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Volumn 1814, Issue 5, 2011, Pages 610-621

N-linked glycosylation of G. mellonella juvenile hormone binding protein - Comparison of recombinant mutants expressed in P. pastoris cells with native protein

Author keywords

Glycosylation; JHBP; Pichia pastoris

Indexed keywords

ASPARAGINE; CARBOHYDRATE; HORMONE BINDING PROTEIN; JUVENILE HORMONE BINDING PROTEIN; RECOMBINANT PROTEIN; UNCLASSIFIED DRUG;

EID: 79955626612     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2011.02.002     Document Type: Article
Times cited : (6)

References (43)
  • 1
    • 0002652592 scopus 로고    scopus 로고
    • Regulation of JH Titers: The Relevance of Degradative Enzymes and Binding Proteins
    • C.A.D. de Kort, and N.A. Granger Regulation of JH titers: the relevance of degradative enzymes and binding proteins Arch. Insect Biochem. Physiol. 33 1996 1 26 (Pubitemid 126418923)
    • (1996) Archives of Insect Biochemistry and Physiology , vol.33 , Issue.1 , pp. 1-26
    • De Kort, C.A.D.1    Granger, N.A.2
  • 3
    • 0016434437 scopus 로고
    • Role of juvenile hormone esterases and carrier proteins in insect development
    • L.L. Sanburg, K.J. Kramer, F.J. Kezdy, J.H. Law, and H. Oberlander Role of juvenile hormone esterases and carrier proteins in insect development Nature 253 1975 266 267
    • (1975) Nature , vol.253 , pp. 266-267
    • Sanburg, L.L.1    Kramer, K.J.2    Kezdy, F.J.3    Law, J.H.4    Oberlander, H.5
  • 4
    • 0016551547 scopus 로고
    • The influence of hemolymph-binding protein on juvenile hormone stability and distribution in Manduca sexta fat body and imaginal discs in vitro
    • B. Hammock, J. Nowock, W. Goodman, V. Stamoudis, and L.I. Gilbert The influence of hemolymph-binding protein on juvenile hormone stability and distribution in Manduca sexta fat body and imaginal discs in vitro Mol. Cell. Endocrinol. 3 1975 167 184
    • (1975) Mol. Cell. Endocrinol. , vol.3 , pp. 167-184
    • Hammock, B.1    Nowock, J.2    Goodman, W.3    Stamoudis, V.4    Gilbert, L.I.5
  • 5
    • 0023641924 scopus 로고
    • Juvenile-hormone-binding protein from the hemolymph of Galleria mellonella (L). Isolation and characterization
    • A. Ożyhar, and M. Kochman Juvenile-hormone-binding protein from the hemolymph of Galleria mellonella (L). Isolation and characterization Eur. J. Biochem. 162 1987 675 682
    • (1987) Eur. J. Biochem. , vol.162 , pp. 675-682
    • Ozyhar, A.1    Kochman, M.2
  • 6
    • 0036753858 scopus 로고    scopus 로고
    • Cloning and sequence analysis of Galleria mellonella juvenile hormone binding protein - A search for ancestors and relatives
    • DOI 10.1515/BC.2002.153
    • J.M. Rodriguez Parkitna, A. Ożyhar, J.R. Wiśniewski, and M. Kochman Cloning and sequence analysis of Galleria mellonella juvenile hormone binding protein - a search for ancestors and relatives Biol. Chem. 383 2002 1343 1355 (Pubitemid 35282952)
    • (2002) Biological Chemistry , vol.383 , Issue.9 , pp. 1343-1355
    • Parkitna, J.M.R.1    Ozyhar, A.2    Wisniewski, J.R.3    Kochman, M.4
  • 8
    • 40649091053 scopus 로고    scopus 로고
    • Insect juvenile hormone binding protein shows ancestral fold present in human lipid-binding proteins
    • R. Kolodziejczyk, G. Bujacz, M. Jakób, A. Ożyhar, M. Jaskolski, and M. Kochman Insect juvenile hormone binding protein shows ancestral fold present in human lipid-binding proteins J. Mol. Biol. 377 2008 870 881
    • (2008) J. Mol. Biol. , vol.377 , pp. 870-881
    • Kolodziejczyk, R.1    Bujacz, G.2    Jakób, M.3    Ozyhar, A.4    Jaskolski, M.5    Kochman, M.6
  • 9
    • 0026093798 scopus 로고
    • Conformational change of the haemolymph juvenile-hormone-binding protein from Galleria mellonella (L)
