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Volumn 16, Issue 10, 2018, Pages 1700-1709

An oligosaccharyltransferase from Leishmania major increases the N-glycan occupancy on recombinant glycoproteins produced in Nicotiana benthamiana

Author keywords

glyco engineering; N glycosylation; Nicotiana benthamiana; oligosaccharyltransferase; plant made pharmaceuticals

Indexed keywords

DOLICHYL-DIPHOSPHOOLIGOSACCHARIDE - PROTEIN GLYCOTRANSFERASE; GLYCOSYLTRANSFERASE; MEMBRANE PROTEIN; RECOMBINANT PROTEIN;

EID: 85044419692     PISSN: 14677644     EISSN: 14677652     Source Type: Journal    
DOI: 10.1111/pbi.12906     Document Type: Article
Times cited : (47)

References (76)
  • 1
    • 84880586512 scopus 로고    scopus 로고
    • N-linked protein glycosylation in the ER
    • Aebi, M. (2013) N-linked protein glycosylation in the ER. Biochim. Biophys. Acta, 1833, 2430–2437.
    • (2013) Biochim. Biophys. Acta , vol.1833 , pp. 2430-2437
    • Aebi, M.1
  • 2
    • 0030003017 scopus 로고    scopus 로고
    • Mutagenesis of the human IgA1 heavy chain tailpiece that prevents dimer assembly
    • Atkin, J.D., Pleass, R.J., Owens, R.J. and Woof, J.M. (1996) Mutagenesis of the human IgA1 heavy chain tailpiece that prevents dimer assembly. J. Immunol. 157, 156–159.
    • (1996) J. Immunol. , vol.157 , pp. 156-159
    • Atkin, J.D.1    Pleass, R.J.2    Owens, R.J.3    Woof, J.M.4
  • 3
    • 77950383145 scopus 로고    scopus 로고
    • Rapid, high-yield production in plants of individualized idiotype vaccines for non-Hodgkin's lymphoma
    • Bendandi, M., Marillonnet, S., Kandzia, R., Thieme, F., Nickstadt, A., Herz, S., Fröde, R. et al. (2010) Rapid, high-yield production in plants of individualized idiotype vaccines for non-Hodgkin's lymphoma. Ann. Oncol. 21, 2420–2427.
    • (2010) Ann. Oncol. , vol.21 , pp. 2420-2427
    • Bendandi, M.1    Marillonnet, S.2    Kandzia, R.3    Thieme, F.4    Nickstadt, A.5    Herz, S.6    Fröde, R.7
  • 5
    • 79956093771 scopus 로고    scopus 로고
    • N-glycosylation engineering of plants for the biosynthesis of glycoproteins with bisected and branched complex N-glycans
    • Castilho, A., Gattinger, P., Grass, J., Jez, J., Pabst, M., Altmann, F., Gorfer, M. et al. (2011) N-glycosylation engineering of plants for the biosynthesis of glycoproteins with bisected and branched complex N-glycans. Glycobiology, 21, 813–823.
    • (2011) Glycobiology , vol.21 , pp. 813-823
    • Castilho, A.1    Gattinger, P.2    Grass, J.3    Jez, J.4    Pabst, M.5    Altmann, F.6    Gorfer, M.7
  • 6
    • 84978483848 scopus 로고    scopus 로고
    • Stabilizing the CH2 domain of an antibody by engineering in an enhanced aromatic sequon
    • Chen, W., Kong, L., Connelly, S., Dendle, J.M., Liu, Y., Wilson, I.A., Powers, E.T. et al. (2016) Stabilizing the CH2 domain of an antibody by engineering in an enhanced aromatic sequon. ACS Chem. Biol. 11, 1852–1861.
    • (2016) ACS Chem. Biol. , vol.11 , pp. 1852-1861
    • Chen, W.1    Kong, L.2    Connelly, S.3    Dendle, J.M.4    Liu, Y.5    Wilson, I.A.6    Powers, E.T.7
  • 8
    • 84956708764 scopus 로고    scopus 로고
    • Transient Glyco-engineering to produce recombinant IgA1 with defined N- and O-Glycans in plants
    • Dicker, M., Tschofen, M., Maresch, D., Konig, J., Juarez, P., Orzaez, D., Altmann, F. et al. (2016) Transient Glyco-engineering to produce recombinant IgA1 with defined N- and O-Glycans in plants. Front Plant Sci. 7, 18.
    • (2016) Front Plant Sci. , vol.7 , pp. 18
    • Dicker, M.1    Tschofen, M.2    Maresch, D.3    Konig, J.4    Juarez, P.5    Orzaez, D.6    Altmann, F.7
  • 9
  • 11
    • 84877017128 scopus 로고    scopus 로고
    • Specialized roles of the conserved subunit OST3/6 of the oligosaccharyltransferase complex in innate immunity and tolerance to abiotic stresses
    • Farid, A., Malinovsky, F.G., Veit, C., Schoberer, J., Zipfel, C. and Strasser, R. (2013) Specialized roles of the conserved subunit OST3/6 of the oligosaccharyltransferase complex in innate immunity and tolerance to abiotic stresses. Plant Physiol. 162, 24–38.
