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Volumn 34, Issue 5, 2004, Pages 485-492

Identification of an aspartylglucosaminidase-like protein in the venom of the parasitic wasp Asobara tabida (Hymenoptera: Braconidae)

Author keywords

Asobara tabida; Aspartylglucosaminidase; Drosophila melanogaster; Enzymes; Insects; Parasitoid; Venom

Indexed keywords

INSECT PROTEIN; N4 (BETA N ACETYLGLUCOSAMINYL)ASPARAGINASE; PROTEIN SUBUNIT; WASP VENOM;

EID: 1942534666     PISSN: 09651748     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ibmb.2004.03.001     Document Type: Article
Times cited : (35)

References (42)
  • 1
    • 0141993544 scopus 로고    scopus 로고
    • A serine proteinase homolog venom protein from an endoparasitoid wasp inhibits melanization of the host hemolymph
    • Asgari S., Zhang G., Zareie R., Schmidt O. A serine proteinase homolog venom protein from an endoparasitoid wasp inhibits melanization of the host hemolymph. Insect Biochem. Mol. Biol. 33:2003a;1017-1024
    • (2003) Insect Biochem. Mol. Biol. , vol.33 , pp. 1017-1024
    • Asgari, S.1    Zhang, G.2    Zareie, R.3    Schmidt, O.4
  • 2
    • 0038266351 scopus 로고    scopus 로고
    • Isolation and characterization of a novel venom protein from an endoparasitoid, Cotesia rubecula (Hym.: Braconidae)
    • Asgari S., Zareie R., Zhang G., Schmidt O. Isolation and characterization of a novel venom protein from an endoparasitoid, Cotesia rubecula (Hym.: Braconidae). Arch. Insect Biochem. Physiol. 53:2003b;92-100
    • (2003) Arch. Insect Biochem. Physiol. , vol.53 , pp. 92-100
    • Asgari, S.1    Zareie, R.2    Zhang, G.3    Schmidt, O.4
  • 3
    • 0003315349 scopus 로고
    • Arthropods venoms
    • Bettini S. Berlin: Springer Verlag
    • Beard R.L. Arthropods venoms. Bettini S. Handbuch der Experimentellen Pharmakologie. vol. 48:1978;773-780 Springer Verlag, Berlin
    • (1978) Handbuch der Experimentellen Pharmakologie , vol.48 , pp. 773-780
    • Beard, R.L.1
  • 4
    • 0001672633 scopus 로고
    • Host hemolymph monophenoloxidase activity in parasitized Manduca sexta larvae and evidence for inhibition by wasp polydnavirus
    • Beckage N.E., Metcalf J.S., Nesbit D.J., Schleifer K.W., Zeltan S.R., de Buron I. Host hemolymph monophenoloxidase activity in parasitized Manduca sexta larvae and evidence for inhibition by wasp polydnavirus. Insect Biochem. Mol. Biol. 20:1990;285-294
    • (1990) Insect Biochem. Mol. Biol. , vol.20 , pp. 285-294
    • Beckage, N.E.1    Metcalf, J.S.2    Nesbit, D.J.3    Schleifer, K.W.4    Zeltan, S.R.5    De Buron, I.6
  • 5
    • 0034708256 scopus 로고    scopus 로고
    • Selective high-affinity transport of aspartate by a Drosophila homologue of the excitatory amino acid transporters
    • Besson M.T., Soustelle L., Birman S. Selective high-affinity transport of aspartate by a Drosophila homologue of the excitatory amino acid transporters. Curr. Biol. 10:2000;207-210
    • (2000) Curr. Biol. , vol.10 , pp. 207-210
    • Besson, M.T.1    Soustelle, L.2    Birman, S.3
  • 6
    • 0019826687 scopus 로고
    • Characterization of human high-density lipoproteins by gradient gel electrophoresis
    • Blanche, P.J., Gong, E.L., Forte, T.M., Nichols, A.V., 1981. Characterization of human high-density lipoproteins by gradient gel electrophoresis. Biochim. Biophys. Acta. 665, 408-419.