    • E. Wieczorek, and M. Kochman Conformational change of the haemolymph juvenile-hormone-binding protein from Galleria mellonella (L) Eur. J. Biochem. 201 1991 347 353
    • (1991) Eur. J. Biochem. , vol.201 , pp. 347-353
    • Wieczorek, E.1    Kochman, M.2
  • 10
    • 0031891850 scopus 로고    scopus 로고
    • UV-difference and CD spectroscopy studies on juvenile hormone binding to its carrier protein
    • D. Krzyzanowska, M. Lisowski, and M. Kochman UV-difference and CD spectroscopy studies on juvenile hormone binding to its carrier protein J. Pept. Res. 51 1998 96 102 (Pubitemid 28092760)
    • (1998) Journal of Peptide Research , vol.51 , Issue.2 , pp. 96-102
    • Krzyzanowska, D.1    Lisowski, M.2    Kochman, M.3
  • 11
    • 0035050715 scopus 로고    scopus 로고
    • The juvenile hormone binding protein of silkworm haemolymph: Gene and functional analysis
    • DOI 10.1046/j.1365-2583.2001.00249.x
    • A.M. Vermunt, M. Kamimura, M. Hirai, M. Kiuchi, and T. Shiotsuki The juvenile hormone binding protein of silkworm haemolymph: gene and functional analysis Insect Mol. Biol. 10 2001 147 154 (Pubitemid 32320270)
    • (2001) Insect Molecular Biology , vol.10 , Issue.2 , pp. 147-154
    • Vermunt, A.M.W.1    Kamimura, M.2    Hirai, M.3    Kiuchi, M.4    Shiotsuki, T.5
  • 12
    • 0028946315 scopus 로고
    • Key disulfide bonds in an insect hormone binding protein: CDNA cloning of a juvenile hormone binding protein of Heliothis virescens and ligand binding by native and mutant forms
    • H. Wojtasek, and G.D. Prestwich Key disulfide bonds in an insect hormone binding protein: cDNA cloning of a juvenile hormone binding protein of Heliothis virescens and ligand binding by native and mutant forms Biochemistry 34 1995 5234 5241
    • (1995) Biochemistry , vol.34 , pp. 5234-5241
    • Wojtasek, H.1    Prestwich, G.D.2
  • 13
    • 0029905993 scopus 로고    scopus 로고
    • Sequence of the hexameric juvenile hormone-binding protein from the hemolymph of Locusta migratoria
    • DOI 10.1074/jbc.271.49.31756
    • R.P. Braun, and G.R. Wyatt Sequence of the hexameric juvenile hormone-binding protein from the hemolymph of Locusta migratoria J. Biol. Chem. 271 1996 31756 31762 (Pubitemid 26408644)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.49 , pp. 31756-31762
    • Braun, R.P.1    Wyatt, G.R.2
  • 15
    • 0035118541 scopus 로고    scopus 로고
    • Characterization of Toxoplasma gondii surface antigen I (SAGI) secreted from Pichia pastoris: Evidence of hyper O-glycosylation
    • DOI 10.1042/BA20000069
    • O. Letourneur, G. Gervasi, S. Gaia, J. Pages, B. Watelet, and M. Jolivet Characterization of Toxoplasma gondii surface antigen 1 (SAG1) secreted from Pichia pastoris: evidence of hyper O-glycosylation Biotechnol. Appl. Biochem. 33 2001 35 45 (Pubitemid 32179388)
    • (2001) Biotechnology and Applied Biochemistry , vol.33 , Issue.1 , pp. 35-45
    • Letourneur, O.1    Gervasi, G.2    Gaia, S.3    Pages, J.4    Watelet, B.5    Jolivet, M.6
  • 16
    • 0034886703 scopus 로고    scopus 로고
    • Glycosylated and phosphorylated proteins - Expression in yeast and oocytes of Xenopus: Prospects and challenges - Relevance to expression of thermostable proteins
    • DOI 10.1006/prep.2001.1431
    • P. Li, X.G. Gao, R.O. Arellano, and V. Renugopalakrishnan Glycosylated and phosphorylated proteins - expression in yeast and oocytes of Xenopus: prospects and challenges - relevance to expression of thermostable proteins Protein Expr. Purif. 22 2001 369 380 (Pubitemid 32745328)
    • (2001) Protein Expression and Purification , vol.22 , Issue.3 , pp. 369-380
    • Li, P.1    Gao, X.-G.2    Arellano, R.O.3    Renugopalakrishnan, V.4
  • 17
    • 17244363998 scopus 로고    scopus 로고