    • (2013) Plant Physiol. , vol.162 , pp. 24-38
    • Farid, A.1    Malinovsky, F.G.2    Veit, C.3    Schoberer, J.4    Zipfel, C.5    Strasser, R.6
  • 12
    • 0024741662 scopus 로고
    • Construction of an Agrobacterium tumefaciens C58 recA mutant
    • Farrand, S.K., O'Morchoe, S.P. and McCutchan, J. (1989) Construction of an Agrobacterium tumefaciens C58 recA mutant. J. Bacteriol. 171, 5314–5321.
    • (1989) J. Bacteriol. , vol.171 , pp. 5314-5321
    • Farrand, S.K.1    O'Morchoe, S.P.2    McCutchan, J.3
  • 13
    • 79961233787 scopus 로고    scopus 로고
    • Unique carbohydrate-carbohydrate interactions are required for high affinity binding between FcgammaRIII and antibodies lacking core fucose
    • Ferrara, C., Grau, S., Jäger, C., Sondermann, P., Brünker, P., Waldhauer, I., Hennig, M. et al. (2011) Unique carbohydrate-carbohydrate interactions are required for high affinity binding between FcgammaRIII and antibodies lacking core fucose. Proc. Natl. Acad. Sci. USA, 108, 12669–12674.
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 12669-12674
    • Ferrara, C.1    Grau, S.2    Jäger, C.3    Sondermann, P.4    Brünker, P.5    Waldhauer, I.6    Hennig, M.7
  • 14
    • 85023189050 scopus 로고    scopus 로고
    • Exploring site-specific N-Glycosylation of HEK293 and plant-produced human IgA isotypes
    • Göritzer, K., Maresch, D., Altmann, F., Obinger, C. and Strasser, R. (2017) Exploring site-specific N-Glycosylation of HEK293 and plant-produced human IgA isotypes. J. Proteome Res. 16, 2560–2570.
    • (2017) J. Proteome Res. , vol.16 , pp. 2560-2570
    • Göritzer, K.1    Maresch, D.2    Altmann, F.3    Obinger, C.4    Strasser, R.5
  • 15
    • 84922879445 scopus 로고    scopus 로고
    • N-glycosylation of cholera toxin B subunit in Nicotiana benthamiana: impacts on host stress response, production yield and vaccine potential
    • Hamorsky, K.T., Kouokam, J.C., Jurkiewicz, J.M., Nelson, B., Moore, L.J., Husk, A.S., Kajiura, H. et al. (2015) N-glycosylation of cholera toxin B subunit in Nicotiana benthamiana: impacts on host stress response, production yield and vaccine potential. Sci. Rep. 5, 8003.
    • (2015) Sci. Rep. , vol.5 , pp. 8003
    • Hamorsky, K.T.1    Kouokam, J.C.2    Jurkiewicz, J.M.3    Nelson, B.4    Moore, L.J.5    Husk, A.S.6    Kajiura, H.7
  • 16
    • 84938054807 scopus 로고    scopus 로고
    • Enhanced expression of recombinant elastase in Pichia pastoris through the substitution of Thr for Ser in Asn-Xaa-Ser sequons
    • Han, M., Wang, W., Wang, X., Liu, X., Cao, H., Tao, Y. and Yu, X. (2015) Enhanced expression of recombinant elastase in Pichia pastoris through the substitution of Thr for Ser in Asn-Xaa-Ser sequons. Appl. Biochem. Biotechnol. 175, 428–435.
    • (2015) Appl. Biochem. Biotechnol. , vol.175 , pp. 428-435
    • Han, M.1    Wang, W.2    Wang, X.3    Liu, X.4    Cao, H.5    Tao, Y.6    Yu, X.7
  • 17
    • 85014284498 scopus 로고    scopus 로고
    • Establishment of a tobacco BY2 cell line devoid of plant-specific xylose and fucose as a platform for the production of biotherapeutic proteins
    • Hanania, U., Ariel, T., Tekoah, Y., Fux, L., Sheva, M., Gubbay, Y., Weiss, M. et al. (2017) Establishment of a tobacco BY2 cell line devoid of plant-specific xylose and fucose as a platform for the production of biotherapeutic proteins. Plant Biotechnol. J. 15, 1120–1129.
    • (2017) Plant Biotechnol. J. , vol.15 , pp. 1120-1129
    • Hanania, U.1    Ariel, T.2    Tekoah, Y.3    Fux, L.4    Sheva, M.5    Gubbay, Y.6    Weiss, M.7
  • 18
    • 58149339850 scopus 로고    scopus 로고
    • The yeast oligosaccharyltransferase complex can be replaced by STT3 from Leishmania major
    • Hese, K., Otto, C., Routier, F.H. and Lehle, L. (2009) The yeast oligosaccharyltransferase complex can be replaced by STT3 from Leishmania major. Glycobiology, 19, 160–171.
    • (2009) Glycobiology , vol.19 , pp. 160-171
    • Hese, K.1    Otto, C.2    Routier, F.H.3    Lehle, L.4
  • 19
    • 85029637509 scopus 로고    scopus 로고
    • Residues comprising the enhanced aromatic sequon influence protein N-glycosylation efficiency
    • Huang, Y.W., Yang, H.I., Wu, Y.T., Hsu, T.L., Lin, T.W., Kelly, J.W. and Wong, C.H. (2017) Residues comprising the enhanced aromatic sequon influence protein N-glycosylation efficiency. J. Am. Chem. Soc. 139, 12947–12955.
