메뉴 건너뛰기




Volumn 101, Issue 5, 1998, Pages 691-698

Superior biologic activity of the recombinant bee venom allergen hyaluronidase expressed in baculovirus-infected insect cells as compared with Escherichia coli

Author keywords

Baculovirus; Bee venom allergy; Enzymatic activity; Hyaluronidase; Recombinant allergens; Specific IgE

Indexed keywords

ALLERGEN; BEE VENOM; HYALURONIDASE; IMMUNOGLOBULIN E; RECOMBINANT PROTEIN;

EID: 0031982094     PISSN: 00916749     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0091-6749(98)70179-4     Document Type: Article
Times cited : (101)

References (38)
  • 2
    • 0024726507 scopus 로고
    • Analysis of the cDNA for phospholipase A2 from honeybee venom glands
    • Kuchler K, Gmachl M, Sippl MJ, Kreil G. Analysis of the cDNA for phospholipase A2 from honeybee venom glands. Eur J Biochem 1989;184:249-54.
    • (1989) Eur J Biochem , vol.184 , pp. 249-254
    • Kuchler, K.1    Gmachl, M.2    Sippl, M.J.3    Kreil, G.4
  • 3
    • 0026458989 scopus 로고
    • High level expression in Escherichia coli and rapid purification of enzymatically active honey bee venom phospholipase A2
    • Dudler T, Chen WQ, Wang SS, Schneider T, Annand RR, Dempcy RO, et al. High level expression in Escherichia coli and rapid purification of enzymatically active honey bee venom phospholipase A2. Biochem Biophys Acta 1992;1165:201-10.
    • (1992) Biochem Biophys Acta , vol.1165 , pp. 201-210
    • Dudler, T.1    Chen, W.Q.2    Wang, S.S.3    Schneider, T.4    Annand, R.R.5    Dempcy, R.O.6
  • 4
    • 0029063616 scopus 로고
    • Natural and recombinant enzymatically active or inactive bee venom phospholipase A2 has the same potency to release histamine from basophils in patients with Hymenoptera allergy
    • Forster E, Dudler T, Gmachl M, Aberer W, Urbanek R, Suter M. Natural and recombinant enzymatically active or inactive bee venom phospholipase A2 has the same potency to release histamine from basophils in patients with Hymenoptera allergy. J Allergy Clin Immunol 1995;95:1229-35.
    • (1995) J Allergy Clin Immunol , vol.95 , pp. 1229-1235
    • Forster, E.1    Dudler, T.2    Gmachl, M.3    Aberer, W.4    Urbanek, R.5    Suter, M.6
  • 6
    • 0022479917 scopus 로고
    • Allergens in Hymenoptera venoms XVI. Studies of the structures and cross-reactivities of vespid venom phospholipases
    • Hoffman DR. Allergens in Hymenoptera venoms XVI. Studies of the structures and cross-reactivities of vespid venom phospholipases. J Allergy Clin Immunol 1986;78:337-43.
    • (1986) J Allergy Clin Immunol , vol.78 , pp. 337-343
    • Hoffman, D.R.1
  • 7
    • 0028956730 scopus 로고
    • Sequence identity and antigenic cross reactivity of white face hornet allergen, also a hyaluronidase, with other proteins
    • Lu G, Kochoumian L, King TP. Sequence identity and antigenic cross reactivity of white face hornet allergen, also a hyaluronidase, with other proteins. J Biol Chem 1995;270:4457-65.
    • (1995) J Biol Chem , vol.270 , pp. 4457-4465
    • Lu, G.1    Kochoumian, L.2    King, T.P.3
  • 8
    • 0029079957 scopus 로고
    • Hyalorunidases - A group of neglected enzymes
    • Kreil G. Hyalorunidases - a group of neglected enzymes. Protein Sci 1995;4:1666-9.
    • (1995) Protein Sci , vol.4 , pp. 1666-1669
    • Kreil, G.1
  • 9
    • 77956924584 scopus 로고
    • Hyaluronidases
    • Boyer PD, editor New York: Academic Press
