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Volumn 47, Issue 4, 2010, Pages 799-808

Dissecting cross-reactivity in hymenoptera venom allergy by circumvention of α-1,3-core fucosylation

Author keywords

Carbohydrates; Cross reactivity; Hyaluronidases; IgE; Venom allergy

Indexed keywords

BEE VENOM; CARBOHYDRATE; FETUIN A; GLYCOPROTEIN; HYALURONIDASE; HYMENOPTERA VENOM; IMMUNOGLOBULIN E; PHOSPHOLIPASE A1;

EID: 72949087521     PISSN: 01615890     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molimm.2009.10.005     Document Type: Article
Times cited : (99)

References (76)
  • 1
    • 0034995912 scopus 로고    scopus 로고
    • Cross-reactivity of IgE antibodies to allergens
    • Aalberse R.C., Akkerdaas J., and van Ree R. Cross-reactivity of IgE antibodies to allergens. Allergy 56 (2001) 478-490
    • (2001) Allergy , vol.56 , pp. 478-490
    • Aalberse, R.C.1    Akkerdaas, J.2    van Ree, R.3
  • 2
    • 0019859015 scopus 로고
    • Immunoglobulin E antibodies that crossreact with vegetable foods, pollen, and Hymenoptera venom
    • Aalberse R.C., Koshte V., and Clemens J.G. Immunoglobulin E antibodies that crossreact with vegetable foods, pollen, and Hymenoptera venom. J. Allergy Clin. Immunol. 68 (1981) 356-364
    • (1981) J. Allergy Clin. Immunol. , vol.68 , pp. 356-364
    • Aalberse, R.C.1    Koshte, V.2    Clemens, J.G.3
  • 3
    • 0032848027 scopus 로고    scopus 로고
    • Insect cells as hosts for the expression of recombinant glycoproteins
    • Altmann F., Staudacher E., Wilson I.B., and Marz L. Insect cells as hosts for the expression of recombinant glycoproteins. Glycoconjugate J. 16 (1999) 109-123
    • (1999) Glycoconjugate J. , vol.16 , pp. 109-123
    • Altmann, F.1    Staudacher, E.2    Wilson, I.B.3    Marz, L.4
  • 4
    • 0017721398 scopus 로고
    • High resolution two-dimensional electrophoresis of human plasma proteins
    • Anderson L., and Anderson N.G. High resolution two-dimensional electrophoresis of human plasma proteins. Proc. Natl. Acad. Sci. U.S.A. 74 (1977) 5421-5425
    • (1977) Proc. Natl. Acad. Sci. U.S.A. , vol.74 , pp. 5421-5425
    • Anderson, L.1    Anderson, N.G.2
  • 5
    • 84990468023 scopus 로고
    • Allergenic potency of bee antigens measured by RAST inhibition
    • Arbesman C.E., Reisman R.E., and Wypych J.I. Allergenic potency of bee antigens measured by RAST inhibition. Clin. Allergy 6 (1976) 587-595
    • (1976) Clin. Allergy , vol.6 , pp. 587-595
    • Arbesman, C.E.1    Reisman, R.E.2    Wypych, J.I.3
  • 7
    • 0038495798 scopus 로고    scopus 로고
    • Fucose: biosynthesis and biological function in mammals
    • Becker D.J., and Lowe J.B. Fucose: biosynthesis and biological function in mammals. Glycobiology 13 (2003) 41R-53R
    • (2003) Glycobiology , vol.13
    • Becker, D.J.1    Lowe, J.B.2
  • 8
    • 2942606516 scopus 로고    scopus 로고
    • Specificity of IgG and IgE antibodies against plant and insect glycoprotein glycans determined with artificial glycoforms of human transferrin
    • Bencurova M., Hemmer W., Focke-Tejkl M., Wilson I.B., and Altmann F. Specificity of IgG and IgE antibodies against plant and insect glycoprotein glycans determined with artificial glycoforms of human transferrin. Glycobiology 14 (2004) 457-466
    • (2004) Glycobiology , vol.14 , pp. 457-466
    • Bencurova, M.1    Hemmer, W.2    Focke-Tejkl, M.3    Wilson, I.B.4    Altmann, F.5
  • 9
    • 72949106361 scopus 로고    scopus 로고
    • Identification, recombinant expression and characterization of 100 kDa high molecular weight hymenoptera venom allergens
    • Submitted for publication
    • Blank S., Seismann, H., Bockisch, B., Braren, I., Cifuentes, L., Rühl, D., Bredehorst, R., Ollert, M.W., Grunwald, T., Spillner, E., 2008. Identification, recombinant expression and characterization of 100 kDa high molecular weight hymenoptera venom allergens. Submitted for publication.