    • (2017) J. Am. Chem. Soc. , vol.139 , pp. 12947-12955
    • Huang, Y.W.1    Yang, H.I.2    Wu, Y.T.3    Hsu, T.L.4    Lin, T.W.5    Kelly, J.W.6    Wong, C.H.7
  • 20
    • 84915737185 scopus 로고    scopus 로고
    • A context-independent N-glycan signal targets the misfolded extracellular domain of Arabidopsis STRUBBELIG to endoplasmic-reticulum-associated degradation
    • Hüttner, S., Veit, C., Vavra, U., Schoberer, J., Dicker, M., Maresch, D., Altmann, F. et al. (2014) A context-independent N-glycan signal targets the misfolded extracellular domain of Arabidopsis STRUBBELIG to endoplasmic-reticulum-associated degradation. Biochem. J. 464, 401–411.
    • (2014) Biochem. J. , vol.464 , pp. 401-411
    • Hüttner, S.1    Veit, C.2    Vavra, U.3    Schoberer, J.4    Dicker, M.5    Maresch, D.6    Altmann, F.7
  • 21
    • 59249097324 scopus 로고    scopus 로고
    • Trypanosoma brucei UDP-glucose:glycoprotein glucosyltransferase has unusual substrate specificity and protects the parasite from stress
    • Izquierdo, L., Atrih, A., Rodrigues, J., Jones, D. and Ferguson, M. (2009) Trypanosoma brucei UDP-glucose:glycoprotein glucosyltransferase has unusual substrate specificity and protects the parasite from stress. Eukaryot. Cell, 8, 230–240.
    • (2009) Eukaryot. Cell , vol.8 , pp. 230-240
    • Izquierdo, L.1    Atrih, A.2    Rodrigues, J.3    Jones, D.4    Ferguson, M.5
  • 22
    • 61649087668 scopus 로고    scopus 로고
    • Glycosylation as a strategy to improve antibody-based therapeutics
    • Jefferis, R. (2009) Glycosylation as a strategy to improve antibody-based therapeutics. Nat. Rev. Drug. Discov. 8, 226–234.
    • (2009) Nat. Rev. Drug. Discov. , vol.8 , pp. 226-234
    • Jefferis, R.1
  • 23
    • 0037013743 scopus 로고    scopus 로고
    • Interaction sites on human IgG-Fc for FcgammaR: current models
    • Jefferis, R. and Lund, J. (2002) Interaction sites on human IgG-Fc for FcgammaR: current models. Immunol. Lett. 82, 57–65.
    • (2002) Immunol. Lett. , vol.82 , pp. 57-65
    • Jefferis, R.1    Lund, J.2
  • 25
    • 45749146309 scopus 로고    scopus 로고
    • Salt tolerance of Arabidopsis thaliana requires maturation of N-glycosylated proteins in the Golgi apparatus
    • Kang, J., Frank, J., Kang, C., Kajiura, H., Vikram, M., Ueda, A., Kim, S. et al. (2008) Salt tolerance of Arabidopsis thaliana requires maturation of N-glycosylated proteins in the Golgi apparatus. Proc. Natl. Acad. Sci. USA, 105, 5933–5938.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 5933-5938
    • Kang, J.1    Frank, J.2    Kang, C.3    Kajiura, H.4    Vikram, M.5    Ueda, A.6    Kim, S.7
  • 26
    • 33645103490 scopus 로고    scopus 로고
    • An evolving view of the eukaryotic oligosaccharyltransferase
    • Kelleher, D. and Gilmore, R. (2006) An evolving view of the eukaryotic oligosaccharyltransferase. Glycobiology, 16, 47R–62R.
    • (2006) Glycobiology , vol.16 , pp. 47R-62R
    • Kelleher, D.1    Gilmore, R.2
  • 27
    • 0032960606 scopus 로고    scopus 로고
    • The oligosaccharyltransferase complex from yeast
    • Knauer, R. and Lehle, L. (1999) The oligosaccharyltransferase complex from yeast. Biochim. Biophys. Acta, 1426, 259–273.
    • (1999) Biochim. Biophys. Acta , vol.1426 , pp. 259-273
    • Knauer, R.1    Lehle, L.2
  • 28
    • 10744227882 scopus 로고    scopus 로고
    • The STT3a subunit isoform of the Arabidopsis oligosaccharyltransferase controls adaptive responses to salt/osmotic stress
    • Koiwa, H., Li, F., McCully, M., Mendoza, I., Koizumi, N., Manabe, Y., Nakagawa, Y. et al. (2003) The STT3a subunit isoform of the Arabidopsis oligosaccharyltransferase controls adaptive responses to salt/osmotic stress. Plant Cell, 15, 2273–2284.