    • Meyer K. Hyaluronidases. In: Boyer PD, editor. The enzymes. 3rd ed. Vol. V. New York: Academic Press; 1971. p. 307-20.
    • (1971) The Enzymes. 3rd Ed. , vol.5 , pp. 307-320
    • Meyer, K.1
  • 10
    • 0021343667 scopus 로고
    • The purification and characterization of hyaluronidase from the venom of the honey bee, Apis mellifera
    • Kemeny DM, Dalton N, Lawrence AJ, Pearce FL, Vernon CA. The purification and characterization of hyaluronidase from the venom of the honey bee, Apis mellifera. Eur J Biochem 1984;139:217-23.
    • (1984) Eur J Biochem , vol.139 , pp. 217-223
    • Kemeny, D.M.1    Dalton, N.2    Lawrence, A.J.3    Pearce, F.L.4    Vernon, C.A.5
  • 11
    • 0027520896 scopus 로고
    • Bee venom hyaluronidase is homologous to a membrane protein of mammalian sperm
    • Gmachl M, Kreil G. Bee venom hyaluronidase is homologous to a membrane protein of mammalian sperm. Proc Natl Acad Sci USA 1993;90:3569-73.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 3569-3573
    • Gmachl, M.1    Kreil, G.2
  • 12
    • 0015320982 scopus 로고
    • Construction and properties of Escherichia coli strains exhibiting alpha-complementation of beta-galactosidase fragments in vivo
    • Zamenhof PJ, Villarejo M. Construction and properties of Escherichia coli strains exhibiting alpha-complementation of beta-galactosidase fragments in vivo. J Bacteriol 1972;110:171-8.
    • (1972) J Bacteriol , vol.110 , pp. 171-178
    • Zamenhof, P.J.1    Villarejo, M.2
  • 13
    • 0000926770 scopus 로고
    • System for high level production in E. coli and rapid purification of recombinant proteins: Application to epitope mapping, preparation of antibodies and structure-function analysis
    • Lefkovits I, Pernis B, editors New York: Academic press
    • Stüber D, Matile H, Garotta G. System for high level production in E. coli and rapid purification of recombinant proteins: application to epitope mapping, preparation of antibodies and structure-function analysis. In: Lefkovits I, Pernis B, editors. Immunological methods. New York: Academic press; 1990. p. 121.
    • (1990) Immunological Methods , pp. 121
    • Stüber, D.1    Matile, H.2    Garotta, G.3
  • 15
    • 0002379321 scopus 로고
    • Analytical methods
    • Darbre A, editor New York: Wiley
    • Darbre A. Analytical methods. In: Darbre A, editor. Practical protein chemistry: a Handbook. New York: Wiley; 1986. p. 227-335.
    • (1986) Practical Protein Chemistry: A Handbook , pp. 227-335
    • Darbre, A.1
  • 17
    • 33646953936 scopus 로고
    • Colorimetric determination of hyaluronidase activity
    • Greif RL. Colorimetric determination of hyaluronidase activity. J Biol Chem 1952;194:619-25.
    • (1952) J Biol Chem , vol.194 , pp. 619-625
    • Greif, R.L.1
  • 19
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970;227:680-5.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.1
  • 20
    • 0019330825 scopus 로고
    • Purification of enzymes by heparin-sepharose affinity chromatography
    • Farooqui AA. Purification of enzymes by heparin-sepharose affinity chromatography. J Chromatography 1980;184:335-45.
    • (1980) J Chromatography , vol.184 , pp. 335-345
    • Farooqui, A.A.1
  • 21
    • 0026100208 scopus 로고
    • Enhanced secretion from insect cells of a foreign protein fused to the honeybee melittin signal peptide