    • (2008)
    • Blank, S.1    Seismann, H.2    Bockisch, B.3    Braren, I.4    Cifuentes, L.5    Rühl, D.6    Bredehorst, R.7    Ollert, M.W.8    Grunwald, T.9    Spillner, E.10
  • 10
    • 0019470313 scopus 로고
    • Steps in the biosynthesis of mosquito cell membrane glycoproteins and the effects of tunicamycin
    • Butters T.D., Hughes R.C., and Vischer P. Steps in the biosynthesis of mosquito cell membrane glycoproteins and the effects of tunicamycin. Biochim. Biophys. Acta 640 (1981) 672-686
    • (1981) Biochim. Biophys. Acta , vol.640 , pp. 672-686
    • Butters, T.D.1    Hughes, R.C.2    Vischer, P.3
  • 12
    • 14744303350 scopus 로고
    • Baculovirus expression of alkaline phosphatase as a reporter gene for evaluation of production, glycosylation and secretion
    • Davis T.R., Trotter K.M., Granados R.R., and Wood H.A. Baculovirus expression of alkaline phosphatase as a reporter gene for evaluation of production, glycosylation and secretion. Biotechnology (NY) 10 (1992) 1148-1150
    • (1992) Biotechnology (NY) , vol.10 , pp. 1148-1150
    • Davis, T.R.1    Trotter, K.M.2    Granados, R.R.3    Wood, H.A.4
  • 13
    • 0033105027 scopus 로고    scopus 로고
    • Use of mannosamine for inducing the addition of outer arm N-acetylglucosamine onto N-linked oligosaccharides of recombinant proteins in insect cells
    • Donaldson M., Wood H.A., Kulakosky P.C., and Shuler M.L. Use of mannosamine for inducing the addition of outer arm N-acetylglucosamine onto N-linked oligosaccharides of recombinant proteins in insect cells. Biotechnol. Prog. 15 (1999) 168-173
    • (1999) Biotechnol. Prog. , vol.15 , pp. 168-173
    • Donaldson, M.1    Wood, H.A.2    Kulakosky, P.C.3    Shuler, M.L.4
  • 15
    • 0031962745 scopus 로고    scopus 로고
    • The frequency and clinical significance of specific IgE to both wasp (Vespula) and honey-bee (Apis) venoms in the same patient
    • Egner W., Ward C., Brown D.L., and Ewan P.W. The frequency and clinical significance of specific IgE to both wasp (Vespula) and honey-bee (Apis) venoms in the same patient. Clin. Exp. Allergy 28 (1998) 26-34
    • (1998) Clin. Exp. Allergy , vol.28 , pp. 26-34
    • Egner, W.1    Ward, C.2    Brown, D.L.3    Ewan, P.W.4
  • 16
    • 0032502896 scopus 로고    scopus 로고
    • Structures of the Erythrina corallodendron lectin and of its complexes with mono- and disaccharides
    • Elgavish S., and Shaanan B. Structures of the Erythrina corallodendron lectin and of its complexes with mono- and disaccharides. J. Mol. Biol. 277 (1998) 917-932
    • (1998) J. Mol. Biol. , vol.277 , pp. 917-932
    • Elgavish, S.1    Shaanan, B.2
  • 17
    • 0035958916 scopus 로고    scopus 로고
    • Identification of core alpha 1,3-fucosylated glycans and cloning of the requisite fucosyltransferase cDNA from Drosophila melanogaster. Potential basis of the neural anti-horseadish peroxidase epitope
    • Fabini G., Freilinger A., Altmann F., and Wilson I.B. Identification of core alpha 1,3-fucosylated glycans and cloning of the requisite fucosyltransferase cDNA from Drosophila melanogaster. Potential basis of the neural anti-horseadish peroxidase epitope. J. Biol. Chem. 276 (2001) 28058-28067
    • (2001) J. Biol. Chem. , vol.276 , pp. 28058-28067
    • Fabini, G.1    Freilinger, A.2    Altmann, F.3    Wilson, I.B.4
  • 18
    • 0027453187 scopus 로고
    • Affinity purification of antibodies specific for Asn-linked glycans containing alpha 1 → 3 fucose or beta 1 → 2 xylose
    • Faye L., Gomord V., Fitchette-Laine A.C., and Chrispeels M.J. Affinity purification of antibodies specific for Asn-linked glycans containing alpha 1 → 3 fucose or beta 1 → 2 xylose. Anal. Biochem. 209 (1993) 104-108
    • (1993) Anal. Biochem. , vol.209 , pp. 104-108
    • Faye, L.1    Gomord, V.2    Fitchette-Laine, A.C.3    Chrispeels, M.J.4
  • 19
    • 0344631775 scopus 로고    scopus 로고
