메뉴 건너뛰기




Volumn 271, Issue 21, 2004, Pages 4241-4258

The N-linked oligosaccharides of aminopeptidase N from Manduca sexta: Site localization and identification of novel N-glycan structures

Author keywords

Aminopeptidase N; Fucose; High energy CID; Insect glycosylation; MALDI TOF TOF

Indexed keywords

GLYCAN; GLYCOPROTEIN; MANNOSE; MICROSOMAL AMINOPEPTIDASE; OLIGOSACCHARIDE; PAUCIMANNOSIDIC N GLYCAN; UNCLASSIFIED DRUG;

EID: 8644242089     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.2004.04364.x     Document Type: Article
Times cited : (34)

References (37)
  • 3
    • 0032848027 scopus 로고    scopus 로고
    • Insect cells as hosts for the expression of recombinant glycoproteins
    • Altmann, F., Staudacher, E., Wilson, I.B.H. & März, L. (1999) Insect cells as hosts for the expression of recombinant glycoproteins. Glycoconj. J. 16, 109-123.
    • (1999) Glycoconj. J. , vol.16 , pp. 109-123
    • Altmann, F.1    Staudacher, E.2    Wilson, I.B.H.3    März, L.4
  • 4
    • 0028915061 scopus 로고
    • The asparagine-linked carbohydrate of honeybee venom hyaluronidase
    • Kubelka, V., Altmann, F. & März, L. (1995) The asparagine-linked carbohydrate of honeybee venom hyaluronidase. Glycoconj. J. 12, 77-83.
    • (1995) Glycoconj. J. , vol.12 , pp. 77-83
    • Kubelka, V.1    Altmann, F.2    März, L.3
  • 6
    • 0032190659 scopus 로고    scopus 로고
    • Engineering N-glycosylation pathways in the baculovirus-insect cell system
    • Jarvis, D.L., Kawar, Z.S. & Hollister, J.R. (1998) Engineering N-glycosylation pathways in the baculovirus-insect cell system. Curr. Op. Biotechnol. 9, 528-533.
    • (1998) Curr. Op. Biotechnol. , vol.9 , pp. 528-533
    • Jarvis, D.L.1    Kawar, Z.S.2    Hollister, J.R.3
  • 7
    • 0023199689 scopus 로고
    • Specific interaction of IgE antibodies with a carbohydrate epitope of honey-bee venom phospholipase-A2
    • Weber, A., Schroder, H., Thalberg, K. & März, L. (1987) Specific interaction of IgE antibodies with a carbohydrate epitope of honey-bee venom phospholipase-A2. Allergy 42, 464-470.
    • (1987) Allergy , vol.42 , pp. 464-470
    • Weber, A.1    Schroder, H.2    Thalberg, K.3    März, L.4
  • 8
    • 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., März, L. & Becker, W.M. (1993) 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, 259-266.
    • (1993) Int. Arch. Allergy Immunol. , vol.102 , pp. 259-266
    • Tretter, V.1    Altmann, F.2    Kubelka, V.3    März, L.4    Becker, W.M.5
  • 9
    • 0028291484 scopus 로고
    • The receptor for Bacillus thuringiensis Cry1A(c) delta-endotoxin in the brushborder membrane of the lepidopteran Manduca sexta is aminopeptidase-N
    • Knight, P.J.K., Crickmore, N. & Ellar, D.J. (1994) The receptor for Bacillus thuringiensis Cry1A(c) delta-endotoxin in the brushborder membrane of the lepidopteran Manduca sexta is aminopeptidase-N. Mol. Microbiol. 11, 429-436.
    • (1994) Mol. Microbiol. , vol.11 , pp. 429-436
    • Knight, P.J.K.1    Crickmore, N.2    Ellar, D.J.3
  • 10
    • 0742288367 scopus 로고    scopus 로고
    • Analysis of glycan structures on the 120 kDa aminopeptidase N of Manduca sexta and their interactions with Bacillus thuringiensis Cry1Ac toxin
    • Knight, P.J.K., Carroll, J. & Ellar, D.J. (2004) Analysis of glycan structures on the 120 kDa aminopeptidase N of Manduca sexta and their interactions with Bacillus thuringiensis Cry1Ac toxin. Insect Biochem. Mol. Biol. 34, 101-112.
    • (2004) Insect Biochem. Mol. Biol. , vol.34 , pp. 101-112
    • Knight, P.J.K.1    Carroll, J.2    Ellar, D.J.3
  • 11
    • 0019520214 scopus 로고
    • Purification and characterization of the entomocidal protoxin of Bacillus thuringiensis
    • Bulla, L.A., Kramer, K.J., Cox, D.J., Jones, B.L., Davidson, L.I. & Lookhart, G.L. (1981) Purification and characterization of the entomocidal protoxin of Bacillus thuringiensis. J. Biol. Chem. 256, 3000-3004.
