메뉴 건너뛰기




Volumn 25, Issue 3, 2008, Pages 245-257

High-level expression of biologically active glycoprotein hormones in Pichia pastoris strains - Selection of strain GS115, and not X-33, for the production of biologically active N-glycosylated 15N-labeled phCG

Author keywords

15N Labeling; Glycosylation; Human chorionic gonadotropin; Human follicle stimulating hormone; Hypermannosylation; Pichia pastoris GS115; Pichia pastoris X 33

Indexed keywords

AMMONIA; CARBON; CHORIONIC GONADOTROPIN; FOLLITROPIN; GLYCEROL; GLYCOPROTEIN; MANNOSE; METHANOL; NITROGEN;

EID: 40949094021     PISSN: 02820080     EISSN: 15734986     Source Type: Journal    
DOI: 10.1007/s10719-007-9082-8     Document Type: Article
Times cited : (30)

References (52)
  • 1
    • 0030272217 scopus 로고    scopus 로고
    • Quality and authenticity of heterologous proteins synthesized in yeast
    • Eckart, M.R., Bussineau, C.M.: Quality and authenticity of heterologous proteins synthesized in yeast. Curr. Opin. Biotechnol. 7, 525-530 (1996)
    • (1996) Curr. Opin. Biotechnol. , vol.7 , pp. 525-530
    • Eckart, M.R.1    Bussineau, C.M.2
  • 2
    • 0033955337 scopus 로고    scopus 로고
    • Heterologous protein expression in the methylotrophic yeast Pichia pastoris
    • Cereghino, J.L., Cregg, J.M.: Heterologous protein expression in the methylotrophic yeast Pichia pastoris. FEMS Microbiol. Rev. 24, 45-66 (2000)
    • (2000) FEMS Microbiol. Rev. , vol.24 , pp. 45-66
    • Cereghino, J.L.1    Cregg, J.M.2
  • 3
    • 0344603650 scopus 로고    scopus 로고
    • Hyperexpression of biologically active human chorionic gonadotropin using the methylotropic yeast, Pichia pastoris
    • Sen Gupta, C., Dighe, R.R.: Hyperexpression of biologically active human chorionic gonadotropin using the methylotropic yeast, Pichia pastoris. J. Mol. Endocrinol. 22, 273-283 (1999)
    • (1999) J. Mol. Endocrinol. , vol.22 , pp. 273-283
    • Sen Gupta, C.1    Dighe, R.R.2
  • 4
    • 0346936019 scopus 로고    scopus 로고
    • Hyperexpression and purification of biologically active human luteinizing hormone and human chorionic gonadotropin using the methylotrophic yeast, Pichia pastoris
    • Gadkari, R., Deshpande, R., Dighe, R.R.: Hyperexpression and purification of biologically active human luteinizing hormone and human chorionic gonadotropin using the methylotrophic yeast, Pichia pastoris. Protein Expr. Purif. 32, 175-184 (2003)
    • (2003) Protein Expr. Purif. , vol.32 , pp. 175-184
    • Gadkari, R.1    Deshpande, R.2    Dighe, R.R.3
  • 5
    • 33845587326 scopus 로고    scopus 로고
    • Characterization of the N-linked oligosaccharides from human chorionic gonadotropin expressed in the methylotrophic yeast Pichia pastoris
    • Blanchard, V., Gadkari, R.A., Gerwig, G.J., Dighe, R.R., Leeflang, B.R., Kamerling, J.P.: Characterization of the N-linked oligosaccharides from human chorionic gonadotropin expressed in the methylotrophic yeast Pichia pastoris. Glycoconj. J. 24, 33-47 (2007)
    • (2007) Glycoconj. J. , vol.24 , pp. 33-47
    • Blanchard, V.1    Gadkari, R.A.2    Gerwig, G.J.3    Dighe, R.R.4    Leeflang, B.R.5    Kamerling, J.P.6
  • 6
    • 0029824825 scopus 로고    scopus 로고
    • NMR studies of the free α-subunit of human chorionic gonadotropin. Structural influences of N-glycosylation and the β-subunit on the conformation of the α-subunit