    • Heterologous protein production using the Pichia pastoris expression system
    • DOI 10.1002/yea.1208
    • S. Macauley-Patrick, M.L. Fazenda, B. McNeil, and L.M. Harvey Heterologous protein production using the Pichia pastoris expression system Yeast 22 2005 249 270 (Pubitemid 40528349)
    • (2005) Yeast , vol.22 , Issue.4 , pp. 249-270
    • Macauley-Patrick, S.1    Fazenda, M.L.2    McNeil, B.3    Harvey, L.M.4
  • 18
    • 0024467392 scopus 로고
    • Effects of N-glycosylation on in vitro activity of Bowes melanoma and human colon fibroblast derived tissue plasminogen activator
    • A.J. Wittwer, S.C. Howard, L.S. Carr, N.K. Harakas, J. Feder, R.B. Parekh, P.M. Rudd, R.A. Dwek, and T.W. Rademacher Effects of N-glycosylation on in vitro activity of Bowes melanoma and human colon fibroblast derived tissue plasminogen activator Biochemistry 28 1989 7662 7669 (Pubitemid 19238109)
    • (1989) Biochemistry , vol.28 , Issue.19 , pp. 7662-7669
    • Wittwer, A.J.1    Howard, S.C.2    Carr, L.S.3    Harakas, N.K.4    Feder, J.5    Parekh, R.B.6    Rudd, P.M.7    Dwek, R.A.8    Rademacher, T.W.9
  • 19
    • 0032727842 scopus 로고    scopus 로고
    • Effect of N-linked glycosylation on glycopeptide and glycoprotein structure
    • B. Imperiali, and S.E. O'Connor Effect of N-linked glycosylation on glycopeptide and glycoprotein structure Curr. Opin. Chem. Biol. 3 1999 643 649
    • (1999) Curr. Opin. Chem. Biol. , vol.3 , pp. 643-649
    • Imperiali, B.1    O'Connor, S.E.2
  • 20
    • 0037418742 scopus 로고    scopus 로고
    • The influence of glycosylation on secretion, stability, and immunogenicity of recombinant HBV pre-S antigen synthesized in Saccharomyces cerevisiae
    • DOI 10.1016/S0006-291X(03)00351-6
    • J. Lee, J.S. Park, J.Y. Moon, K.Y. Kim, and H.M. Moon The influence of glycosylation on secretion, stability, and immunogenicity of recombinant HBV pre-S antigen synthesized in Saccharomyces cerevisiae Biochem. Biophys. Res. Commun. 303 2003 427 432 (Pubitemid 36349186)
    • (2003) Biochemical and Biophysical Research Communications , vol.303 , Issue.2 , pp. 427-432
    • Lee, J.1    Park, J.-S.2    Moon, J.-Y.3    Kim, K.-Y.4    Moon, H.-M.5
  • 21
    • 0034053424 scopus 로고    scopus 로고
    • Characteristics of glycosylated streptokinase secreted from Pichia pastoris: Enhanced resistance of SK to proteolysis by glycosylation
    • J. Pratap, G. Rajamohan, and K.L. Dikshit Characteristics of glycosylated streptokinase secreted from Pichia pastoris: enhanced resistance of SK to proteolysis by glycosylation Appl. Microbiol. Biotechnol. 53 2000 469 475 (Pubitemid 30236122)
    • (2000) Applied Microbiology and Biotechnology , vol.53 , Issue.4 , pp. 469-475
    • Pratap, J.1    Rajamohan, G.2    Dikshit, K.L.3
  • 22
    • 0141730230 scopus 로고    scopus 로고
    • The contribution of N-glycans and their processing in the endoplasmic reticulum to glycoprotein biosynthesis
    • DOI 10.1093/glycob/cwg075
    • E.S. Trombetta The contribution of N-glycans and their processing in the endoplasmic reticulum to glycoprotein biosynthesis Glycobiology 13 2003 77R 91R (Pubitemid 37220438)
    • (2003) Glycobiology , vol.13 , Issue.9
    • Trombetta, E.S.1
  • 23
    • 0024637162 scopus 로고
    • Size distribution and general structural features of N-linked oligosaccharides from the methylotrophic yeast, Pichia pastoris
    • L.S. Grinna, and J.F. Tschopp Size distribution and general structural features of N-linked oligosaccharides from the methylotrophic yeast, Pichia pastoris Yeast 5 1989 107 115
    • (1989) Yeast , vol.5 , pp. 107-115
    • Grinna, L.S.1    Tschopp, J.F.2
  • 24
    • 0026020091 scopus 로고
    • 1 and endo H hydrolyze only high mannose and hybrid glycans