    • (1981) J. Biol. Chem. , vol.256 , pp. 3000-3004
    • Bulla, L.A.1    Kramer, K.J.2    Cox, D.J.3    Jones, B.L.4    Davidson, L.I.5    Lookhart, G.L.6
  • 12
    • 0036899846 scopus 로고    scopus 로고
    • Transgenic Drosophila reveals a functional in vivo receptor for the Bacillus thuringiensis toxin Cry1Ac1
    • Gill, M. & Ellar, D.J. (2002) Transgenic Drosophila reveals a functional in vivo receptor for the Bacillus thuringiensis toxin Cry1Ac1. Insect Mol. Biol. 11, 619-625.
    • (2002) Insect Mol. Biol. , vol.11 , pp. 619-625
    • Gill, M.1    Ellar, D.J.2
  • 13
    • 0030239953 scopus 로고    scopus 로고
    • A 106 kDa form of aminopeptidase is a receptor for Bacillus thuringiensis Cry1c delta-endotoxin in the brush border membrane of Manduca sexta
    • Luo, K., Lu, Y. & Adang, M.J. (1996) A 106 kDa form of aminopeptidase is a receptor for Bacillus thuringiensis Cry1c delta-endotoxin in the brush border membrane of Manduca sexta. Insect Biochem. Mol. Biol. 26, 783-791.
    • (1996) Insect Biochem. Mol. Biol. , vol.26 , pp. 783-791
    • Luo, K.1    Lu, Y.2    Adang, M.J.3
  • 14
    • 0030767349 scopus 로고    scopus 로고
    • Cloning and characterization of Manduca sexta and Plutella xylostella midgut amino-peptidase N enzymes related to Bacillus thuringiensis toxin-binding proteins
    • Denolf, P., Hendrickx, K., Van Damme, J., Jansens, S., Peferoen, M., Degheele, D. & Van Rie, J. (1997) Cloning and characterization of Manduca sexta and Plutella xylostella midgut amino-peptidase N enzymes related to Bacillus thuringiensis toxin-binding proteins. Eur. J. Biochem. 248, 748-761.
    • (1997) Eur. J. Biochem. , vol.248 , pp. 748-761
    • Denolf, P.1    Hendrickx, K.2    Van Damme, J.3    Jansens, S.4    Peferoen, M.5    Degheele, D.6    Van Rie, J.7
  • 15
    • 0028926641 scopus 로고
    • Kinetic comparison of peptide N-glycosidase F and N-glycosidase A reveals several differences in substrate specificity
    • Altmann, F., Schweiszer, S. & Weber, C. (1995) Kinetic comparison of peptide N-glycosidase F and N-glycosidase A reveals several differences in substrate specificity. Glycoconj. J. 12, 84-93.
    • (1995) Glycoconj. J. , vol.12 , pp. 84-93
    • Altmann, F.1    Schweiszer, S.2    Weber, C.3
  • 16
    • 0033551196 scopus 로고    scopus 로고
    • Site-specific characterization of the N-linked glycans of murine prion protein by high-performance liquid chromatography electrospray mass spectrometry and exoglycosidase digestions
    • Stimson, E., Hope, J., Chong, A. & Burlingame, A.L. (1999) Site-specific characterization of the N-linked glycans of murine prion protein by high-performance liquid chromatography electrospray mass spectrometry and exoglycosidase digestions. Biochemistry 38, 4885-4895.
    • (1999) Biochemistry , vol.38 , pp. 4885-4895
    • Stimson, E.1    Hope, J.2    Chong, A.3    Burlingame, A.L.4
  • 18
    • 0034701053 scopus 로고    scopus 로고
    • Hybrid and complex glycans are linked to the conserved N-glycosylation site of the third eight-cysteine domain of LTBP-1 in insect cells
    • Rudd, P.M., Downing, K.A., Cadene, M., Harvey, D.J., Wormald, M.R., Weir, I., Dwek, R.A., Rifkin, D.B. & Gleizes, P.E. (2000) Hybrid and complex glycans are linked to the conserved N-glycosylation site of the third eight-cysteine domain of LTBP-1 in insect cells. Biochemistry 39, 1596-1603.
    • (2000) Biochemistry , vol.39 , pp. 1596-1603
    • Rudd, P.M.1    Downing, K.A.2    Cadene, M.3    Harvey, D.J.4    Wormald, M.R.5    Weir, I.6    Dwek, R.A.7    Rifkin, D.B.8    Gleizes, P.E.9
  • 20
    • 0028236119 scopus 로고
    • Structures of the N-linked oligosaccharides of the membrane-glycoproteins from 3 lepidopteran cell-lines (SF-21, IZD-MB-0503, BM-N)