    • Involvement of carbohydrate epitopes in the IgE response of celery-allergic patients
    • Fotisch K., Altmann F., Haustein D., and Vieths S. Involvement of carbohydrate epitopes in the IgE response of celery-allergic patients. Int. Arch. Allergy Immunol. 120 (1999) 30-42
    • (1999) Int. Arch. Allergy Immunol. , vol.120 , pp. 30-42
    • Fotisch, K.1    Altmann, F.2    Haustein, D.3    Vieths, S.4
  • 21
    • 0027520896 scopus 로고
    • Bee venom hyaluronidase is homologous to a membrane protein of mammalian sperm
    • Gmachl M., and Kreil G. Bee venom hyaluronidase is homologous to a membrane protein of mammalian sperm. Proc. Natl. Acad. Sci. U.S.A. 90 (1993) 3569-3573
    • (1993) Proc. Natl. Acad. Sci. U.S.A. , vol.90 , pp. 3569-3573
    • Gmachl, M.1    Kreil, G.2
  • 22
  • 25
    • 1642391757 scopus 로고    scopus 로고
    • Identification by immunoblot of venom glycoproteins displaying immunoglobulin E-binding N-glycans as cross-reactive allergens in honeybee and yellow jacket venom
    • Hemmer W., Focke M., Kolarich D., Dalik I., Gotz M., and Jarisch R. Identification by immunoblot of venom glycoproteins displaying immunoglobulin E-binding N-glycans as cross-reactive allergens in honeybee and yellow jacket venom. Clin. Exp. Allergy 34 (2004) 460-469
    • (2004) Clin. Exp. Allergy , vol.34 , pp. 460-469
    • Hemmer, W.1    Focke, M.2    Kolarich, D.3    Dalik, I.4    Gotz, M.5    Jarisch, R.6
  • 26
    • 0035217040 scopus 로고    scopus 로고
    • Antibody binding to venom carbohydrates is a frequent cause for double positivity to honeybee and yellow jacket venom in patients with stinging-insect allergy
    • Hemmer W., Focke M., Kolarich D., Wilson I.B., Altmann F., Wohrl S., Gotz M., and Jarisch R. Antibody binding to venom carbohydrates is a frequent cause for double positivity to honeybee and yellow jacket venom in patients with stinging-insect allergy. J. Allergy Clin. Immunol. 108 (2001) 1045-1052
    • (2001) J. Allergy Clin. Immunol. , vol.108 , pp. 1045-1052
    • Hemmer, W.1    Focke, M.2    Kolarich, D.3    Wilson, I.B.4    Altmann, F.5    Wohrl, S.6    Gotz, M.7    Jarisch, R.8
  • 27
    • 0035576365 scopus 로고    scopus 로고
    • Major venom allergen of yellow jackets, Ves v 5: structural characterization of a pathogenesis-related protein superfamily
    • Henriksen A., King T.P., Mirza O., Monsalve R.I., Meno K., Ipsen H., Larsen J.N., Gajhede M., and Spangfort M.D. Major venom allergen of yellow jackets, Ves v 5: structural characterization of a pathogenesis-related protein superfamily. Proteins 45 (2001) 438-448
    • (2001) Proteins , vol.45 , pp. 438-448
    • Henriksen, A.1    King, T.P.2    Mirza, O.3    Monsalve, R.I.4    Meno, K.5    Ipsen, H.6    Larsen, J.N.7    Gajhede, M.8    Spangfort, M.D.9
  • 28
    • 14844312386 scopus 로고    scopus 로고
    • Sol i 1, the phospholipase allergen of imported fire ant venom
    • Hoffman D.R., Sakell R.H., and Schmidt M. Sol i 1, the phospholipase allergen of imported fire ant venom. J. Allergy Clin. Immunol. 115 (2005) 611-616
    • (2005) J. Allergy Clin. Immunol. , vol.115 , pp. 611-616
    • Hoffman, D.R.1    Sakell, R.H.2    Schmidt, M.3
  • 29
    • 2242455924 scopus 로고    scopus 로고
    • Engineering the protein N-glycosylation pathway in insect cells for production of biantennary, complex N-glycans
    • Hollister J., Grabenhorst E., Nimtz M., Conradt H., and Jarvis D.L. Engineering the protein N-glycosylation pathway in insect cells for production of biantennary, complex N-glycans. Biochemistry 41 (2002) 15093-15104
    • (2002) Biochemistry , vol.41 , pp. 15093-15104
    • Hollister, J.1    Grabenhorst, E.2    Nimtz, M.3    Conradt, H.4    Jarvis, D.L.5
  • 30
    • 0033526537 scopus 로고    scopus 로고
    • Constraints on the transport and glycosylation of recombinant IFN-gamma in Chinese hamster ovary and insect cells