    • R.B. Trimble, and A.L. Tarentino Identification of distinct endoglycosidase (endo) activities in Flavobacterium meningosepticum: endo F1, endo F2, and endo F3. Endo F1 and endo H hydrolyze only high mannose and hybrid glycans J. Biol. Chem. 266 1991 1646 1651 (Pubitemid 21908350)
    • (1991) Journal of Biological Chemistry , vol.266 , Issue.3 , pp. 1646-1651
    • Trimble, R.B.1    Tarentino, A.L.2
  • 25
    • 0029778534 scopus 로고    scopus 로고
    • Functional analysis of the glycosylation of murine acid sphingomyelinase
    • DOI 10.1074/jbc.271.50.32089
    • D. Newrzella, and W. Stoffel Functional analysis of the glycosylation of murine acid sphingomyelinase J. Biol. Chem. 271 1996 32089 32095 (Pubitemid 26422239)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.50 , pp. 32089-32095
    • Newrzella, D.1    Stoffel, W.2
  • 26
    • 0028880799 scopus 로고
    • The effects of the site-directed removal of N-glycosylation sites from β-1, 4-N-acetylgalactosaminyltransferase on its function
    • M. Haraguchi, S. Yamashiro, K. Furukawa, K. Takamiya, H. Shiku, and K. Furukawa The effects of the site-directed removal of N-glycosylation sites from β-1, 4-N-acetylgalactosaminyltransferase on its function Biochem. J. 312 1995 273 280
    • (1995) Biochem. J. , vol.312 , pp. 273-280
    • Haraguchi, M.1    Yamashiro, S.2    Furukawa, K.3    Takamiya, K.4    Shiku, H.5    Furukawa, K.6
  • 27
    • 0000483960 scopus 로고
    • Age dependent changes in the binding and hydrolysis of juvenile hormone in the haemolymph of Galleria mellonella
    • A. Ożyhar, J. Wiśniewski, F. Sehnal, and M. Kochman Age dependent changes in the binding and hydrolysis of juvenile hormone in the haemolymph of Galleria mellonella Insect Biochem. 13 1983 435 441
    • (1983) Insect Biochem. , vol.13 , pp. 435-441
    • Ozyhar, A.1    Wiśniewski, J.2    Sehnal, F.3    Kochman, M.4
  • 28
    • 0030334651 scopus 로고    scopus 로고
    • Immunoaffinity purification of juvenile hormone-binding protein from Galleria mellonella hemolymph
    • E. Wieczorek, J.M. Rodriguez Parkitna, J. Szkudlarek, A. Ożyhar, and M. Kochman Immunoaffinity purification of juvenile hormone-binding protein from Galleria mellonella hemolymph Acta Biochim. Pol. 43 1996 603 610 (Pubitemid 126417446)
    • (1996) Acta Biochimica Polonica , vol.43 , Issue.4 , pp. 603-610
    • Wieczorek, E.1    Rodriguez Parkitna, J.M.2    Szkudlarek, J.3    Ozyhar, A.4    Kochman, M.5
  • 29
    • 0017992640 scopus 로고
    • Purification and characterization of a juvenile hormone binding protein from the hemolymph of the fourth instar tobacco hornworm, Manduca sexta
    • W. Goodman, P.A. O'Hern, R.H. Zaugg, and L.I. Gilbert Purification and characterization of a juvenile hormone binding protein from the hemolymph of the fourth instar tobacco hornworm, Manduca sexta Mol. Cell. Endocrinol. 11 1978 225 242
    • (1978) Mol. Cell. Endocrinol. , vol.11 , pp. 225-242
    • Goodman, W.1    O'Hern, P.A.2    Zaugg, R.H.3    Gilbert, L.I.4
  • 30
    • 0019451644 scopus 로고
    • Immunochemistry of groups A, B, and C meningococcal polysaccharide- tetanus toxoid conjugates
    • H.J. Jennings, and C. Lugowski Immunochemistry of groups A, B, and C meningococcal polysaccharide - tetanus toxoid conjugates J. Immunol. 127 1981 1011 1018 (Pubitemid 11051148)
    • (1981) Journal of Immunology , vol.127 , Issue.3 , pp. 1011-1018
    • Jennings, H.J.1    Lugowski, C.2
  • 32
    • 0029245364 scopus 로고
    • Site-directed mutagenesis by double polymerase chain reaction
    • S. Barik Site-directed mutagenesis by double polymerase chain reaction Mol. Biotechnol. 3 1995 1 7
    • (1995) Mol. Biotechnol. , vol.3 , pp. 1-7
    • Barik, S.1
  • 33