    • Kubelka, V., Altmann, F., Kornfeld, G. & März, L. (1994) Structures of the N-linked oligosaccharides of the membrane-glycoproteins from 3 lepidopteran cell-lines (SF-21, IZD-MB-0503, BM-N). Arch. Biochem. Biophys. 308, 148-157.
    • (1994) Arch. Biochem. Biophys , vol.308 , pp. 148-157
    • Kubelka, V.1    Altmann, F.2    Kornfeld, G.3    März, L.4
  • 21
    • 0030463632 scopus 로고    scopus 로고
    • Effect of reducing-terminal substituents on the high-energy collision-induced dissociation matrix-assisted laser desorption/ionization mass spectra of oligosaccharides
    • Küster, B., Naven, T.J.P. & Harvey, D.J. (1996) Effect of reducing-terminal substituents on the high-energy collision-induced dissociation matrix-assisted laser desorption/ionization mass spectra of oligosaccharides. Rapid Commun. Mass Spectrom. 10, 1645-1651.
    • (1996) Rapid Commun. Mass Spectrom. , vol.10 , pp. 1645-1651
    • Küster, B.1    Naven, T.J.P.2    Harvey, D.J.3
  • 22
    • 0019888484 scopus 로고
    • Facile cleavage of complex oligosaccharides from glycopeptides by almond emulsin peptide-N-glycosidase
    • Plummer, T.H. Jr & Tarentino, A.L. (1981) Facile cleavage of complex oligosaccharides from glycopeptides by almond emulsin peptide-N-glycosidase. J. Biol. Chem. 256, 10243-10246.
    • (1981) J. Biol. Chem. , vol.256 , pp. 10243-10246
    • Plummer Jr., T.H.1    Tarentino, A.L.2
  • 23
    • 0023657495 scopus 로고
    • Detection and quantification of peptide-N-4-(N-acetyl-beta-glucosaminyl) asparagine amidases
    • Plummer, T.H. Jr, Phelan, A.W. & Tarentino, A.L. (1987) Detection and quantification of peptide-N-4-(N-acetyl-beta-glucosaminyl) asparagine amidases. Eur. J. Biochem. 163, 167-173.
    • (1987) Eur. J. Biochem. , vol.163 , pp. 167-173
    • Plummer Jr., T.H.1    Phelan, A.W.2    Tarentino, A.L.3
  • 24
    • 1942454436 scopus 로고    scopus 로고
    • Fragmentation characteristics of neutral N-linked glycans using a MALDI-TOF/TOF tandem mass spectrometer
    • Stephens, E., Maslen, S.L., Green, L.G. & Williams, D.H. (2004) Fragmentation characteristics of neutral N-linked glycans using a MALDI-TOF/TOF tandem mass spectrometer. Anal. Chem. 76, 2343-2354.
    • (2004) Anal. Chem. , vol.76 , pp. 2343-2354
    • Stephens, E.1    Maslen, S.L.2    Green, L.G.3    Williams, D.H.4
  • 25
    • 1242272032 scopus 로고    scopus 로고
    • New fragmentation mechanisms in matrix-assisted laser desorption/ionization time-of-flight/time-of-flight tandem mass spectrometry
    • Spina, E., Sturiale, L., Romeo, D., Impallomeni, G., Garozzo, D., Waidelich, D. & Glueckmann, M. (2004) New fragmentation mechanisms in matrix-assisted laser desorption/ionization time-of-flight/time-of-flight tandem mass spectrometry. Rapid Commun. Mass Spectrom. 18, 392-398.
    • (2004) Rapid Commun. Mass Spectrom. , vol.18 , pp. 392-398
    • Spina, E.1    Sturiale, L.2    Romeo, D.3    Impallomeni, G.4    Garozzo, D.5    Waidelich, D.6    Glueckmann, M.7
  • 26
    • 0141482211 scopus 로고    scopus 로고
    • Structural characterization of oligosaccharides using MALDI-TOF/TOF tandem mass spectrometry
    • Mechref, Y., Novotny, M.V. & Krishan, C. (2003) Structural characterization of oligosaccharides using MALDI-TOF/TOF tandem mass spectrometry. Anal. Chem. 75, 4895-4903.
    • (2003) Anal. Chem. , vol.75 , pp. 4895-4903
    • Mechref, Y.1    Novotny, M.V.2    Krishan, C.3
  • 27
    • 0024206786 scopus 로고
    • A systematic nomenclature for carbohydrate fragmentations in FAB-MS/MS spectra of glycoconjugates
    • Domon, B. & Costello, C.E. (1988) A systematic nomenclature for carbohydrate fragmentations in FAB-MS/MS spectra of glycoconjugates. Glycoconjugate J. 5, 397-409.
    • (1988) Glycoconjugate J. , vol.5 , pp. 397-409
    • Domon, B.1    Costello, C.E.2
  • 28
    • 0031037943 scopus 로고    scopus 로고