    • Tessier DC, Thomas DY, Khouri HE, Laliberte F, Vernet T. Enhanced secretion from insect cells of a foreign protein fused to the honeybee melittin signal peptide. Gene 1991;98:177-83.
    • (1991) Gene , vol.98 , pp. 177-183
    • Tessier, D.C.1    Thomas, D.Y.2    Khouri, H.E.3    Laliberte, F.4    Vernet, T.5
  • 22
    • 0025000922 scopus 로고
    • Linearization of baculovirus DNA enhances the recovery of recombinant virus expression vectors
    • Kitts PA, Ayres MD, Possee RD. Linearization of baculovirus DNA enhances the recovery of recombinant virus expression vectors. Nucleic Acids Res 1990;18:5667-72.
    • (1990) Nucleic Acids Res , vol.18 , pp. 5667-5672
    • Kitts, P.A.1    Ayres, M.D.2    Possee, R.D.3
  • 23
    • 14744303350 scopus 로고
    • Baculovirus expression of alkaline phosphatase as a reporter gene for evaluation of production, glycosylation and secretion
    • Davis TR, Trotter KM, Granados RR, Wood HA. Baculovirus expression of alkaline phosphatase as a reporter gene for evaluation of production, glycosylation and secretion. Biotechnology 1992;10: 1148-50.
    • (1992) Biotechnology , vol.10 , pp. 1148-1150
    • Davis, T.R.1    Trotter, K.M.2    Granados, R.R.3    Wood, H.A.4
  • 24
    • 0023256289 scopus 로고
    • Monitoring of antibodies in patients on immunotherapy with insect venoms by immunoblotting
    • Einarsson R. Monitoring of antibodies in patients on immunotherapy with insect venoms by immunoblotting. Int Archs Allergy Appl Immunol 1987;83:217-9.
    • (1987) Int Archs Allergy Appl Immunol , vol.83 , pp. 217-219
    • Einarsson, R.1
  • 28
    • 0029776726 scopus 로고    scopus 로고
    • Production of a recombinant imported fire and venom allergen, Sol i 2, in native and immunoreactive form
    • Schmidt M, McConnell TJ, Hoffman DR. Production of a recombinant imported fire and venom allergen, Sol i 2, in native and immunoreactive form. J Allergy Clin Immunol 1996;98:82-8.
    • (1996) J Allergy Clin Immunol , vol.98 , pp. 82-88
    • Schmidt, M.1    McConnell, T.J.2    Hoffman, D.R.3
  • 29
    • 0021010433 scopus 로고
    • Production of human beta Interferon in insect cells infected with a baculovirus expression vector
    • Smith GE, Summers MD, Fraser MJ. Production of human beta Interferon in insect cells infected with a baculovirus expression vector. Mol Cell Biol 1983;3:2156-65.
    • (1983) Mol Cell Biol , vol.3 , pp. 2156-2165
    • Smith, G.E.1    Summers, M.D.2    Fraser, M.J.3
  • 30
    • 0037838073 scopus 로고
    • Modification and secretion of human interleukin 2 produced in insect cells by a baculovirus expression vector
    • Smith GE, Ju G, Ericson BL, Moschera L, Lahm H, Chizzonite R, et al. Modification and secretion of human interleukin 2 produced in insect cells by a baculovirus expression vector. Proc Natl Acad Sci USA 1985;42:8404-8.
    • (1985) Proc Natl Acad Sci USA , vol.42 , pp. 8404-8408
    • Smith, G.E.1    Ju, G.2    Ericson, B.L.3    Moschera, L.4    Lahm, H.5    Chizzonite, R.6
  • 31
    • 0025336176 scopus 로고
    • Oligosaccaride processing in the expression of human plasminogen cDNA by lepidopteran insect (Spodoptera frugiperda) cells
    • Davidson DJ, Fraser MJ, Castellino FJ. Oligosaccaride processing in the expression of human plasminogen cDNA by lepidopteran insect (Spodoptera frugiperda) cells. Biochemistry 1990;29:5584-90.
    • (1990) Biochemistry , vol.29 , pp. 5584-5590