    • (2003) Plant Cell , vol.15 , pp. 2273-2284
    • Koiwa, H.1    Li, F.2    McCully, M.3    Mendoza, I.4    Koizumi, N.5    Manabe, Y.6    Nakagawa, Y.7
  • 29
    • 84930028449 scopus 로고    scopus 로고
    • Multiplexed, targeted gene editing in Nicotiana benthamiana for glyco-engineering and monoclonal antibody production
    • Li, J., Stoddard, T.J., Demorest, Z.L., Lavoie, P.O., Luo, S., Clasen, B.M., Cedrone, F. et al. (2016) Multiplexed, targeted gene editing in Nicotiana benthamiana for glyco-engineering and monoclonal antibody production. Plant Biotechnol. J. 14, 533–542.
    • (2016) Plant Biotechnol. J. , vol.14 , pp. 533-542
    • Li, J.1    Stoddard, T.J.2    Demorest, Z.L.3    Lavoie, P.O.4    Luo, S.5    Clasen, B.M.6    Cedrone, F.7
  • 30
    • 84958259501 scopus 로고    scopus 로고
    • The production of human glucocerebrosidase in glyco-engineered Nicotiana benthamiana plants
    • Limkul, J., Iizuka, S., Sato, Y., Misaki, R., Ohashi, T. and Fujiyama, K. (2016) The production of human glucocerebrosidase in glyco-engineered Nicotiana benthamiana plants. Plant Biotechnol. J. 14, 1682–1694.
    • (2016) Plant Biotechnol. J. , vol.14 , pp. 1682-1694
    • Limkul, J.1    Iizuka, S.2    Sato, Y.3    Misaki, R.4    Ohashi, T.5    Fujiyama, K.6
  • 31
    • 84890158776 scopus 로고    scopus 로고
    • The availability of glucose to CHO cells affects the intracellular lipid-linked oligosaccharide distribution, site occupancy and the N-glycosylation profile of a monoclonal antibody
    • Liu, B., Spearman, M., Doering, J., Lattová, E., Perreault, H. and Butler, M. (2014) The availability of glucose to CHO cells affects the intracellular lipid-linked oligosaccharide distribution, site occupancy and the N-glycosylation profile of a monoclonal antibody. J. Biotechnol. 170, 17–27.
    • (2014) J. Biotechnol. , vol.170 , pp. 17-27
    • Liu, B.1    Spearman, M.2    Doering, J.3    Lattová, E.4    Perreault, H.5    Butler, M.6
  • 34
    • 85017326066 scopus 로고    scopus 로고
    • Inactivation of the β(1,2)-xylosyltransferase and the α(1,3)-fucosyltransferase genes in Nicotiana tabacum BY-2 Cells by a Multiplex CRISPR/Cas9 Strategy Results in Glycoproteins without Plant-Specific Glycans
    • Mercx, S., Smargiasso, N., Chaumont, F., De Pauw, E., Boutry, M. and Navarre, C. (2017) Inactivation of the β(1,2)-xylosyltransferase and the α(1,3)-fucosyltransferase genes in Nicotiana tabacum BY-2 Cells by a Multiplex CRISPR/Cas9 Strategy Results in Glycoproteins without Plant-Specific Glycans. Front Plant Sci. 8, 403.
    • (2017) Front Plant Sci. , vol.8 , pp. 403
    • Mercx, S.1    Smargiasso, N.2    Chaumont, F.3    De Pauw, E.4    Boutry, M.5    Navarre, C.6
  • 35
    • 79961171901 scopus 로고    scopus 로고
    • Oligosaccharyltransferase: the central enzyme of N-linked protein glycosylation
    • Mohorko, E., Glockshuber, R. and Aebi, M. (2011) Oligosaccharyltransferase: the central enzyme of N-linked protein glycosylation. J. Inherit. Metab. Dis. 34, 869–878.
    • (2011) J. Inherit. Metab. Dis. , vol.34 , pp. 869-878
    • Mohorko, E.1    Glockshuber, R.2    Aebi, M.3
  • 37
    • 84939653631 scopus 로고    scopus 로고
    • Enhanced aromatic sequons increase oligosaccharyltransferase glycosylation efficiency and glycan homogeneity
    • Murray, A.N., Chen, W., Antonopoulos, A., Hanson, S.R., Wiseman, R.L., Dell, A., Haslam, S.M. et al. (2015) Enhanced aromatic sequons increase oligosaccharyltransferase glycosylation efficiency and glycan homogeneity. Chem. Biol. 22, 1052–1062.
    • (2015) Chem. Biol. , vol.22 , pp. 1052-1062
    • Murray, A.N.1    Chen, W.2    Antonopoulos, A.3    Hanson, S.R.4    Wiseman, R.L.5    Dell, A.6    Haslam, S.M.7
  • 38
    • 55549132977 scopus 로고    scopus 로고
    • All in one: Leishmania major STT3 proteins substitute for the whole oligosaccharyltransferase complex in Saccharomyces cerevisiae
    • Nasab, F.P., Schulz, B.L., Gamarro, F., Parodi, A.J. and Aebi, M. (2008) All in one: Leishmania major STT3 proteins substitute for the whole oligosaccharyltransferase complex in Saccharomyces cerevisiae. Mol. Biol. Cell, 19, 3758–3768.