    • De Beer, T., van Zuylen, C.W., Leeflang, B.R., Hård, K., Boelens, R., Kaptein, R., Kamerling, J.P., Vliegenthart, J.F.G.: NMR studies of the free α-subunit of human chorionic gonadotropin. Structural influences of N-glycosylation and the β-subunit on the conformation of the α-subunit. Eur. J. Biochem. 241, 229-242 (1996)
    • (1996) Eur. J. Biochem. , vol.241 , pp. 229-242
    • De Beer, T.1    Van Zuylen, C.W.2    Leeflang, B.R.3    Hård, K.4    Boelens, R.5    Kaptein, R.6    Kamerling, J.P.7    Vliegenthart, J.F.G.8
  • 7
    • 0032539529 scopus 로고    scopus 로고
    • Mobilities of the inner three core residues and the Man(α1-6) branch of the glycan at Asn78 of the α-subunit of human chorionic gonadotropin are restricted by the protein
    • Van Zuylen, C.W., de Beer, T., Leeflang, B.R., Boelens, R., Kaptein, R., Kamerling, J.P., Vliegenthart, J.F.G.: Mobilities of the inner three core residues and the Man(α1-6) branch of the glycan at Asn78 of the α-subunit of human chorionic gonadotropin are restricted by the protein. Biochemistry 37, 1933-1940 (1998)
    • (1998) Biochemistry , vol.37 , pp. 1933-1940
    • Van Zuylen, C.W.1    De Beer, T.2    Leeflang, B.R.3    Boelens, R.4    Kaptein, R.5    Kamerling, J.P.6    Vliegenthart, J.F.G.7
  • 9
    • 0034705002 scopus 로고    scopus 로고
    • Effects of the N-linked glycans on the 3D structure of the free α-subunit of human chorionic gonadotropin
    • Erbel, P.J., Karimi-Nejad, Y., van Kuik, J.A., Boelens, R., Kamerling, J.P., Vliegenthart, J.F.G.: Effects of the N-linked glycans on the 3D structure of the free α-subunit of human chorionic gonadotropin. Biochemistry 39, 6012-6021 (2000)
    • (2000) Biochemistry , vol.39 , pp. 6012-6021
    • Erbel, P.J.1    Karimi-Nejad, Y.2    Van Kuik, J.A.3    Boelens, R.4    Kamerling, J.P.5    Vliegenthart, J.F.G.6
  • 10
    • 0028773646 scopus 로고
    • Structure of human chorionic gonadotropin at 2.6 Å resolution from MAD analysis of the selenomethionyl protein
    • Wu, H., Lustbader, J.W., Liu, Y., Canfield, R.E., Hendrickson, W.A.: Structure of human chorionic gonadotropin at 2.6 Å resolution from MAD analysis of the selenomethionyl protein. Structure 2, 545-558 (1994)
    • (1994) Structure , vol.2 , pp. 545-558
    • Wu, H.1    Lustbader, J.W.2    Liu, Y.3    Canfield, R.E.4    Hendrickson, W.A.5
  • 13
    • 0028081167 scopus 로고
    • High-level secretion and very efficient isotopic labeling of tick anticoagulant peptide (TAP) expressed in the methylotrophic yeast, Pichia pastoris
    • Laroche, Y., Storme, V., De Meutter, J., Messens, J., Lauwereys, M.: High-level secretion and very efficient isotopic labeling of tick anticoagulant peptide (TAP) expressed in the methylotrophic yeast, Pichia pastoris. Bio/Technology 12, 1119-1124 (1994)
    • (1994) Bio/Technology , vol.12 , pp. 1119-1124
    • Laroche, Y.1    Storme, V.2    De Meutter, J.3    Messens, J.4    Lauwereys, M.5
  • 14
    • 0034742111 scopus 로고    scopus 로고
    • 15N double labeling of the avirulence protein AVR4 in a methanol-utilizing strain (Mut+) of Pichia pastoris
    • 15N double labeling of the avirulence protein AVR4 in a methanol-utilizing strain (Mut+) of Pichia pastoris. J. Biomol. NMR 20, 251-261 (2001)
    • (2001) J. Biomol. NMR , vol.20 , pp. 251-261
    • Van Den Burg, H.A.1    De Wit, P.J.G.M.2    Vervoort, J.3
  • 15
  • 16
    • 0025340220 scopus 로고