    • Davidson, D.J.1    Fraser, M.J.2    Castellino, F.J.3
  • 32
    • 0027731402 scopus 로고
    • Glycosylation and high-level secretion of human TNF-beta in recombinant baculovirus-infected insect cells
    • Chai H, Vasudevan SG, Porter AG, Chua KL, Oh S, Yap M. Glycosylation and high-level secretion of human TNF-beta in recombinant baculovirus-infected insect cells. Biotechnol Appl Biochem 1993;18:259-73.
    • (1993) Biotechnol Appl Biochem , vol.18 , pp. 259-273
    • Chai, H.1    Vasudevan, S.G.2    Porter, A.G.3    Chua, K.L.4    Oh, S.5    Yap, M.6
  • 33
    • 0020363515 scopus 로고
    • Preferential codon usage in prokaryotic genes: The optimal codon-anticodon interaction energy and the selective codon usage in efficiently expressed genes
    • Grosjean H, Fiers W. Preferential codon usage in prokaryotic genes: the optimal codon-anticodon interaction energy and the selective codon usage in efficiently expressed genes. Gene 1982; 18:199-209.
    • (1982) Gene , vol.18 , pp. 199-209
    • Grosjean, H.1    Fiers, W.2
  • 34
    • 0028117390 scopus 로고
    • Structural analysis and localization of the carbohydrate moieties of a soluble human Interferon gamma receptor produced in baculovirus-infected insect cells
    • Manneberg M, Friedlein A, Kurth H, Lahm HW, Fountoulakis M. Structural analysis and localization of the carbohydrate moieties of a soluble human Interferon gamma receptor produced in baculovirus-infected insect cells. Protein Sci 1994;3:30-8.
    • (1994) Protein Sci , vol.3 , pp. 30-38
    • Manneberg, M.1    Friedlein, A.2    Kurth, H.3    Lahm, H.W.4    Fountoulakis, M.5
  • 35
    • 0027381117 scopus 로고
    • Expression of human Interferon 1 in Sf9 cells. No evidence for complex-type N-linked glycosylation or sialylation
    • Voss T, Ergülen E, Ahorn H, Kubelka V, Sugiyama K, Maurer-Fogy I, et al. Expression of human Interferon 1 in Sf9 cells. No evidence for complex-type N-linked glycosylation or sialylation. Eur J Biochem 1993;217:913-9.
    • (1993) Eur J Biochem , vol.217 , pp. 913-919
    • Voss, T.1    Ergülen, E.2    Ahorn, H.3    Kubelka, V.4    Sugiyama, K.5    Maurer-Fogy, I.6
  • 36
    • 0027508349 scopus 로고
    • Site-specific N-glycosylation and oligosaccharide structures of recombinant HIV-1 gp120 derived from a baculovirus expression system
    • Yeh JC, Seals JR, Murphy CI, van Halbeek H, Cummings RD. Site-specific N-glycosylation and oligosaccharide structures of recombinant HIV-1 gp120 derived from a baculovirus expression system. Biochemistry 1993;32:11087-99.
    • (1993) Biochemistry , vol.32 , pp. 11087-11099
    • Yeh, J.C.1    Seals, J.R.2    Murphy, C.I.3    Van Halbeek, H.4    Cummings, R.D.5
  • 37
    • 0029904281 scopus 로고    scopus 로고
    • Influence of the carbohydrate moiety on the stability of glycoproteins
    • Wang Ch, Eufemi M, Turano C, Giartosio A. Influence of the carbohydrate moiety on the stability of glycoproteins. Biochemistry 1996;35:7299-307.
    • (1996) Biochemistry , vol.35 , pp. 7299-7307
    • Wang, Ch.1    Eufemi, M.2    Turano, C.3    Giartosio, A.4
  • 38
    • 0027519943 scopus 로고
    • Protein glycosylation: Structural and functional aspects
    • Lis H, Sharon N. Protein glycosylation: structural and functional aspects. Eur J Biochem 1993;218:1-27.
    • (1993) Eur J Biochem , vol.218 , pp. 1-27
    • Lis, H.1    Sharon, N.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.