    • (2008) Mol. Biol. Cell , vol.19 , pp. 3758-3768
    • Nasab, F.P.1    Schulz, B.L.2    Gamarro, F.3    Parodi, A.J.4    Aebi, M.5
  • 39
    • 70350755586 scopus 로고    scopus 로고
    • Control of the pattern-recognition receptor EFR by an ER protein complex in plant immunity
    • Nekrasov, V., Li, J., Batoux, M., Roux, M., Chu, Z., Lacombe, S., Rougon, A. et al. (2009) Control of the pattern-recognition receptor EFR by an ER protein complex in plant immunity. EMBO J. 28, 3428–3438.
    • (2009) EMBO J. , vol.28 , pp. 3428-3438
    • Nekrasov, V.1    Li, J.2    Batoux, M.3    Roux, M.4    Chu, Z.5    Lacombe, S.6    Rougon, A.7
  • 40
    • 0021041854 scopus 로고
    • Biological significance of carbohydrate chains on monoclonal antibodies
    • Nose, M. and Wigzell, H. (1983) Biological significance of carbohydrate chains on monoclonal antibodies. Proc. Natl. Acad. Sci. USA, 80, 6632–6636.
    • (1983) Proc. Natl. Acad. Sci. USA , vol.80 , pp. 6632-6636
    • Nose, M.1    Wigzell, H.2
  • 41
    • 84873837791 scopus 로고    scopus 로고
    • A combined system for engineering glycosylation efficiency and glycan structure in Saccharomyces cerevisiae
    • Parsaie Nasab, F., Aebi, M., Bernhard, G. and Frey, A.D. (2013) A combined system for engineering glycosylation efficiency and glycan structure in Saccharomyces cerevisiae. Appl. Environ. Microbiol. 79, 997–1007.
    • (2013) Appl. Environ. Microbiol. , vol.79 , pp. 997-1007
    • Parsaie Nasab, F.1    Aebi, M.2    Bernhard, G.3    Frey, A.D.4
  • 43
    • 37749007243 scopus 로고    scopus 로고
    • Recombinant antibody 2G12 produced in maize endosperm efficiently neutralizes HIV-1 and contains predominantly single-GlcNAc N-glycans
    • Rademacher, T., Sack, M., Arcalis, E., Stadlmann, J., Balzer, S., Altmann, F., Quendler, H. et al. (2008) Recombinant antibody 2G12 produced in maize endosperm efficiently neutralizes HIV-1 and contains predominantly single-GlcNAc N-glycans. Plant Biotechnol. J. 6, 189–201.
    • (2008) Plant Biotechnol. J. , vol.6 , pp. 189-201
    • Rademacher, T.1    Sack, M.2    Arcalis, E.3    Stadlmann, J.4    Balzer, S.5    Altmann, F.6    Quendler, H.7
  • 44
    • 84993960651 scopus 로고    scopus 로고
    • Review of the recombinant human interferon gamma as an immunotherapeutic: Impacts of production platforms and glycosylation
    • Razaghi, A., Owens, L. and Heimann, K. (2016) Review of the recombinant human interferon gamma as an immunotherapeutic: Impacts of production platforms and glycosylation. J. Biotechnol. 240, 48–60.
    • (2016) J. Biotechnol. , vol.240 , pp. 48-60
    • Razaghi, A.1    Owens, L.2    Heimann, K.3
  • 45
    • 84955194105 scopus 로고    scopus 로고
    • Fc glycans of therapeutic antibodies as critical quality attributes
    • Reusch, D. and Tejada, M.L. (2015) Fc glycans of therapeutic antibodies as critical quality attributes. Glycobiology, 25, 1325–1334.
    • (2015) Glycobiology , vol.25 , pp. 1325-1334
    • Reusch, D.1    Tejada, M.L.2
  • 46
    • 0021191796 scopus 로고
    • Natural human interferon-gamma. Complete amino acid sequence and determination of sites of glycosylation
    • Rinderknecht, E., O'Connor, B.H. and Rodriguez, H. (1984) Natural human interferon-gamma. Complete amino acid sequence and determination of sites of glycosylation. J. Biol. Chem. 259, 6790–6797.
    • (1984) J. Biol. Chem. , vol.259 , pp. 6790-6797
    • Rinderknecht, E.1    O'Connor, B.H.2    Rodriguez, H.3
  • 47
    • 84869134251 scopus 로고    scopus 로고
    • The oligosaccharyltransferase subunits OST48, DAD1 and KCP2 function as ubiquitous and selective modulators of mammalian N-glycosylation
    • Roboti, P. and High, S. (2012) The oligosaccharyltransferase subunits OST48, DAD1 and KCP2 function as ubiquitous and selective modulators of mammalian N-glycosylation. J. Cell Sci. 125, 3474–3484.
    • (2012) J. Cell Sci. , vol.125 , pp. 3474-3484
    • Roboti, P.1    High, S.2
  • 48
    • 58249093866 scopus 로고    scopus 로고
    • Cotranslational and posttranslational N-glycosylation of polypeptides by distinct mammalian OST isoforms
    • Ruiz-Canada, C., Kelleher, D.J. and Gilmore, R. (2009) Cotranslational and posttranslational N-glycosylation of polypeptides by distinct mammalian OST isoforms. Cell, 136, 272–283.
