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Volumn 365, Issue 4, 2008, Pages 657-663

An efficient method to express GPI-anchor proteins in insect cells

Author keywords

Baculovirus; Glycosylphosphatidylinositols; High Five; Insect cells; N acetylglucosaminyl phosphatidylinositol de N acetylase; N glycosylation; PIGL; SAG1; Sf9; Toxoplasma gondii

Indexed keywords

GLYCOSYLPHOSPHATIDYLINOSITOL ANCHORED PROTEIN; N ACETYLGLUCOSAMINYL PHOSPHATIDYLINOSITOL DE N ACETYLASE; UNCLASSIFIED DRUG;

EID: 36849080955     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2007.11.026     Document Type: Article
Times cited : (6)

References (35)
  • 1
    • 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
  • 2
    • 0036532579 scopus 로고    scopus 로고
    • Recombinant baculoviruses as mammalian cell gene-delivery vectors
    • Kost T.A., and Condreay J.P. Recombinant baculoviruses as mammalian cell gene-delivery vectors. Trends Biotechnol. 20 (2002) 173-180
    • (2002) Trends Biotechnol. , vol.20 , pp. 173-180
    • Kost, T.A.1    Condreay, J.P.2
  • 3
    • 22844450442 scopus 로고    scopus 로고
    • Baculovirus as versatile vectors for protein expression in insect and mammalian cells
    • Kost T.A., Condreay J.P., and Jarvis D.L. Baculovirus as versatile vectors for protein expression in insect and mammalian cells. Nat. Biotechnol. 23 (2005) 567-575
    • (2005) Nat. Biotechnol. , vol.23 , pp. 567-575
    • Kost, T.A.1    Condreay, J.P.2    Jarvis, D.L.3
  • 4
    • 0035169615 scopus 로고    scopus 로고
    • Baculovirus infection of nondividing mammalian cells: mechanisms of entry and nuclear transport of capsids
    • van Loo N.D., Fortunati E., Ehlert E., Rabelink M., Grosveld F., and Scholte B.J. Baculovirus infection of nondividing mammalian cells: mechanisms of entry and nuclear transport of capsids. J. Virol. 75 (2001) 961-970
    • (2001) J. Virol. , vol.75 , pp. 961-970
    • van Loo, N.D.1    Fortunati, E.2    Ehlert, E.3    Rabelink, M.4    Grosveld, F.5    Scholte, B.J.6
  • 5
    • 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. Glycoconj. J. 16 (1999) 109-123
    • (1999) Glycoconj. J. , vol.16 , pp. 109-123
    • Altmann, F.1    Staudacher, E.2    Wilson, I.B.3    Marz, L.4
  • 6
    • 33748742271 scopus 로고    scopus 로고
    • Protein N-glycosylation in the baculovirus-insect cell expression system and engineering of insect cells to produce "mammalianized" recombinant glycoproteins
    • Harrison R.L., and Jarvis D.L. Protein N-glycosylation in the baculovirus-insect cell expression system and engineering of insect cells to produce "mammalianized" recombinant glycoproteins. Adv. Virus Res. 68 (2006) 159-191
    • (2006) Adv. Virus Res. , vol.68 , pp. 159-191
    • Harrison, R.L.1    Jarvis, D.L.2
  • 7
    • 0032951863 scopus 로고    scopus 로고
    • Yeast glycosylation-foundations and building blocks
    • Robbins P.W. Yeast glycosylation-foundations and building blocks. Biochim. Biophys. Acta 1426 (1999) 225-226
    • (1999) Biochim. Biophys. Acta , vol.1426 , pp. 225-226
    • Robbins, P.W.1
  • 8
    • 33750468309 scopus 로고    scopus 로고
    • Protein glycosylation, conserved from yeast to man: a model organism helps elucidate congenital human diseases
    • Lehle L., Strahl S., and Tanner W. Protein glycosylation, conserved from yeast to man: a model organism helps elucidate congenital human diseases. Angew Chem. Int. Ed. Engl. 45 (2006) 6802-6818
    • (2006) Angew Chem. Int. Ed. Engl. , vol.45 , pp. 6802-6818
    • Lehle, L.1    Strahl, S.2    Tanner, W.3
  • 9
    • 0023645171 scopus 로고
    • Product of SEC53 is required for folding and glycosylation of secretory proteins in the lumen of the yeast endoplasmic reticulum
    • Feldman R.I., Bernstein M., and Schekman R. Product of SEC53 is required for folding and glycosylation of secretory proteins in the lumen of the yeast endoplasmic reticulum. J. Biol. Chem. 262 (1987) 9332-9339
    • (1987) J. Biol. Chem. , vol.262 , pp. 9332-9339
    • Feldman, R.I.1    Bernstein, M.2    Schekman, R.3
  • 10
    • 0025765996 scopus 로고
    • Removal of N-glycosylation sites of the yeast acid phosphatase severely affects protein folding
    • Riederer M.A., and Hinnen A. Removal of N-glycosylation sites of the yeast acid phosphatase severely affects protein folding. J. Bacteriol. 173 (1991) 3539-3546
    • (1991) J. Bacteriol. , vol.173 , pp. 3539-3546
    • Riederer, M.A.1    Hinnen, A.2
  • 11
    • 2942746462 scopus 로고    scopus 로고
    • Evidence that invasion-inhibitory antibodies specific for the 19-kDa fragment of merozoite surface protein-1 (MSP-1 19) can play a protective role against blood-stage Plasmodium falciparum infection in individuals in a malaria endemic area of Africa