    • Hooker A.D., Green N.H., Baines A.J., Bull A.T., Jenkins N., Strange P.G., and James D.C. Constraints on the transport and glycosylation of recombinant IFN-gamma in Chinese hamster ovary and insect cells. Biotechnol. Bioeng. 63 (1999) 559-572
    • (1999) Biotechnol. Bioeng. , vol.63 , pp. 559-572
    • Hooker, A.D.1    Green, N.H.2    Baines, A.J.3    Bull, A.T.4    Jenkins, N.5    Strange, P.G.6    James, D.C.7
  • 31
    • 33748307416 scopus 로고    scopus 로고
    • In vitro hymenoptera venom allergy diagnosis: improved by screening for cross-reactive carbohydrate determinants and reciprocal inhibition
    • Jappe U., Raulf-Heimsoth M., Hoffmann M., Burow G., Hubsch-Muller C., and Enk A. In vitro hymenoptera venom allergy diagnosis: improved by screening for cross-reactive carbohydrate determinants and reciprocal inhibition. Allergy 61 (2006) 1220-1229
    • (2006) Allergy , vol.61 , pp. 1220-1229
    • Jappe, U.1    Raulf-Heimsoth, M.2    Hoffmann, M.3    Burow, G.4    Hubsch-Muller, C.5    Enk, A.6
  • 32
    • 0032190659 scopus 로고    scopus 로고
    • Engineering N-glycosylation pathways in the baculovirus-insect cell system
    • Jarvis D.L., Kawar Z.S., and Hollister J.R. Engineering N-glycosylation pathways in the baculovirus-insect cell system. Curr. Opin. Biotechnol. 9 (1998) 528-533
    • (1998) Curr. Opin. Biotechnol. , vol.9 , pp. 528-533
    • Jarvis, D.L.1    Kawar, Z.S.2    Hollister, J.R.3
  • 33
    • 38149058818 scopus 로고    scopus 로고
    • Affinity of IgE and IgG against cross-reactive carbohydrate determinants on plant and insect glycoproteins
    • e2
    • Jin C., Hantusch B., Hemmer W., Stadlmann J., and Altmann F. Affinity of IgE and IgG against cross-reactive carbohydrate determinants on plant and insect glycoproteins. J. Allergy Clin. Immunol. 121 (2008) 185-190 e2
    • (2008) J. Allergy Clin. Immunol. , vol.121 , pp. 185-190
    • Jin, C.1    Hantusch, B.2    Hemmer, W.3    Stadlmann, J.4    Altmann, F.5
  • 34
    • 3042691090 scopus 로고    scopus 로고
    • Carbohydrate-mediated cell adhesion in cancer metastasis and angiogenesis
    • Kannagi R., Izawa M., Koike T., Miyazaki K., and Kimura N. Carbohydrate-mediated cell adhesion in cancer metastasis and angiogenesis. Cancer Sci. 95 (2004) 377-384
    • (2004) Cancer Sci. , vol.95 , pp. 377-384
    • Kannagi, R.1    Izawa, M.2    Koike, T.3    Miyazaki, K.4    Kimura, N.5
  • 35
    • 0029911048 scopus 로고    scopus 로고
    • Yellow jacket venom allergens, hyaluronidase and phospholipase: sequence similarity and antigenic cross-reactivity with their hornet and wasp homologs and possible implications for clinical allergy
    • King T.P., Lu G., Gonzalez M., Qian N., and Soldatova L. Yellow jacket venom allergens, hyaluronidase and phospholipase: sequence similarity and antigenic cross-reactivity with their hornet and wasp homologs and possible implications for clinical allergy. J. Allergy Clin. Immunol. 98 (1996) 588-600
    • (1996) J. Allergy Clin. Immunol. , vol.98 , pp. 588-600
    • King, T.P.1    Lu, G.2    Gonzalez, M.3    Qian, N.4    Soldatova, L.5
  • 37
    • 0033759739 scopus 로고    scopus 로고
    • Structure and biology of stinging insect venom allergens
    • King T.P., and Spangfort M.D. Structure and biology of stinging insect venom allergens. Int. Arch. Allergy Immunol. 123 (2000) 99-106
    • (2000) Int. Arch. Allergy Immunol. , vol.123 , pp. 99-106
    • King, T.P.1    Spangfort, M.D.2
  • 38
    • 17744384039 scopus 로고    scopus 로고
    • Prevalence and clinical relevance of specific immunoglobulin E to pollen caused by sting-induced specific immunoglobulin E to cross-reacting carbohydrate determinants in Hymenoptera venoms
    • Kochuyt A.M., Van Hoeyveld E.M., and Stevens E.A. Prevalence and clinical relevance of specific immunoglobulin E to pollen caused by sting-induced specific immunoglobulin E to cross-reacting carbohydrate determinants in Hymenoptera venoms. Clin. Exp. Allergy 35 (2005) 441-447