    • (2009) Cell , vol.136 , pp. 272-283
    • Ruiz-Canada, C.1    Kelleher, D.J.2    Gilmore, R.3
  • 49
    • 70350786920 scopus 로고    scopus 로고
    • Receptor quality control in the endoplasmic reticulum for plant innate immunity
    • Saijo, Y., Tintor, N., Lu, X., Rauf, P., Pajerowska-Mukhtar, K., Häweker, H., Dong, X. et al. (2009) Receptor quality control in the endoplasmic reticulum for plant innate immunity. EMBO J. 28, 3439–3449.
    • (2009) EMBO J. , vol.28 , pp. 3439-3449
    • Saijo, Y.1    Tintor, N.2    Lu, X.3    Rauf, P.4    Pajerowska-Mukhtar, K.5    Häweker, H.6    Dong, X.7
  • 50
    • 13444281918 scopus 로고    scopus 로고
    • The diversity of dolichol-linked precursors to Asn-linked glycans likely results from secondary loss of sets of glycosyltransferases
    • Samuelson, J., Banerjee, S., Magnelli, P., Cui, J., Kelleher, D.J., Gilmore, R. and Robbins, P.W. (2005) The diversity of dolichol-linked precursors to Asn-linked glycans likely results from secondary loss of sets of glycosyltransferases. Proc. Natl. Acad. Sci. USA, 102, 1548–1553.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 1548-1553
    • Samuelson, J.1    Banerjee, S.2    Magnelli, P.3    Cui, J.4    Kelleher, D.J.5    Gilmore, R.6    Robbins, P.W.7
  • 52
    • 0028989689 scopus 로고
    • N-glycosylation of human interferon-gamma: glycans at Asn-25 are critical for protease resistance
    • Sareneva, T., Pirhonen, J., Cantell, K. and Julkunen, I. (1995) N-glycosylation of human interferon-gamma: glycans at Asn-25 are critical for protease resistance. Biochem. J. 308, 9–14.
    • (1995) Biochem. J. , vol.308 , pp. 9-14
    • Sareneva, T.1    Pirhonen, J.2    Cantell, K.3    Julkunen, I.4
  • 53
    • 0029828073 scopus 로고    scopus 로고
    • Biosynthesis and N-glycosylation of human interferon-gamma. Asn25 and Asn97 differ markedly in how efficiently they are glycosylated and in their oligosaccharide composition
    • Sareneva, T., Mørtz, E., Tölö, H., Roepstorff, P. and Julkunen, I. (1996) Biosynthesis and N-glycosylation of human interferon-gamma. Asn25 and Asn97 differ markedly in how efficiently they are glycosylated and in their oligosaccharide composition. Eur. J. Biochem. 242, 191–200.
    • (1996) Eur. J. Biochem. , vol.242 , pp. 191-200
    • Sareneva, T.1    Mørtz, E.2    Tölö, H.3    Roepstorff, P.4    Julkunen, I.5
  • 55
    • 58149185093 scopus 로고    scopus 로고
    • Arginine/lysine residues in the cytoplasmic tail promote ER export of plant glycosylation enzymes
    • Schoberer, J., Vavra, U., Stadlmann, J., Hawes, C., Mach, L., Steinkellner, H. and Strasser, R. (2009) Arginine/lysine residues in the cytoplasmic tail promote ER export of plant glycosylation enzymes. Traffic, 10, 101–115.
    • (2009) Traffic , vol.10 , pp. 101-115
    • Schoberer, J.1    Vavra, U.2    Stadlmann, J.3    Hawes, C.4    Mach, L.5    Steinkellner, H.6    Strasser, R.7
  • 56
    • 84875714380 scopus 로고    scopus 로고
    • Time-resolved fluorescence imaging reveals differential interactions of N-glycan processing enzymes across the Golgi stack in planta
    • Schoberer, J., Liebminger, E., Botchway, S.W., Strasser, R. and Hawes, C. (2013) Time-resolved fluorescence imaging reveals differential interactions of N-glycan processing enzymes across the Golgi stack in planta. Plant Physiol. 161, 1737–1754.
    • (2013) Plant Physiol. , vol.161 , pp. 1737-1754
    • Schoberer, J.1    Liebminger, E.2    Botchway, S.W.3    Strasser, R.4    Hawes, C.5
  • 57
    • 17644366824 scopus 로고    scopus 로고
    • Proteomic analysis of mammalian oligosaccharyltransferase reveals multiple subcomplexes that contain Sec61, TRAP, and two potential new subunits
    • Shibatani, T., David, L.L., McCormack, A.L., Frueh, K. and Skach, W.R. (2005) Proteomic analysis of mammalian oligosaccharyltransferase reveals multiple subcomplexes that contain Sec61, TRAP, and two potential new subunits. Biochemistry, 44, 5982–5992.
    • (2005) Biochemistry , vol.44 , pp. 5982-5992
    • Shibatani, T.1    David, L.L.2    McCormack, A.L.3    Frueh, K.4    Skach, W.R.5
  • 58
    • 0037178791 scopus 로고    scopus 로고
    • Lack of fucose on human IgG1 N-linked oligosaccharide improves binding to human Fcgamma RIII and antibody-dependent cellular toxicity
    • Shields, R.L., Lai, J., Keck, R., O'Connell, L.Y., Hong, K., Meng, Y.G., Weikert, S.H. et al. (2002) Lack of fucose on human IgG1 N-linked oligosaccharide improves binding to human Fcgamma RIII and antibody-dependent cellular toxicity. J. Biol. Chem. 277, 26733–26740.