    • Two simple and rapid methods to detect monoclonal antibodies with identical epitope specificities in a large population of monoclonal antibodies
    • Dighe, R.R., Murthy, G.S., Moudgal, N.R.: Two simple and rapid methods to detect monoclonal antibodies with identical epitope specificities in a large population of monoclonal antibodies. J. Immunol. Methods 131, 229-236 (1990)
    • (1990) J. Immunol. Methods , vol.131 , pp. 229-236
    • Dighe, R.R.1    Murthy, G.S.2    Moudgal, N.R.3
  • 17
    • 0020590536 scopus 로고
    • Use of α- And β-subunit specific antibodies in studying interaction of hCG with Leydig cell receptors
    • Dighe, R.R., Moudgal, N.R.: Use of α- and β-subunit specific antibodies in studying interaction of hCG with Leydig cell receptors. Arch. Biochem. Biophys. 225, 490-499 (1983)
    • (1983) Arch. Biochem. Biophys. , vol.225 , pp. 490-499
    • Dighe, R.R.1    Moudgal, N.R.2
  • 19
    • 34447326804 scopus 로고
    • A simple and rapid method for the permethylation of carbohydrates
    • Ciucanu, I., and Kerek, F.: A simple and rapid method for the permethylation of carbohydrates. Carbohydr. Res. 131, 209-219 (1984)
    • (1984) Carbohydr. Res. , vol.131 , pp. 209-219
    • Ciucanu, I.1    Kerek, F.2
  • 21
    • 0029164230 scopus 로고
    • Nonselective and efficient fluorescent labeling of glycans using 2-aminobenzamide and anthranilic acid
    • Bigge, J.C., Patel, T.P., Bruce, J.A., Goulding, P.N., Charles, S.M., Parekh, R.B.: Nonselective and efficient fluorescent labeling of glycans using 2-aminobenzamide and anthranilic acid. Anal. Biochem. 230, 229-238 (1995)
    • (1995) Anal. Biochem. , vol.230 , pp. 229-238
    • Bigge, J.C.1    Patel, T.P.2    Bruce, J.A.3    Goulding, P.N.4    Charles, S.M.5    Parekh, R.B.6
  • 22
    • 44949276869 scopus 로고
    • Sensitivity improvement in proton-detected two-dimensional heteronuclear correlation NMR spectroscopy
    • Palmer, A.G., III, Cavanagh, J., Wright, P.E., Rance, M.: Sensitivity improvement in proton-detected two-dimensional heteronuclear correlation NMR spectroscopy. J. Magn. Reson. 93, 151-170 (1991)
    • (1991) J. Magn. Reson. , vol.93 , pp. 151-170
    • Palmer III, A.G.1    Cavanagh, J.2    Wright, P.E.3    Rance, M.4
  • 23
    • 0006925492 scopus 로고
    • Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity
    • Kay, L.E., Keifer, P., Saarinen, T.: Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity. J. Am. Chem. Soc. 114, 10663-10665 (1992)
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 10663-10665
    • Kay, L.E.1    Keifer, P.2    Saarinen, T.3
  • 25
    • 0021983928 scopus 로고
    • Isolation of alcohol oxidase and two other methanol regulatable genes from the yeast Pichia pastoris
    • Ellis, S.B., Brust, P.F., Koutz, P.J., Waters, A.F., Harpold, M.M., Gingeras, T.R.: Isolation of alcohol oxidase and two other methanol regulatable genes from the yeast Pichia pastoris. Mol. Cell. Biol. 5, 1111-1121 (1985)
    • (1985) Mol. Cell. Biol. , vol.5 , pp. 1111-1121
    • Ellis, S.B.1    Brust, P.F.2    Koutz, P.J.3    Waters, A.F.4    Harpold, M.M.5    Gingeras, T.R.6
  • 26
    • 0023650956 scopus 로고
    • Expression of the lacZ gene from two methanol-regulated promoters in Pichia pastoris
    • Tschopp, J.F., Brust, P.F., Cregg, J.M., Stillman, C.A., Gingeras, T.R.: Expression of the lacZ gene from two methanol-regulated promoters in Pichia pastoris. Nucleic Acids Res. 9, 3859-3876 (1987)