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • M.M. Bradford A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding Anal. Biochem. 72 1976 248 254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 34
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • U.K. Laemmli Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature 227 1970 680 685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 35
    • 0015236352 scopus 로고
    • Electrophoretic analysis of the major polypeptides of the human erythrocyte membrane
    • G. Fairbanks, T.L. Steck, and D.F. Wallach Electrophoretic analysis of the major polypeptides of the human erythrocyte membrane Biochemistry 10 1971 2606 2617
    • (1971) Biochemistry , vol.10 , pp. 2606-2617
    • Fairbanks, G.1    Steck, T.L.2    Wallach, D.F.3
  • 36
    • 0018786476 scopus 로고
    • Structural determinants of concanavalin A specificity for oligosaccharides
    • J.U. Baenziger, and D. Fiete Structural determinants of concanavalin A specificity for oligosaccharides J. Biol. Chem. 254 1979 2400 2407
    • (1979) J. Biol. Chem. , vol.254 , pp. 2400-2407
    • Baenziger, J.U.1    Fiete, D.2
  • 37
    • 84969001783 scopus 로고
    • The attractions of proteins for small molecules and ions
    • G. Scatchard The attractions of proteins for small molecules and ions Ann. NY Acad. Sci. 51 1949 660 672
    • (1949) Ann. NY Acad. Sci. , vol.51 , pp. 660-672
    • Scatchard, G.1
  • 38
    • 0026327987 scopus 로고
    • Structure of oligosaccharides on Saccharomyces SUC2 invertase secreted by the methylotrophic yeast Pichia pastoris
    • R.B. Trimble, P.H. Atkinson, J.F. Tschopp, R.R. Townsend, and F. Maley Structure of oligosaccharides on Saccharomyces SUC2 invertase secreted by the methylotrophic yeast Pichia pastoris J. Biol. Chem. 5 1991 22807 22817 (Pubitemid 21908723)
    • (1991) Journal of Biological Chemistry , vol.266 , Issue.34 , pp. 22807-22817
    • Trimble, R.B.1    Atkinson, P.H.2    Tschopp, J.F.3    Townsend, R.R.4    Maley, F.5
  • 39
    • 0030843878 scopus 로고    scopus 로고
    • Protection of mice against a lethal influenza challenge by immunization with yeast-derived recombinant influenza neuraminidase
    • W. Martinet, X. Saelens, T. Deroo, S. Neirynck, R. Contreras, W. Min Jou, and W. Fiers Protection of mice against a lethal influenza challenge by immunization with yeast-derived recombinant influenza neuraminidase Eur. J. Biochem. 247 1997 332 338 (Pubitemid 27319521)
    • (1997) European Journal of Biochemistry , vol.247 , Issue.1 , pp. 332-338
    • Martinet, W.1    Saelens, X.2    Deroo, T.3    Neirynck, S.4    Contreras, R.5    Min Jou, W.6    Fiers, W.7
  • 40
    • 0038544334 scopus 로고    scopus 로고
    • Developing baculovirus-insect cell expression systems for humanized recombinant glycoprotein production
    • DOI 10.1016/S0042-6822(03)00120-X, PII S004268220300120X
    • D.L. Jarvis Developing baculovirus-insect cell expression systems for humanized recombinant glycoprotein production Virology 310 2003 1 7 (Pubitemid 38352575)
    • (2003) Virology , vol.310 , Issue.1 , pp. 1-7
    • Jarvis, D.L.1
  • 42
    • 0029916898 scopus 로고    scopus 로고
    • The amino acid at the X position of an Asn-X-Ser sequon is an important determinant of N-linked core-glycosylation efficiency
    • DOI 10.1074/jbc.271.11.6363
    • S.H. Shakin-Eshleman, S.L. Spitalnik, and L. Kasturi The amino acid at the X position of an Asn-X-Ser sequon is an important determinant of N-linked core-glycosylation efficiency J. Biol. Chem. 271 1996 6363 6366 (Pubitemid 26095445)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.11 , pp. 6363-6366
    • Shakin-Eshleman, S.H.1    Spitalnik, S.L.2    Kasturi, L.3


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