    • (2002) J. Biol. Chem. , vol.277 , pp. 26733-26740
    • Shields, R.L.1    Lai, J.2    Keck, R.3    O'Connell, L.Y.4    Hong, K.5    Meng, Y.G.6    Weikert, S.H.7
  • 59
    • 84981541252 scopus 로고    scopus 로고
    • Reduced paucimannosidic N-glycan formation by suppression of a specific β-hexosaminidase from Nicotiana benthamiana
    • Shin, Y.J., Castilho, A., Dicker, M., Sádio, F., Vavra, U., Grünwald-Gruber, C., Kwon, T.H. et al. (2017) Reduced paucimannosidic N-glycan formation by suppression of a specific β-hexosaminidase from Nicotiana benthamiana. Plant Biotechnol. J. 15, 197–206.
    • (2017) Plant Biotechnol. J. , vol.15 , pp. 197-206
    • Shin, Y.J.1    Castilho, A.2    Dicker, M.3    Sádio, F.4    Vavra, U.5    Grünwald-Gruber, C.6    Kwon, T.H.7
  • 60
    • 84876319236 scopus 로고    scopus 로고
    • Extreme C-terminal sites are posttranslocationally glycosylated by the STT3B isoform of the OST
    • Shrimal, S., Trueman, S.F. and Gilmore, R. (2013) Extreme C-terminal sites are posttranslocationally glycosylated by the STT3B isoform of the OST. J. Cell Biol. 201, 81–95.
    • (2013) J. Cell Biol. , vol.201 , pp. 81-95
    • Shrimal, S.1    Trueman, S.F.2    Gilmore, R.3
  • 61
    • 84931091527 scopus 로고    scopus 로고
    • Cotranslational and posttranslocational N-glycosylation of proteins in the endoplasmic reticulum
    • Shrimal, S., Cherepanova, N.A. and Gilmore, R. (2015) Cotranslational and posttranslocational N-glycosylation of proteins in the endoplasmic reticulum. Semin. Cell Dev. Biol. 41, 71–78.
    • (2015) Semin. Cell Dev. Biol. , vol.41 , pp. 71-78
    • Shrimal, S.1    Cherepanova, N.A.2    Gilmore, R.3
  • 62
    • 48949089988 scopus 로고    scopus 로고
    • Analysis of immunoglobulin glycosylation by LC-ESI-MS of glycopeptides and oligosaccharides
    • Stadlmann, J., Pabst, M., Kolarich, D., Kunert, R. and Altmann, F. (2008) Analysis of immunoglobulin glycosylation by LC-ESI-MS of glycopeptides and oligosaccharides. Proteomics, 8, 2858–2871.
    • (2008) Proteomics , vol.8 , pp. 2858-2871
    • Stadlmann, J.1    Pabst, M.2    Kolarich, D.3    Kunert, R.4    Altmann, F.5
  • 63
    • 84990943724 scopus 로고    scopus 로고
    • Plant protein glycosylation
    • Strasser, R. (2016) Plant protein glycosylation. Glycobiology, 26, 926–939.
    • (2016) Glycobiology , vol.26 , pp. 926-939
    • Strasser, R.1
  • 64
    • 1542358140 scopus 로고    scopus 로고
    • Generation of Arabidopsis thaliana plants with complex N-glycans lacking beta1,2-linked xylose and core alpha1,3-linked fucose
    • Strasser, R., Altmann, F., Mach, L., Glössl, J. and Steinkellner, H. (2004) Generation of Arabidopsis thaliana plants with complex N-glycans lacking beta1,2-linked xylose and core alpha1,3-linked fucose. FEBS Lett. 561, 132–136.
    • (2004) FEBS Lett. , vol.561 , pp. 132-136
    • Strasser, R.1    Altmann, F.2    Mach, L.3    Glössl, J.4    Steinkellner, H.5
  • 66
    • 41749105290 scopus 로고    scopus 로고
    • Generation of glyco-engineered Nicotiana benthamiana for the production of monoclonal antibodies with a homogeneous human-like N-glycan structure
    • Strasser, R., Stadlmann, J., Schähs, M., Stiegler, G., Quendler, H., Mach, L., Glössl, J. et al. (2008) Generation of glyco-engineered Nicotiana benthamiana for the production of monoclonal antibodies with a homogeneous human-like N-glycan structure. Plant Biotechnol. J. 6, 392–402.
    • (2008) Plant Biotechnol. J. , vol.6 , pp. 392-402
    • Strasser, R.1    Stadlmann, J.2    Schähs, M.3    Stiegler, G.4    Quendler, H.5    Mach, L.6    Glössl, J.7
  • 67
    • 84903758537 scopus 로고    scopus 로고
    • Controlled glycosylation of plant-produced recombinant proteins
    • Strasser, R., Altmann, F. and Steinkellner, H. (2014) Controlled glycosylation of plant-produced recombinant proteins. Curr. Opin. Biotechnol. 30C, 95–100.