    • (1987) Nucleic Acids Res. , vol.9 , pp. 3859-3876
    • Tschopp, J.F.1    Brust, P.F.2    Cregg, J.M.3    Stillman, C.A.4    Gingeras, T.R.5
  • 27
    • 0032587512 scopus 로고    scopus 로고
    • Production of isotopically labeled protein in Pichia pastoris by fermentation
    • Wood, M.J., Komives, E.A.: Production of isotopically labeled protein in Pichia pastoris by fermentation. J. Biomol. NMR 13, 149-159 (1999)
    • (1999) J. Biomol. NMR , vol.13 , pp. 149-159
    • Wood, M.J.1    Komives, E.A.2
  • 28
    • 0034923785 scopus 로고    scopus 로고
    • 13C isotopic labeling of proteins expressed in Pichia pastoris
    • 13C isotopic labeling of proteins expressed in Pichia pastoris. J. Biochem. 130, 19-22 (2001)
    • (2001) J. Biochem. , vol.130 , pp. 19-22
    • Rodriguez, E.1    Krishna, N.R.2
  • 30
    • 2542450374 scopus 로고    scopus 로고
    • Glycosylation modification improved the characteristics of recombinant chicken cystatin and its application on mackerel surimi
    • Tzeng, S.S., Jiang, S.T.: Glycosylation modification improved the characteristics of recombinant chicken cystatin and its application on mackerel surimi. J. Agric. Food Chem. 52, 3612-3616 (2004)
    • (2004) J. Agric. Food Chem. , vol.52 , pp. 3612-3616
    • Tzeng, S.S.1    Jiang, S.T.2
  • 32
    • 0030749698 scopus 로고    scopus 로고
    • Mass spectrometric characterization of nicked fragments of the β-subunit of human chorionic gonadotropin
    • Liu, C., Bowers, L.D.: Mass spectrometric characterization of nicked fragments of the β-subunit of human chorionic gonadotropin. Clin. Chem. 43, 1172-1181 (1997)
    • (1997) Clin. Chem. , vol.43 , pp. 1172-1181
    • Liu, C.1    Bowers, L.D.2
  • 33
    • 0024336222 scopus 로고
    • Characterization of glycoproteins and their associated oligosaccharides through the use of endoglycosidases
    • Maley, F., Trimble, R.B., Tarentino, A.L., Plummer, T.H. Jr.: Characterization of glycoproteins and their associated oligosaccharides through the use of endoglycosidases. Anal. Biochem. 180, 195-204 (1989)
    • (1989) Anal. Biochem. , vol.180 , pp. 195-204
    • Maley, F.1    Trimble, R.B.2    Tarentino, A.L.3    Plummer Jr., T.H.4
  • 34
    • 0024511030 scopus 로고
    • Site-specificity of the chorionic gonadotropin N-linked oligosaccharides in signal transduction
    • Matzuk, M.M., Keene, J.L., Boime, I.: Site-specificity of the chorionic gonadotropin N-linked oligosaccharides in signal transduction. J. Biol. Chem. 264, 2409-2414 (1989)
    • (1989) J. Biol. Chem. , vol.264 , pp. 2409-2414
    • Matzuk, M.M.1    Keene, J.L.2    Boime, I.3
  • 35
    • 0026776801 scopus 로고
    • Comparison of the biological and immunological properties of glycosylation deficient human chorionic gonadotropin variants produced by site directed mutagenesis and chemical deglycosylation
    • Sairam, M.R., Jiang, L.G.: Comparison of the biological and immunological properties of glycosylation deficient human chorionic gonadotropin variants produced by site directed mutagenesis and chemical deglycosylation. Mol. Cell. Endocrinol. 85, 227-235 (1992)
    • (1992) Mol. Cell. Endocrinol. , vol.85 , pp. 227-235
    • Sairam, M.R.1    Jiang, L.G.2
  • 36
    • 0036606845 scopus 로고    scopus 로고
    • Studies on the relevance of the glycan at Asn-52 of the α-subunit of human chorionic gonadotropin in the αβ dimer