    • (1981) Biochim. Biophys. Acta. , vol.665 , pp. 408-419
    • Blanche, P.J.1    Gong, E.L.2    Forte, T.M.3    Nichols, A.V.4
  • 7
    • 84990473710 scopus 로고
    • Evaluation of teratocyte functions: An overview
    • Dahlman D.L. Evaluation of teratocyte functions: an overview. Arch. Insect Biochem. Physiol. 13:1990;159-166
    • (1990) Arch. Insect Biochem. Physiol. , vol.13 , pp. 159-166
    • Dahlman, D.L.1
  • 8
    • 0002200407 scopus 로고
    • Etude quantitative du développement de la Drosophile élevée en milieu axénique
    • David J.R. Etude quantitative du développement de la Drosophile élevée en milieu axénique. Bull. Biol. Fr. Belg. 93:1959;472-505
    • (1959) Bull. Biol. Fr. Belg. , vol.93 , pp. 472-505
    • David, J.R.1
  • 10
    • 0030848062 scopus 로고    scopus 로고
    • Physiological and biochemical analysis of factors in the female venom gland and larval salivary secretions of the ectoparasitoid wasp Eupelmus orientalis
    • Doury G., Bigot Y., Periquet G. Physiological and biochemical analysis of factors in the female venom gland and larval salivary secretions of the ectoparasitoid wasp Eupelmus orientalis. J. Insect Physiol. 43:1997;69-81
    • (1997) J. Insect Physiol. , vol.43 , pp. 69-81
    • Doury, G.1    Bigot, Y.2    Periquet, G.3
  • 11
    • 0030475898 scopus 로고    scopus 로고
    • Avoidance of encapsulation in the absence of VLP by a braconid parasitoid of Drosophila larvae: An ultrastructural study
    • Eslin P., Giordanengo P., Fourdrain Y., Prévost G. Avoidance of encapsulation in the absence of VLP by a braconid parasitoid of Drosophila larvae: an ultrastructural study. Can. J. Zool. 74:1996;2193-2198
    • (1996) Can. J. Zool. , vol.74 , pp. 2193-2198
    • Eslin, P.1    Giordanengo, P.2    Fourdrain, Y.3    Prévost, G.4
  • 12
    • 0026089364 scopus 로고
    • Aspartylglucosaminuria: CDNA encoding human aspartylglucosaminidase and the missense mutation causing the disease
    • Ikonen E., Baumann M., Grön K., Syvänen A.-C., Enomaa N., Halila R., Aula P., Peltonen L. Aspartylglucosaminuria: cDNA encoding human aspartylglucosaminidase and the missense mutation causing the disease. EMBO J. 10:1991;51-58
    • (1991) EMBO J. , vol.10 , pp. 51-58
    • Ikonen, E.1    Baumann, M.2    Grön, K.3    Syvänen, A.-C.4    Enomaa, N.5    Halila, R.6    Aula, P.7    Peltonen, L.8
  • 13
    • 0027389271 scopus 로고
    • Lysosomal aspartylglucosaminidase is processed to the active subunit complex in the endoplasmic reticulum
    • Ikonen E., Julkunen I., Tollersrud O.-K., Kalkkinen N., Peltonen L. Lysosomal aspartylglucosaminidase is processed to the active subunit complex in the endoplasmic reticulum. EMBO J. 12:1993;295-302
    • (1993) EMBO J. , vol.12 , pp. 295-302
    • Ikonen, E.1    Julkunen, I.2    Tollersrud, O.-K.3    Kalkkinen, N.4    Peltonen, L.5
  • 14
    • 0026724927 scopus 로고
    • Sequence, structure and expression of a wasp venom protein with a negatively charged signal peptide and a novel repeating internal structure
    • Jones D., Sawicki G., Wozniak M. Sequence, structure and expression of a wasp venom protein with a negatively charged signal peptide and a novel repeating internal structure. J. Biol. Chem. 267:1992;14871-14878
    • (1992) J. Biol. Chem. , vol.267 , pp. 14871-14878
    • Jones, D.1    Sawicki, G.2    Wozniak, M.3
  • 15
    • 0026095291 scopus 로고
    • Glycoasparaginase from human leukocytes. Inactivation and covalent modification with diazo-oxonorvaline
    • Kaartinen V., Williams J.C., Tomich J., Yates J.R., Hood L.E., Mononen I. Glycoasparaginase from human leukocytes. Inactivation and covalent modification with diazo-oxonorvaline. J. Biol. Chem. 266:1991;5860-5869