    • (2005) Clin. Exp. Allergy , vol.35 , pp. 441-447
    • Kochuyt, A.M.1    Van Hoeyveld, E.M.2    Stevens, E.A.3
  • 39
    • 27144480341 scopus 로고    scopus 로고
    • The N-glycans of yellow jacket venom hyaluronidases and the protein sequence of its major isoform in Vespula vulgaris
    • Kolarich D., Leonard R., Hemmer W., and Altmann F. The N-glycans of yellow jacket venom hyaluronidases and the protein sequence of its major isoform in Vespula vulgaris. Febs J. 272 (2005) 5182-5190
    • (2005) Febs J. , vol.272 , pp. 5182-5190
    • Kolarich, D.1    Leonard, R.2    Hemmer, W.3    Altmann, F.4
  • 40
    • 0028915061 scopus 로고
    • The asparagine-linked carbohydrate of honeybee venom hyaluronidase
    • Kubelka V., Altmann F., and Marz L. The asparagine-linked carbohydrate of honeybee venom hyaluronidase. Glycoconjugate J. 12 (1995) 77-83
    • (1995) Glycoconjugate J. , vol.12 , pp. 77-83
    • Kubelka, V.1    Altmann, F.2    Marz, L.3
  • 42
    • 0024726507 scopus 로고
    • Analysis of the cDNA for phospholipase A2 from honeybee venom glands. The deduced amino acid sequence reveals homology to the corresponding vertebrate enzymes
    • Kuchler K., Gmachl M., Sippl M.J., and Kreil G. Analysis of the cDNA for phospholipase A2 from honeybee venom glands. The deduced amino acid sequence reveals homology to the corresponding vertebrate enzymes. Eur. J. Biochem. 184 (1989) 249-254
    • (1989) Eur. J. Biochem. , vol.184 , pp. 249-254
    • Kuchler, K.1    Gmachl, M.2    Sippl, M.J.3    Kreil, G.4
  • 43
    • 0025797046 scopus 로고
    • The structure of a neural specific carbohydrate epitope of horseradish peroxidase recognized by anti-horseradish peroxidase antiserum
    • Kurosaka A., Yano A., Itoh N., Kuroda Y., Nakagawa T., and Kawasaki T. The structure of a neural specific carbohydrate epitope of horseradish peroxidase recognized by anti-horseradish peroxidase antiserum. J. Biol. Chem. 266 (1991) 4168-4172
    • (1991) J. Biol. Chem. , vol.266 , pp. 4168-4172
    • Kurosaka, A.1    Yano, A.2    Itoh, N.3    Kuroda, Y.4    Nakagawa, T.5    Kawasaki, T.6
  • 45
    • 18744416937 scopus 로고    scopus 로고
    • IgE-reactive carbohydrate epitopes-classification, cross-reactivity, and clinical impact
    • Malandain H. IgE-reactive carbohydrate epitopes-classification, cross-reactivity, and clinical impact. Eur. Ann. Allergy Clin. Immunol. 37 (2005) 122-128
    • (2005) Eur. Ann. Allergy Clin. Immunol. , vol.37 , pp. 122-128
    • Malandain, H.1
  • 46
    • 45149085609 scopus 로고    scopus 로고
    • Evaluation by double-blind placebo-controlled oral challenge of the clinical relevance of IgE antibodies against plant glycans
    • Mari A., Ooievaar-de Heer P., Scala E., Giani M., Pirrotta L., Zuidmeer L., Bethell D., and van Ree R. Evaluation by double-blind placebo-controlled oral challenge of the clinical relevance of IgE antibodies against plant glycans. Allergy 63 (2008) 891-896
    • (2008) Allergy , vol.63 , pp. 891-896
    • Mari, A.1    Ooievaar-de Heer, P.2    Scala, E.3    Giani, M.4    Pirrotta, L.5    Zuidmeer, L.6    Bethell, D.7    van Ree, R.8
  • 48
    • 0032508502 scopus 로고    scopus 로고
    • Quantitation of hyaluronidases by the Morgan-Elson reaction: comparison of the enzyme activities in the plasma of tumor patients and healthy volunteers
    • Muckenschnabel I., Bernhardt G., Spruss T., Dietl B., and Buschauer A. Quantitation of hyaluronidases by the Morgan-Elson reaction: comparison of the enzyme activities in the plasma of tumor patients and healthy volunteers. Cancer Lett. 131 (1998) 13-20
    • (1998) Cancer Lett. , vol.131 , pp. 13-20
    • Muckenschnabel, I.1    Bernhardt, G.2    Spruss, T.3    Dietl, B.4    Buschauer, A.5
  • 49
    • 0026505753 scopus 로고