    • Erbel, P.J., Haseley, S.R., Kamerling, J.P., Vliegenthart, J.F.G.: Studies on the relevance of the glycan at Asn-52 of the α-subunit of human chorionic gonadotropin in the αβ dimer. Biochem. J. 364, 485-495 (2002)
    • (2002) Biochem. J. , vol.364 , pp. 485-495
    • Erbel, P.J.1    Haseley, S.R.2    Kamerling, J.P.3    Vliegenthart, J.F.G.4
  • 37
    • 0000566952 scopus 로고
    • Complete mass spectra of the per-trimethylsilylated amino acids
    • Leimer, K.R., Rice, R.H., Gehrke, C.W.: Complete mass spectra of the per-trimethylsilylated amino acids. J. Chromatogr. A 141, 355-375 (1977)
    • (1977) J. Chromatogr. a , vol.141 , pp. 355-375
    • Leimer, K.R.1    Rice, R.H.2    Gehrke, C.W.3
  • 38
    • 0028796622 scopus 로고
    • Tryptic mapping of human chorionic gonadotropin by matrix-assisted laser desorption/ionization mass spectrometry
    • Laidler, P., Cowan, D.A., Hider, R.C., Keane, A., Kicman, A.T.: Tryptic mapping of human chorionic gonadotropin by matrix-assisted laser desorption/ionization mass spectrometry. Rapid Commun. Mass Spectrom. 9, 1021-1026 (1995)
    • (1995) Rapid Commun. Mass Spectrom. , vol.9 , pp. 1021-1026
    • Laidler, P.1    Cowan, D.A.2    Hider, R.C.3    Keane, A.4    Kicman, A.T.5
  • 39
    • 0033755856 scopus 로고    scopus 로고
    • Determination of the glycoforms of human chorionic gonadotropin β-core fragment by matrix-assisted laser desorption/ionization mass spectrometry
    • Jacoby, E.S., Kicman, A.T., Laidler, P., Iles, R.K.: Determination of the glycoforms of human chorionic gonadotropin β-core fragment by matrix-assisted laser desorption/ionization mass spectrometry. Clin. Chem. 46, 1796-1803 (2000)
    • (2000) Clin. Chem. , vol.46 , pp. 1796-1803
    • Jacoby, E.S.1    Kicman, A.T.2    Laidler, P.3    Iles, R.K.4
  • 41
    • 0016763284 scopus 로고
    • Gonadotropin and subunit conformation
    • Holladay, L.A., Puett, D.: Gonadotropin and subunit conformation. Arch. Biochem. Biophys. 171, 708-720 (1975)
    • (1975) Arch. Biochem. Biophys. , vol.171 , pp. 708-720
    • Holladay, L.A.1    Puett, D.2
  • 42
    • 0029149009 scopus 로고
    • Bacterial expression of human chorionic gonadotropin α-subunit: Studies on refolding, dimer assembly and interaction with two different β-subunits
    • Ren, P., Sairam, M.R., Yarney, T.A.: Bacterial expression of human chorionic gonadotropin α-subunit: studies on refolding, dimer assembly and interaction with two different β-subunits. Mol. Cell. Endocrinol. 113, 39-51 (1995)
    • (1995) Mol. Cell. Endocrinol. , vol.113 , pp. 39-51
    • Ren, P.1    Sairam, M.R.2    Yarney, T.A.3
  • 43
    • 0027964252 scopus 로고
    • Bacterial expression and in vitro folding of the β-subunit of human chorionic gonadotropin (hCGβ) and functional assembly of recombinant hCGβ with hCGα
    • Huth, J.R., Norton, S.E., Lockridge, O., Shikone, T., Hsueh, A.J.W., Ruddon, R.W.: Bacterial expression and in vitro folding of the β-subunit of human chorionic gonadotropin (hCGβ) and functional assembly of recombinant hCGβ with hCGα. Endocrinology 135, 911-918 (1994)
    • (1994) Endocrinology , vol.135 , pp. 911-918
    • Huth, J.R.1    Norton, S.E.2    Lockridge, O.3    Shikone, T.4    Hsueh, A.J.W.5    Ruddon, R.W.6
  • 44
    • 0026199809 scopus 로고
    • Construction, purification and characterization of a recombinant baculovirus containing the gene for α-subunit of human chorionic gonadotropin