    • (1991) J. Biol. Chem. , vol.266 , pp. 5860-5869
    • Kaartinen, V.1    Williams, J.C.2    Tomich, J.3    Yates, J.R.4    Hood, L.E.5    Mononen, I.6
  • 16
    • 0028165757 scopus 로고
    • Geographical variation in resistance of the parasitoid Asobara tabida against encapsulation by Drosophila melanogaster larvae: The mechanism explored
    • Kraaijeveld A.R., van Alphen J.M. Geographical variation in resistance of the parasitoid Asobara tabida against encapsulation by Drosophila melanogaster larvae: the mechanism explored. Phys. Entomol. 19:1994;9-14
    • (1994) Phys. Entomol. , vol.19 , pp. 9-14
    • Kraaijeveld, A.R.1    Van Alphen, J.M.2
  • 17
    • 0028017691 scopus 로고
    • Isolation, cloning and characterization of new chitinase stored in active form in chitin-lined venom reservoir
    • Krishnan A., Nair P.N., Jones D.J. Isolation, cloning and characterization of new chitinase stored in active form in chitin-lined venom reservoir. J. Biol. Chem. 269:1994;20971-20976
    • (1994) J. Biol. Chem. , vol.269 , pp. 20971-20976
    • Krishnan, A.1    Nair, P.N.2    Jones, D.J.3
  • 18
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:1970;680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 19
    • 0029837611 scopus 로고    scopus 로고
    • Purification, biochemistry and molecular cloning of an insect glycosylasparaginase from Spodoptera frugiperda
    • Liu Y., Dunn G.S., Aronson N.N. Jr. Purification, biochemistry and molecular cloning of an insect glycosylasparaginase from Spodoptera frugiperda. Glycobiology. 6:1996;527-536
    • (1996) Glycobiology , vol.6 , pp. 527-536
    • Liu, Y.1    Dunn, G.S.2    Aronson Jr., N.N.3
  • 21
    • 0032619186 scopus 로고    scopus 로고
    • Staining of preparative 2-D gels. Coomassie blue and imidazole-zinc negative staining
    • Matsui N.M., Smith-Beckerman D.M., Epstein L.B. Staining of preparative 2-D gels. Coomassie blue and imidazole-zinc negative staining. Methods Mol. Biol. 112:1999;307-311
    • (1999) Methods Mol. Biol. , vol.112 , pp. 307-311
    • Matsui, N.M.1    Smith-Beckerman, D.M.2    Epstein, L.B.3
  • 22
    • 0000052495 scopus 로고
    • Avoidance of encapsulation by Asobara tabida, a larval parasitoid of Drosophila species
    • Monconduit H., Prévost G. Avoidance of encapsulation by Asobara tabida, a larval parasitoid of Drosophila species. Norw. J. Agr. Sci. 16:1994;301-309
    • (1994) Norw. J. Agr. Sci. , vol.16 , pp. 301-309
    • Monconduit, H.1    Prévost, G.2
  • 23
    • 0036248855 scopus 로고    scopus 로고
    • Effects of parasitism by Asobara tabida (Hymenoptera: Braconidae) on the development, survival and activity of Drosophila melanogaster larvae
    • Moreau S.J.M., Dingremont A., Doury G., Giordanengo P. Effects of parasitism by Asobara tabida (Hymenoptera: Braconidae) on the development, survival and activity of Drosophila melanogaster larvae. J. Insect Physiol. 48:2002;337-347
    • (2002) J. Insect Physiol. , vol.48 , pp. 337-347
    • Moreau, S.J.M.1    Dingremont, A.2    Doury, G.3    Giordanengo, P.4
  • 24
    • 0019800463 scopus 로고
    • Silver stain for proteins in polyacrylamide gels: A modified procedure with enhanced uniform sensitivity
    • Morrissey J.H. Silver stain for proteins in polyacrylamide gels: a modified procedure with enhanced uniform sensitivity. Anal. Biochem. 117:1981;307-310
    • (1981) Anal. Biochem. , vol.117 , pp. 307-310
    • Morrissey, J.H.1
  • 25
    • 0028786346 scopus 로고
    • Three-dimensional structure of human lysosomal aspartylglucosaminidase
    • Oinonen C., Tikkanen R., Rouvinen J., Peltonen L. Three-dimensional structure of human lysosomal aspartylglucosaminidase. Nat. Struct. Biol. 2:1995;1102-1108