    • High-energy collision-induced fragmentation of complex oligosaccharides ionized by matrix-assisted laser desorption/ionization mass spectrometry
    • Harvey, D.J., Bateman, R.H. & Green, M.R. (1997) High-energy collision-induced fragmentation of complex oligosaccharides ionized by matrix-assisted laser desorption/ionization mass spectrometry. J. Mass Spectrom. 32, 167-187.
    • (1997) J. Mass Spectrom. , vol.32 , pp. 167-187
    • Harvey, D.J.1    Bateman, R.H.2    Green, M.R.3
  • 30
    • 0026534774 scopus 로고
    • Alpha-1-6 (alpha-1-3)-difucosylation of the asparagine-bound N-acetylglucosamine in honeybee venom phospholipase-A2
    • Staudacher, E., Altmann, F., März, L., Hard, K., Kamerling, J.P. & Vliegenthart, J.F. (1992) Alpha-1-6 (alpha-1-3)-difucosylation of the asparagine-bound N-acetylglucosamine in honeybee venom phospholipase-A2. Glycoconj. J. 9, 82-85.
    • (1992) Glycoconj. J. , vol.9 , pp. 82-85
    • Staudacher, E.1    Altmann, F.2    März, L.3    Hard, K.4    Kamerling, J.P.5    Vliegenthart, J.F.6
  • 31
    • 0029852531 scopus 로고    scopus 로고
    • Haemonchus contortus glycoproteins contain N-linked oligosaccharides with novel highly fucosylated core structures
    • Haslam, S.M., Coles, G.C., Munn, E.A., Smith,T.S., Smith, H.F., Morris, H.R. & Dell, A. (1996) Haemonchus contortus glycoproteins contain N-linked oligosaccharides with novel highly fucosylated core structures. J. Biol. Chem. 271, 30561-30570.
    • (1996) J. Biol. Chem. , vol.271 , pp. 30561-30570
    • Haslam, S.M.1    Coles, G.C.2    Munn, E.A.3    Smith, T.S.4    Smith, H.F.5    Morris, H.R.6    Dell, A.7
  • 32
    • 0031821356 scopus 로고    scopus 로고
    • N-linked glycosylation of a baculovirus-expressed recombinant glycoprotein in insect larvae and tissue culture cells
    • Kulakosky, P.C., Hughes, P.R. & Wood, H.A. (1998) N-linked glycosylation of a baculovirus-expressed recombinant glycoprotein in insect larvae and tissue culture cells. Glycobiology 8, 741-745.
    • (1998) Glycobiology , vol.8 , pp. 741-745
    • Kulakosky, P.C.1    Hughes, P.R.2    Wood, H.A.3
  • 33
    • 0029085691 scopus 로고
    • Insect cells contain an unusual, membrane bound beta-N- acetylglucosaminidase probably involved in the processing of protein N-glycans
    • Altmann, F., Schwihla, H., Staudacher, E., Glössl, J. & März, L. (1995) Insect cells contain an unusual, membrane bound beta-N-acetylglucosaminidase probably involved in the processing of protein N-glycans. J. Biol. Chem. 270, 17344-17349.
    • (1995) J. Biol. Chem. , vol.270 , pp. 17344-17349
    • Altmann, F.1    Schwihla, H.2    Staudacher, E.3    Glössl, J.4    März, L.5
  • 35
    • 0026172013 scopus 로고
    • The (1-3)-linked alpha-1-fucosyl group of the N-glycans of the Wistaria floribunda lectins is recognized by a rabbit antiserum
    • Ramirez-Soto, D. & Poretz, R.D. (1991) The (1-3)-linked alpha-1-fucosyl group of the N-glycans of the Wistaria floribunda lectins is recognized by a rabbit antiserum. Carbohydr. Res. 213, 27-36.
    • (1991) Carbohydr. Res. , vol.213 , pp. 27-36
    • Ramirez-Soto, D.1    Poretz, R.D.2
  • 36
    • 0026691179 scopus 로고
    • The anti-genicity of the carbohydrate moiety of an insect glycoprotein, honeybee (Apis mellifera) venom phospholipase-A(2) - The role of alpha-1,3-fucosylation of the asparagine-bound N-acetylglucosamine
    • Prenner, C., Mach, L., Glössl, J. & März, L. (1992) The anti-genicity of the carbohydrate moiety of an insect glycoprotein, honeybee (Apis mellifera) venom phospholipase-A(2) - the role of alpha-1,3-fucosylation of the asparagine-bound N-acetylglucosamine. Biochem. J. 284, 337-380.
    • (1992) Biochem. J. , vol.284 , pp. 337-380
    • Prenner, C.1    Mach, L.2    Glössl, J.3    März, L.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.