    • Immunotherapy with honeybee venom and yellow jacket venom is different regarding efficacy and safety
    • Muller U., Helbling A., and Berchtold E. Immunotherapy with honeybee venom and yellow jacket venom is different regarding efficacy and safety. J. Allergy Clin. Immunol. 89 (1992) 529-535
    • (1992) J. Allergy Clin. Immunol. , vol.89 , pp. 529-535
    • Muller, U.1    Helbling, A.2    Berchtold, E.3
  • 50
    • 0036095653 scopus 로고    scopus 로고
    • Recombinant Hymenoptera venom allergens
    • Muller U.R. Recombinant Hymenoptera venom allergens. Allergy 57 (2002) 570-576
    • (2002) Allergy , vol.57 , pp. 570-576
    • Muller, U.R.1
  • 51
    • 17744410662 scopus 로고    scopus 로고
    • Recent developments and future strategies for immunotherapy of insect venom allergy
    • Muller U.R. Recent developments and future strategies for immunotherapy of insect venom allergy. Curr. Opin. Allergy Clin. Immunol. 3 (2003) 299-303
    • (2003) Curr. Opin. Allergy Clin. Immunol. , vol.3 , pp. 299-303
    • Muller, U.R.1
  • 55
    • 0001513835 scopus 로고
    • Fetuin, a new globulin isolated from serum
    • Pedersen K.O. Fetuin, a new globulin isolated from serum. Nature (1944) 575
    • (1944) Nature , pp. 575
    • Pedersen, K.O.1
  • 56
    • 0026691179 scopus 로고
    • The antigenicity of the carbohydrate moiety of an insect glycoprotein, honey-bee (Apis mellifera) venom phospholipase A2. The role of alpha 1,3-fucosylation of the asparagine-bound N-acetylglucosamine
    • Prenner C., Mach L., Glossl J., and Marz L. The antigenicity of the carbohydrate moiety of an insect glycoprotein, honey-bee (Apis mellifera) venom phospholipase A2. The role of alpha 1,3-fucosylation of the asparagine-bound N-acetylglucosamine. Biochem. J. 284 Pt 2 (1992) 377-380
    • (1992) Biochem. J. , vol.284 , Issue.PART 2 , pp. 377-380
    • Prenner, C.1    Mach, L.2    Glossl, J.3    Marz, L.4
  • 57
    • 77049251255 scopus 로고
    • A modified colorimetric method for the estimation of N-acetylamino sugars
    • Reissig J.L., Storminger J.L., and Leloir L.F. A modified colorimetric method for the estimation of N-acetylamino sugars. J. Biol. Chem. 217 (1955) 959-966
    • (1955) J. Biol. Chem. , vol.217 , pp. 959-966
    • Reissig, J.L.1    Storminger, J.L.2    Leloir, L.F.3
  • 59
    • 33846949412 scopus 로고    scopus 로고
    • Towards abolition of immunogenic structures in insect cells: characterization of a honey-bee (Apis mellifera) multi-gene family reveals both an allergy-related core alpha1,3-fucosyltransferase and the first insect Lewis-histo-blood-group-related antigen-synthesizing enzyme
    • Rendic D., Klaudiny J., Stemmer U., Schmidt J., Paschinger K., and Wilson I.B. Towards abolition of immunogenic structures in insect cells: characterization of a honey-bee (Apis mellifera) multi-gene family reveals both an allergy-related core alpha1,3-fucosyltransferase and the first insect Lewis-histo-blood-group-related antigen-synthesizing enzyme. Biochem. J. 402 (2007) 105-115
    • (2007) Biochem. J. , vol.402 , pp. 105-115
    • Rendic, D.1    Klaudiny, J.2    Stemmer, U.3    Schmidt, J.4    Paschinger, K.5    Wilson, I.B.6
  • 60
    • 0026596843 scopus 로고
    • Occurrence of sialic acids in Drosophila melanogaster
    • Roth J., Kempf A., Reuter G., Schauer R., and Gehring W.J. Occurrence of sialic acids in Drosophila melanogaster. Science 256 (1992) 673-675
    • (1992) Science , vol.256 , pp. 673-675
    • Roth, J.1    Kempf, A.2    Reuter, G.3    Schauer, R.4    Gehring, W.J.5
  • 61
    • 0029884624 scopus 로고    scopus 로고
    • The sting challenge test in Hymenoptera venom allergy. Position paper of the Subcommittee on Insect Venom Allergy of the European Academy of Allergology and Clinical Immunology