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 1102-1108
    • Oinonen, C.1    Tikkanen, R.2    Rouvinen, J.3    Peltonen, L.4
  • 26
    • 0002556454 scopus 로고    scopus 로고
    • Noxious components of venom from the pupa-specific parasitoid Pimpla hypochondriaca
    • Parkinson N.M., Weaver R.J. Noxious components of venom from the pupa-specific parasitoid Pimpla hypochondriaca. J. Invertebr. Pathol. 73:1999;74-83
    • (1999) J. Invertebr. Pathol. , vol.73 , pp. 74-83
    • Parkinson, N.M.1    Weaver, R.J.2
  • 27
    • 0035182123 scopus 로고    scopus 로고
    • A new form of arthropod phenoloxidase is abundant in venom of the parasitoid wasp Pimpla hypochondriaca
    • Parkinson N.M., Smith I., Weaver R.J., Edwards J.P. A new form of arthropod phenoloxidase is abundant in venom of the parasitoid wasp Pimpla hypochondriaca. Insect Biochem. Mol. Biol. 31:2001;57-63
    • (2001) Insect Biochem. Mol. Biol. , vol.31 , pp. 57-63
    • Parkinson, N.M.1    Smith, I.2    Weaver, R.J.3    Edwards, J.P.4
  • 28
    • 0035983806 scopus 로고    scopus 로고
    • A venom protein from the endoparasitoid wasp Pimpla hypocondriaca is similar to snake venom reprolysin-type metalloproteases
    • Parkinson N.M., Conyers C., Smith I. A venom protein from the endoparasitoid wasp Pimpla hypocondriaca is similar to snake venom reprolysin-type metalloproteases. J. Invertebr. Pathol. 79:2002a;129-131
    • (2002) J. Invertebr. Pathol. , vol.79 , pp. 129-131
    • Parkinson, N.M.1    Conyers, C.2    Smith, I.3
  • 29
    • 0036015607 scopus 로고    scopus 로고
    • Analysis of venom constituents from the parasitoid wasp Pimpla hypocondriaca and cloning of cDNA encoding a venom protein
    • Parkinson N.M., Richards E.H., Conyers C., Smith I., Edwards J.P. Analysis of venom constituents from the parasitoid wasp Pimpla hypocondriaca and cloning of cDNA encoding a venom protein. Insect Biochem. Mol. Biol. 32:2002b;729-735
    • (2002) Insect Biochem. Mol. Biol. , vol.32 , pp. 729-735
    • Parkinson, N.M.1    Richards, E.H.2    Conyers, C.3    Smith, I.4    Edwards, J.P.5
  • 30
    • 0037396329 scopus 로고    scopus 로고
    • CDNAs encoding large venom proteins from the parasitoid wasp Pimpla hypocondriaca identified by random sequence analysis
    • Parkinson N.M., Conyers C., Keen J.N., MacNicoll A.D., Smith I., Weaver R.J. cDNAs encoding large venom proteins from the parasitoid wasp Pimpla hypocondriaca identified by random sequence analysis. Comp. Biochem. Physiol. Part C. 134:2003;513-520
    • (2003) Comp. Biochem. Physiol. Part C , vol.134 , pp. 513-520
    • Parkinson, N.M.1    Conyers, C.2    Keen, J.N.3    MacNicoll, A.D.4    Smith, I.5    Weaver, R.J.6
  • 31
    • 0029998354 scopus 로고    scopus 로고
    • Ser72Pro active-site disease mutation in human lysosomal aspartylglucosaminidase: Abnormal intracellular processing and evidence for extracellular activation
    • Peltola M., Tikkanen R., Peltonen L., Jalanko A. Ser72Pro active-site disease mutation in human lysosomal aspartylglucosaminidase: abnormal intracellular processing and evidence for extracellular activation. Hum. Mol. Genet. 6:1996;737-743
    • (1996) Hum. Mol. Genet. , vol.6 , pp. 737-743
    • Peltola, M.1    Tikkanen, R.2    Peltonen, L.3    Jalanko, A.4
  • 32
    • 0028675596 scopus 로고
    • Purification and characterization of insecticidal toxins from venom glands of the parasitic wasp, Bracon hebetor
    • Quistad G.B., Nguyen Q., Bernasconi P., Leisy D. Purification and characterization of insecticidal toxins from venom glands of the parasitic wasp, Bracon hebetor. Insect Biochem. Mol. Biol. 24:1994;955-961
    • (1994) Insect Biochem. Mol. Biol. , vol.24 , pp. 955-961
    • Quistad, G.B.1    Nguyen, Q.2    Bernasconi, P.3    Leisy, D.4