    • (2014) Curr. Opin. Biotechnol. , vol.30C , pp. 95-100
    • Strasser, R.1    Altmann, F.2    Steinkellner, H.3
  • 68
    • 84955170377 scopus 로고    scopus 로고
    • Rice endosperm produces an underglycosylated and potent form of the HIV-neutralizing monoclonal antibody 2G12
    • Vamvaka, E., Twyman, R.M., Murad, A.M., Melnik, S., Teh, A.Y., Arcalis, E., Altmann, F. et al. (2016) Rice endosperm produces an underglycosylated and potent form of the HIV-neutralizing monoclonal antibody 2G12. Plant Biotechnol. J. 14, 97–108.
    • (2016) Plant Biotechnol. J. , vol.14 , pp. 97-108
    • Vamvaka, E.1    Twyman, R.M.2    Murad, A.M.3    Melnik, S.4    Teh, A.Y.5    Arcalis, E.6    Altmann, F.7
  • 69
    • 33846614234 scopus 로고    scopus 로고
    • Aberrant localization and underglycosylation of highly accumulating single-chain Fv-Fc antibodies in transgenic Arabidopsis seeds
    • Van Droogenbroeck, B., Cao, J., Stadlmann, J., Altmann, F., Colanesi, S., Hillmer, S., Robinson, D.G. et al. (2007) Aberrant localization and underglycosylation of highly accumulating single-chain Fv-Fc antibodies in transgenic Arabidopsis seeds. Proc. Natl. Acad. Sci. USA, 104, 1430–1435.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 1430-1435
    • Van Droogenbroeck, B.1    Cao, J.2    Stadlmann, J.3    Altmann, F.4    Colanesi, S.5    Hillmer, S.6    Robinson, D.G.7
  • 70
    • 0024544730 scopus 로고
    • Aglycosylation of human IgG1 and IgG3 monoclonal antibodies can eliminate recognition by human cells expressing Fc gamma RI and/or Fc gamma RII receptors
    • Walker, M.R., Lund, J., Thompson, K.M. and Jefferis, R. (1989) Aglycosylation of human IgG1 and IgG3 monoclonal antibodies can eliminate recognition by human cells expressing Fc gamma RI and/or Fc gamma RII receptors. Biochem. J. 259, 347–353.
    • (1989) Biochem. J. , vol.259 , pp. 347-353
    • Walker, M.R.1    Lund, J.2    Thompson, K.M.3    Jefferis, R.4
  • 71
    • 78651471034 scopus 로고    scopus 로고
    • Profiling of N-glycosylation gene expression in CHO cell fed-batch cultures
    • Wong, D.C., Wong, N.S., Goh, J.S., May, L.M. and Yap, M.G. (2010) Profiling of N-glycosylation gene expression in CHO cell fed-batch cultures. Biotechnol. Bioeng. 107, 516–528.
    • (2010) Biotechnol. Bioeng. , vol.107 , pp. 516-528
    • Wong, D.C.1    Wong, N.S.2    Goh, J.S.3    May, L.M.4    Yap, M.G.5
  • 72
    • 0037033113 scopus 로고    scopus 로고
    • Studies on the function of oligosaccharyl transferase subunits. Stt3p is directly involved in the glycosylation process
    • Yan, Q. and Lennarz, W.J. (2002) Studies on the function of oligosaccharyl transferase subunits. Stt3p is directly involved in the glycosylation process. J. Biol. Chem. 277, 47692–47700.
    • (2002) J. Biol. Chem. , vol.277 , pp. 47692-47700
    • Yan, Q.1    Lennarz, W.J.2
  • 73
    • 84952940199 scopus 로고    scopus 로고
    • N-glycoprotein macroheterogeneity: biological implications and proteomic characterization
    • Zacchi, L.F. and Schulz, B.L. (2016) N-glycoprotein macroheterogeneity: biological implications and proteomic characterization. Glycoconj. J. 33, 359–376.
    • (2016) Glycoconj. J. , vol.33 , pp. 359-376
    • Zacchi, L.F.1    Schulz, B.L.2
  • 75
    • 77953240454 scopus 로고    scopus 로고
    • Precision mapping of an in vivo N-glycoproteome reveals rigid topological and sequence constraints
    • Zielinska, D.F., Gnad, F., Wiśniewski, J.R. and Mann, M. (2010) Precision mapping of an in vivo N-glycoproteome reveals rigid topological and sequence constraints. Cell, 141, 897–907.
    • (2010) Cell , vol.141 , pp. 897-907
    • Zielinska, D.F.1    Gnad, F.2    Wiśniewski, J.R.3    Mann, M.4
  • 76
    • 84861427459 scopus 로고    scopus 로고
    • Mapping N-glycosylation sites across seven evolutionarily distant species reveals a divergent substrate proteome despite a common core machinery
    • Zielinska, D.F., Gnad, F., Schropp, K., Wiśniewski, J.R. and Mann, M. (2012) Mapping N-glycosylation sites across seven evolutionarily distant species reveals a divergent substrate proteome despite a common core machinery. Mol. Cell, 46, 542–548.
    • (2012) Mol. Cell , vol.46 , pp. 542-548
    • Zielinska, D.F.1    Gnad, F.2    Schropp, K.3    Wiśniewski, J.R.4    Mann, M.5


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