    • Rueff F., Przybilla B., Muller U., and Mosbech H. The sting challenge test in Hymenoptera venom allergy. Position paper of the Subcommittee on Insect Venom Allergy of the European Academy of Allergology and Clinical Immunology. Allergy 51 (1996) 216-225
    • (1996) Allergy , vol.51 , pp. 216-225
    • Rueff, F.1    Przybilla, B.2    Muller, U.3    Mosbech, H.4
  • 62
    • 0022559251 scopus 로고
    • Expression of Lewisa, Lewisb, X, and Y blood group antigens in human colonic tumors and normal tissue and in human tumor-derived cell lines
    • Sakamoto J., Furukawa K., Cordon-Cardo C., Yin B.W., Rettig W.J., Oettgen H.F., Old L.J., and Lloyd K.O. Expression of Lewisa, Lewisb, X, and Y blood group antigens in human colonic tumors and normal tissue and in human tumor-derived cell lines. Cancer Res. 46 (1986) 1553-1561
    • (1986) Cancer Res. , vol.46 , pp. 1553-1561
    • Sakamoto, J.1    Furukawa, K.2    Cordon-Cardo, C.3    Yin, B.W.4    Rettig, W.J.5    Oettgen, H.F.6    Old, L.J.7    Lloyd, K.O.8
  • 63
    • 0025668794 scopus 로고
    • Crystal structure of bee-venom phospholipase A2 in a complex with a transition-state analogue
    • Scott D.L., Otwinowski Z., Gelb M.H., and Sigler P.B. Crystal structure of bee-venom phospholipase A2 in a complex with a transition-state analogue. Science 250 (1990) 1563-1566
    • (1990) Science , vol.250 , pp. 1563-1566
    • Scott, D.L.1    Otwinowski, Z.2    Gelb, M.H.3    Sigler, P.B.4
  • 64
    • 67349283491 scopus 로고    scopus 로고
    • Structural and immunological characterization of the N-glycans from the major yellow jacket allergen Ves v 2: the N-glycan structures are needed for the human antibody recognition
    • Seppala U., Selby D., Monsalve R., King T.P., Ebner C., Roepstorff P., and Bohle B. Structural and immunological characterization of the N-glycans from the major yellow jacket allergen Ves v 2: the N-glycan structures are needed for the human antibody recognition. Mol. Immunol. 46 (2009) 2014-2021
    • (2009) Mol. Immunol. , vol.46 , pp. 2014-2021
    • Seppala, U.1    Selby, D.2    Monsalve, R.3    King, T.P.4    Ebner, C.5    Roepstorff, P.6    Bohle, B.7
  • 65
    • 0026337737 scopus 로고
    • Structure of a legume lectin with an ordered N-linked carbohydrate in complex with lactose
    • Shaanan B., Lis H., and Sharon N. Structure of a legume lectin with an ordered N-linked carbohydrate in complex with lactose. Science 254 (1991) 862-866
    • (1991) Science , vol.254 , pp. 862-866
    • Shaanan, B.1    Lis, H.2    Sharon, N.3
  • 67
    • 0031982094 scopus 로고    scopus 로고
    • Superior biologic activity of the recombinant bee venom allergen hyaluronidase expressed in baculovirus-infected insect cells as compared with Escherichia coli
    • Soldatova L.N., Crameri R., Gmachl M., Kemeny D.M., Schmidt M., Weber M., and Mueller U.R. Superior biologic activity of the recombinant bee venom allergen hyaluronidase expressed in baculovirus-infected insect cells as compared with Escherichia coli. J. Allergy Clin. Immunol. 101 (1998) 691-698
    • (1998) J. Allergy Clin. Immunol. , vol.101 , pp. 691-698
    • Soldatova, L.N.1    Crameri, R.2    Gmachl, M.3    Kemeny, D.M.4    Schmidt, M.5    Weber, M.6    Mueller, U.R.7
  • 68
    • 0026734854 scopus 로고
    • Distinct N-glycan fucosylation potentials of three lepidopteran cell lines
    • Staudacher E., Kubelka V., and Marz L. Distinct N-glycan fucosylation potentials of three lepidopteran cell lines. Eur. J. Biochem. 207 (1992) 987-993
    • (1992) Eur. J. Biochem. , vol.207 , pp. 987-993
    • Staudacher, E.1    Kubelka, V.2    Marz, L.3
  • 69
    • 0037234667 scopus 로고    scopus 로고
    • Complex-type biantennary N-glycans of recombinant human transferrin from Trichoplusia ni insect cells expressing mammalian [beta]-1,4-galactosyltransferase and [beta]-1,2-N-acetylglucosaminyltransferase II
