus 로고    scopus 로고
    • Cell adhesion properties of hemolin, an insect immune protein in the Ig superfamily
    • R. Bettencourt, H. Lanz-Mendoza, K.R. Lindquist, and I. Faye Cell adhesion properties of hemolin, an insect immune protein in the Ig superfamily Eur J Biochem 250 1997 630 637
    • (1997) Eur J Biochem , vol.250 , pp. 630-637
    • Bettencourt, R.1    Lanz-Mendoza, H.2    Lindquist, K.R.3    Faye, I.4
  • 30
    • 3042739339 scopus 로고    scopus 로고
    • Immuno-histochemical expression of alpha 1, alpha 2 and alpha 3 integrin subunits during angiogenesis in vitro
    • H. Suda, Y. Asami, E. Murata, K. Fujita, and M. Akita Immuno-histochemical expression of alpha 1, alpha 2 and alpha 3 integrin subunits during angiogenesis in vitro Histol Histopathol 19 3 2004 735 742
    • (2004) Histol Histopathol , vol.19 , Issue.3 , pp. 735-742
    • Suda, H.1    Asami, Y.2    Murata, E.3    Fujita, K.4    Akita, M.5
  • 31
    • 0031558798 scopus 로고    scopus 로고
    • Standard conformations for the canonical structures of immunoglobulins
    • B. Al-Lazikani, A.M. Lesk, and C. Chothia Standard conformations for the canonical structures of immunoglobulins J Mol Biol 273 1997 927 948
    • (1997) J Mol Biol , vol.273 , pp. 927-948
    • Al-Lazikani, B.1    Lesk, A.M.2    Chothia, C.3
  • 32
    • 0028676261 scopus 로고
    • Structural conservation of hypervariable regions in immunoglobulins evolution
    • S. Barre, A.S. Greenberg, M.F. Flajnik, and C. Chothia Structural conservation of hypervariable regions in immunoglobulins evolution Nat Struct Biol 1 1994 915 920
    • (1994) Nat Struct Biol , vol.1 , pp. 915-920
    • Barre, S.1    Greenberg, A.S.2    Flajnik, M.F.3    Chothia, C.4
  • 33
    • 0024279567 scopus 로고
    • One type of gamma-turn, rather than the other gives rise to chain-reversal in proteins
    • E. Milner-White, B.M. Ross, R. Ismail, K. Belhadj-Mostefa, and R. Poet One type of gamma-turn, rather than the other gives rise to chain-reversal in proteins J Mol Biol 204 1988 777 782
    • (1988) J Mol Biol , vol.204 , pp. 777-782
    • Milner-White, E.1    Ross, B.M.2    Ismail, R.3    Belhadj-Mostefa, K.4    Poet, R.5
  • 34
  • 36
    • 0031882369 scopus 로고    scopus 로고
    • Protein phylogenies provide evidence of a radical discountinuity between arthropod and vertebrate immune systems
    • A.L. Hughes Protein phylogenies provide evidence of a radical discountinuity between arthropod and vertebrate immune systems Immunogenetics 47 1998 283 296
    • (1998) Immunogenetics , vol.47 , pp. 283-296
    • Hughes, A.L.1
  • 37
    • 0030666222 scopus 로고    scopus 로고
    • Innate immunity: The virtues of a nonclonal system of recognition
    • R. Medzhitov, and C.A. Janeaway Jr Innate immunity: the virtues of a nonclonal system of recognition Cell 91 1997 295 298
    • (1997) Cell , vol.91 , pp. 295-298
    • Medzhitov, R.1    Janeaway Jr., C.A.2
  • 38
    • 0242333147 scopus 로고    scopus 로고
    • The evolution of parasite recognition genes in the innate immune system: Purifying selection on Drosophila melanogaster peptidoglycan recognition proteins
    • F.M. Jiggins, and G.D. Hurst The evolution of parasite recognition genes in the innate immune system: purifying selection on Drosophila melanogaster peptidoglycan recognition proteins J Mol Evol 57 2003 598 605
    • (2003) J Mol Evol , vol.57 , pp. 598-605
    • Jiggins, F.M.1    Hurst, G.D.2
  • 39
    • 0030860232 scopus 로고    scopus 로고
    • O-GLYCBASE version 2.0: A revised database of O-glycosylated proteins
    • J.E. Hansen, O. Lund, K. Rapacki, and S. Brunak O-GLYCBASE version 2.0: a revised database of O-glycosylated proteins Nucleic Acids Res 25 1997 278 282
    • (1997) Nucleic Acids Res , vol.25 , pp. 278-282
    • Hansen, J.E.1    Lund, O.2    Rapacki, K.3    Brunak, S.4
  • 40
    • 0022706389 scopus 로고
    • The relation between the divergence of sequence and structure in proteins
    • C. Chothia, and A.M. Lesk The relation between the divergence of sequence and structure in proteins EMBO J 5 1986 823 826
    • (1986) EMBO J , vol.5 , pp. 823-826
    • Chothia, C.1    Lesk, A.M.2
  • 41
    • 0036228004 scopus 로고    scopus 로고
    • Binding of hemolin to bacterial lipopolysaccharide and lipoteichoic acid. An immunoglobulin superfamily member from insects as a pattern-recognition receptor
    • X.Q. Yu, and M.R. Kanost Binding of hemolin to bacterial lipopolysaccharide and lipoteichoic acid. An immunoglobulin superfamily member from insects as a pattern-recognition receptor Eur J Biochem 269 2002 1827 1834
    • (2002) Eur J Biochem , vol.269 , pp. 1827-1834
    • Yu, X.Q.1    Kanost, M.R.2
  • 42
    • 0023764283 scopus 로고
    • Pattern of nucleotide substitution at major histocompatibility complex class-I loci reveals overdominant selection
    • A.L. Hughes, and M. Nei Pattern of nucleotide substitution at major histocompatibility complex class-I loci reveals overdominant selection Nature 335 1988 167 170
    • (1988) Nature , vol.335 , pp. 167-170
    • Hughes, A.L.1    Nei, M.2
  • 43
    • 0040771786 scopus 로고
    • Nucleotide substitution at major histocompatibility complex class-II loci - Evidence for overdominant selection
    • A.L. Hughes, and M. Nei Nucleotide substitution at major histocompatibility complex class-II loci - evidence for overdominant selection Proc Natl Acad Sci USA 86 1989 958 962
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 958-962
    • Hughes, A.L.1    Nei, M.2
  • 44
    • 0024392448 scopus 로고
    • Positive darwinian selection observed at the variable-region genes of immunoglobulins
    • T. Tanaka, and M. Nei Positive darwinian selection observed at the variable-region genes of immunoglobulins Mol Biol Evol 6 1989 447 459
    • (1989) Mol Biol Evol , vol.6 , pp. 447-459
    • Tanaka, T.1    Nei, M.2
  • 45
    • 3943102816 scopus 로고    scopus 로고
    • Baculovirus and dsRNA induce Hemolin, but no antibacterial activity, in Antheraea pernyi
    • M. Hirai, O. Terenius, W. Li, and I. Faye Baculovirus and dsRNA induce Hemolin, but no antibacterial activity, in Antheraea pernyi Insect Mol Biol 13 2004 399 405
    • (2004) Insect Mol Biol , vol.13 , pp. 399-405
    • Hirai, M.1    Terenius, O.2    Li, W.3    Faye, I.4


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