  • 33
    • 0028956744 scopus 로고
    • Immediate interaction between the nascent subunits and two conserved amino acids Trp34 and Thr206 are needed for the catalytic activity of aspartylglucosaminidase
    • Riikonen A., Tikkanen R., Jalanko A., Peltonen L. Immediate interaction between the nascent subunits and two conserved amino acids Trp34 and Thr206 are needed for the catalytic activity of aspartylglucosaminidase. J. Biol. Chem. 270:1995;4903-4907
    • (1995) J. Biol. Chem. , vol.270 , pp. 4903-4907
    • Riikonen, A.1    Tikkanen, R.2    Jalanko, A.3    Peltonen, L.4
  • 34
    • 0029835573 scopus 로고    scopus 로고
    • Primary folding of aspartylglucosaminidase. Significance of disulfide bridges and evidence of early multimerization
    • Riikonen A., Rouvinen J., Tikkanen R., Julkunen I., Peltonen L., Jalanko A. Primary folding of aspartylglucosaminidase. Significance of disulfide bridges and evidence of early multimerization. J. Biol. Chem. 271:1996;21340-21344
    • (1996) J. Biol. Chem. , vol.271 , pp. 21340-21344
    • Riikonen, A.1    Rouvinen, J.2    Tikkanen, R.3    Julkunen, I.4    Peltonen, L.5    Jalanko, A.6
  • 38
    • 0001396176 scopus 로고    scopus 로고
    • Polydnavirus and venom of the egg-larval parasitoid Chelonus inanitus (Braconidae) induce developmental arrest in the prepupa of its host Spodoptera littoralis (Noctuidae)
    • Soller M., Lanzrein B. Polydnavirus and venom of the egg-larval parasitoid Chelonus inanitus (Braconidae) induce developmental arrest in the prepupa of its host Spodoptera littoralis (Noctuidae). J. Insect Physiol. 42:1996;471-481
    • (1996) J. Insect Physiol. , vol.42 , pp. 471-481
    • Soller, M.1    Lanzrein, B.2
  • 39
    • 0028311306 scopus 로고
    • Development and partial characterization of monoclonal antibodies to venom of the parasitoid Microplitis demolitor
    • Strand M.R., Johnson J.A., Noda T., Dover B.A. Development and partial characterization of monoclonal antibodies to venom of the parasitoid Microplitis demolitor. Arch. Insect Biochem. Physiol. 26:1994;123-136
    • (1994) Arch. Insect Biochem. Physiol. , vol.26 , pp. 123-136
    • Strand, M.R.1    Johnson, J.A.2    Noda, T.3    Dover, B.A.4
  • 40
    • 0029936212 scopus 로고    scopus 로고
    • Functional analyses of active site residues of human lysosomal aspartylglucosaminidase: Implications for catalytic mechanism and autocatalytic activation
    • Tikkanen R., Riikonen A., Oinonen C., Rouvinen J., Peltonen L. Functional analyses of active site residues of human lysosomal aspartylglucosaminidase: implications for catalytic mechanism and autocatalytic activation. EMBO J. 15:1996;2954-2960
    • (1996) EMBO J. , vol.15 , pp. 2954-2960
    • Tikkanen, R.1    Riikonen, A.2    Oinonen, C.3    Rouvinen, J.4    Peltonen, L.5
  • 41
    • 0037474204 scopus 로고    scopus 로고
    • Two-step dimerization for autoproteolysis to activate glycosylasparaginase
    • Wang, Y., Guo, H.C., 2003. Two-step dimerization for autoproteolysis to activate glycosylasparaginase. J. Biol. Chem. 278, 3210-3219.
    • (2003) J. Biol. Chem. , vol.278 , pp. 3210-3219
    • Wang, Y.1    Guo, H.C.2
  • 42
    • 0028250378 scopus 로고
    • Evidence for an early immunosuppressive role for related Campoletis sonorensis venom and ovarian proteins in Heliothis virescens
    • Webb B.A., Luckhart S. Evidence for an early immunosuppressive role for related Campoletis sonorensis venom and ovarian proteins in Heliothis virescens. Arch. Insect Biochem. Physiol. 26:1994;147-163
    • (1994) Arch. Insect Biochem. Physiol. , vol.26 , pp. 147-163
    • Webb, B.A.1    Luckhart, S.2


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