    • Tomiya N., Howe D., Aumiller J.J., Pathak M., Park J., Palter K.B., Jarvis D.L., Betenbaugh M.J., and Lee Y.C. Complex-type biantennary N-glycans of recombinant human transferrin from Trichoplusia ni insect cells expressing mammalian [beta]-1,4-galactosyltransferase and [beta]-1,2-N-acetylglucosaminyltransferase II. Glycobiology 13 (2003) 23-34
    • (2003) Glycobiology , vol.13 , pp. 23-34
    • Tomiya, N.1    Howe, D.2    Aumiller, J.J.3    Pathak, M.4    Park, J.5    Palter, K.B.6    Jarvis, D.L.7    Betenbaugh, M.J.8    Lee, Y.C.9
  • 70
    • 7244254552 scopus 로고    scopus 로고
    • Comparing N-glycan processing in mammalian cell lines to native and engineered lepidopteran insect cell lines
    • Tomiya N., Narang S., Lee Y.C., and Betenbaugh M.J. Comparing N-glycan processing in mammalian cell lines to native and engineered lepidopteran insect cell lines. Glycoconjugate J. 21 (2004) 343-360
    • (2004) Glycoconjugate J. , vol.21 , pp. 343-360
    • Tomiya, N.1    Narang, S.2    Lee, Y.C.3    Betenbaugh, M.J.4
  • 71
    • 0027426870 scopus 로고
    • Fucose alpha 1,3-linked to the core region of glycoprotein N-glycans creates an important epitope for IgE from honeybee venom allergic individuals
    • Tretter V., Altmann F., Kubelka V., Marz L., and Becker W.M. Fucose alpha 1,3-linked to the core region of glycoprotein N-glycans creates an important epitope for IgE from honeybee venom allergic individuals. Int. Arch. Allergy Immunol. 102 (1993) 259-266
    • (1993) Int. Arch. Allergy Immunol. , vol.102 , pp. 259-266
    • Tretter, V.1    Altmann, F.2    Kubelka, V.3    Marz, L.4    Becker, W.M.5
  • 72
    • 0017475358 scopus 로고
    • The establishment of two cell lines from the insect Spodoptera frugiperda (Lepidoptera; Noctuidae)
    • Vaughn J.L., Goodwin R.H., Tompkins G.J., and McCawley P. The establishment of two cell lines from the insect Spodoptera frugiperda (Lepidoptera; Noctuidae). In Vitro 13 (1977) 213-217
    • (1977) In Vitro , vol.13 , pp. 213-217
    • Vaughn, J.L.1    Goodwin, R.H.2    Tompkins, G.J.3    McCawley, P.4
  • 73
    • 0027381117 scopus 로고
    • Expression of human interferon omega 1 in Sf9 cells. No evidence for complex-type N-linked glycosylation or sialylation
    • Voss T., Ergulen E., Ahorn H., Kubelka V., Sugiyama K., Maurer-Fogy I., and Glossl J. Expression of human interferon omega 1 in Sf9 cells. No evidence for complex-type N-linked glycosylation or sialylation. Eur. J. Biochem. 217 (1993) 913-919
    • (1993) Eur. J. Biochem. , vol.217 , pp. 913-919
    • Voss, T.1    Ergulen, E.2    Ahorn, H.3    Kubelka, V.4    Sugiyama, K.5    Maurer-Fogy, I.6    Glossl, J.7
  • 74
    • 0029933189 scopus 로고    scopus 로고
    • Elongation of the N-glycans of fowl plague virus hemagglutinin expressed in Spodoptera frugiperda (Sf9) cells by coexpression of human beta 1,2-N-acetylglucosaminyltransferase I
    • Wagner R., Liedtke S., Kretzschmar E., Geyer H., Geyer R., and Klenk H.D. Elongation of the N-glycans of fowl plague virus hemagglutinin expressed in Spodoptera frugiperda (Sf9) cells by coexpression of human beta 1,2-N-acetylglucosaminyltransferase I. Glycobiology 6 (1996) 165-175
    • (1996) Glycobiology , vol.6 , pp. 165-175
    • Wagner, R.1    Liedtke, S.2    Kretzschmar, E.3    Geyer, H.4    Geyer, R.5    Klenk, H.D.6
  • 75
    • 2942744674 scopus 로고    scopus 로고
    • Carbohydrate moieties can induce mediator release: a detailed characterization of two major timothy grass pollen allergens
    • Wicklein D., Lindner B., Moll H., Kolarich D., Altmann F., Becker W.M., and Petersen A. Carbohydrate moieties can induce mediator release: a detailed characterization of two major timothy grass pollen allergens. Biol. Chem. 385 (2004) 397-407
    • (2004) Biol. Chem. , vol.385 , pp. 397-407
    • Wicklein, D.1    Lindner, B.2    Moll, H.3    Kolarich, D.4    Altmann, F.5    Becker, W.M.6    Petersen, A.7


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