    • Nakhai, B., Sridhar, P., Talwar, G.P., Hasnain, S.E.: Construction, purification and characterization of a recombinant baculovirus containing the gene for α-subunit of human chorionic gonadotropin. Indian J. Biochem. Biophys. 28, 237-242 (1991)
    • (1991) Indian J. Biochem. Biophys. , vol.28 , pp. 237-242
    • Nakhai, B.1    Sridhar, P.2    Talwar, G.P.3    Hasnain, S.E.4
  • 45
    • 0026905698 scopus 로고
    • Over-expression and characterization of recombinant β-subunit of the human chorionic gonadotropin hormone synthesized in insect cells infected with a genetically engineered baculovirus
    • Nakhai, B., Sridhar, P., Pal, R., Talwar, G.P., Hasnain, S.E.: Over-expression and characterization of recombinant β-subunit of the human chorionic gonadotropin hormone synthesized in insect cells infected with a genetically engineered baculovirus. Indian J. Biochem. Biophys. 29, 315-321 (1992)
    • (1992) Indian J. Biochem. Biophys. , vol.29 , pp. 315-321
    • Nakhai, B.1    Sridhar, P.2    Pal, R.3    Talwar, G.P.4    Hasnain, S.E.5
  • 49
    • 0033797841 scopus 로고    scopus 로고
    • Induction of final follicular maturation and early luteinization in women undergoing ovulation induction for assisted reproduction treatment-recombinant hCG versus urinary hCG
    • The European Recombinant Human Chorionic Gonadotrophin Study Group
    • The European Recombinant Human Chorionic Gonadotrophin Study Group: Induction of final follicular maturation and early luteinization in women undergoing ovulation induction for assisted reproduction treatment-recombinant hCG versus urinary hCG. Hum. Reprod. 15, 1446-1451 (2000)
    • (2000) Hum. Reprod. , vol.15 , pp. 1446-1451
  • 50
    • 0034961460 scopus 로고    scopus 로고
    • Recombinant human chorionic gonadotropin (rhCG) in assisted reproductive technology: Results of a clinical trial comparing two doses of rhCG (Ovidrel) to urinary hCG (Profasi) for induction of final follicular maturation in in vitro fertilization-embryo transfer
    • Chang, P., Kenley, S., Burns, T., Denton, G., Currie, K., DeVane, G, O'Dea, L.: Recombinant human chorionic gonadotropin (rhCG) in assisted reproductive technology: results of a clinical trial comparing two doses of rhCG (Ovidrel) to urinary hCG (Profasi) for induction of final follicular maturation in in vitro fertilization-embryo transfer. Fertil. Steril. 76, 67-74 (2001)
    • (2001) Fertil. Steril. , vol.76 , pp. 67-74
    • Chang, P.1    Kenley, S.2    Burns, T.3    Denton, G.4    Currie, K.5    Devane, G.6    O'Dea, L.7
  • 51
    • 0030167995 scopus 로고    scopus 로고
    • Expression of human chorionic gonadotropin uniformly labeled with NMR isotopes in Chinese hamster ovary cells: An advance towards rapid determination of glycoprotein structures
    • Lustbader, J.W., Birken, S., Pollak, S., Pound, A., Chait, B.T., Mirza, U.A., Ramnarain, S., Canfield, R.E., Miles Brown, J.: Expression of human chorionic gonadotropin uniformly labeled with NMR isotopes in Chinese hamster ovary cells: an advance towards rapid determination of glycoprotein structures. J. Biomol. NMR 7, 295-304 (1996)
    • (1996) J. Biomol. NMR , vol.7 , pp. 295-304
    • Lustbader, J.W.1    Birken, S.2    Pollak, S.3    Pound, A.4    Chait, B.T.5    Mirza, U.A.6    Ramnarain, S.7    Canfield, R.E.8    Miles Brown, J.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.