    • John C.C., O'Donnell R.A., Sumba P.O., Moormann A.M., de Koning-Ward T.F., King C.L., Kazura J.W., and Crabb B.S. Evidence that invasion-inhibitory antibodies specific for the 19-kDa fragment of merozoite surface protein-1 (MSP-1 19) can play a protective role against blood-stage Plasmodium falciparum infection in individuals in a malaria endemic area of Africa. J. Immunol. 173 (2004) 666-672
    • (2004) J. Immunol. , vol.173 , pp. 666-672
    • John, C.C.1    O'Donnell, R.A.2    Sumba, P.O.3    Moormann, A.M.4    de Koning-Ward, T.F.5    King, C.L.6    Kazura, J.W.7    Crabb, B.S.8
  • 12
    • 11844261511 scopus 로고    scopus 로고
    • Antibodies to the conserved C-terminal domain of the Plasmodium falciparum merozoite surface protein 1 and to the merozoite extract and their relationship with in vitro inhibitory antibodies and protection against clinical malaria in a Senegalese village
    • Perraut R., Marrama L., Diouf B., Sokhna C., Tall A., Nabeth P., Trape J.F., Longacre S., and Mercereau-Puijalon O. Antibodies to the conserved C-terminal domain of the Plasmodium falciparum merozoite surface protein 1 and to the merozoite extract and their relationship with in vitro inhibitory antibodies and protection against clinical malaria in a Senegalese village. J. Infect. Dis. 191 (2005) 264-271
    • (2005) J. Infect. Dis. , vol.191 , pp. 264-271
    • Perraut, R.1    Marrama, L.2    Diouf, B.3    Sokhna, C.4    Tall, A.5    Nabeth, P.6    Trape, J.F.7    Longacre, S.8    Mercereau-Puijalon, O.9
  • 13
    • 19344365599 scopus 로고    scopus 로고
    • Differential antibody responses to Plasmodium falciparum glycosylphosphatidylinositol anchors in patients with cerebral and mild malaria
    • Perraut R., Diatta B., Marrama L., Garraud O., Jambou R., Longacre S., Krishnegowda G., Dieye A., and Gowda D.C. Differential antibody responses to Plasmodium falciparum glycosylphosphatidylinositol anchors in patients with cerebral and mild malaria. Microbes Infect. 7 (2005) 682-687
    • (2005) Microbes Infect. , vol.7 , pp. 682-687
    • Perraut, R.1    Diatta, B.2    Marrama, L.3    Garraud, O.4    Jambou, R.5    Longacre, S.6    Krishnegowda, G.7    Dieye, A.8    Gowda, D.C.9
  • 14
    • 0031906086 scopus 로고    scopus 로고
    • A longitudinal investigation of IgG and IgM antibody responses to the merozoite surface protein-1 19-kiloDalton domain of Plasmodium falciparum in pregnant women and infants: associations with febrile illness, parasitemia, and anemia
    • Branch O.H., Udhayakumar V., Hightower A.W., Oloo A.J., Hawley W.A., Nahlen B.L., Bloland P.B., Kaslow D.C., and Lal A.A. A longitudinal investigation of IgG and IgM antibody responses to the merozoite surface protein-1 19-kiloDalton domain of Plasmodium falciparum in pregnant women and infants: associations with febrile illness, parasitemia, and anemia. Am. J. Trop. Med. Hyg. 58 (1998) 211-219
    • (1998) Am. J. Trop. Med. Hyg. , vol.58 , pp. 211-219
    • Branch, O.H.1    Udhayakumar, V.2    Hightower, A.W.3    Oloo, A.J.4    Hawley, W.A.5    Nahlen, B.L.6    Bloland, P.B.7    Kaslow, D.C.8    Lal, A.A.9
  • 15
    • 0027268692 scopus 로고
    • The glycoinositol phospholipids of Leishmania mexicana promastigotes. Evidence for the presence of three distinct pathways of glycolipid biosynthesis
    • McConville M.J., Collidge T.A., Ferguson M.A., and Schneider P. The glycoinositol phospholipids of Leishmania mexicana promastigotes. Evidence for the presence of three distinct pathways of glycolipid biosynthesis. J. Biol. Chem. 268 (1993) 15595-15604
    • (1993) J. Biol. Chem. , vol.268 , pp. 15595-15604
    • McConville, M.J.1    Collidge, T.A.2    Ferguson, M.A.3    Schneider, P.4
  • 16
    • 0032820595 scopus 로고    scopus 로고
    • The structure, biosynthesis and functions of glycosylphosphatidylinositol anchors, and the contributions of trypanosome research
    • Ferguson M.A. The structure, biosynthesis and functions of glycosylphosphatidylinositol anchors, and the contributions of trypanosome research. J. Cell Sci. 112 Pt 17 (1999) 2799-2809
    • (1999) J. Cell Sci. , vol.112 , Issue.PART 17 , pp. 2799-2809
    • Ferguson, M.A.1
  • 17
    • 0033229883 scopus 로고    scopus 로고
    • Selective inhibitors of the glycosylphosphatidylinositol biosynthetic pathway of Trypanosoma brucei
    • Smith T.K., Sharma D.K., Crossman A., Brimacombe J.S., and Ferguson M.A. Selective inhibitors of the glycosylphosphatidylinositol biosynthetic pathway of Trypanosoma brucei. Embo J. 18 (1999) 5922-5930
    • (1999) Embo J. , vol.18 , pp. 5922-5930
    • Smith, T.K.1    Sharma, D.K.2    Crossman, A.3    Brimacombe, J.S.4    Ferguson, M.A.5
  • 18
    • 0035796558 scopus 로고    scopus 로고
    • Specificity of GlcNAc-PI de-N-acetylase of GPI biosynthesis and synthesis of parasite-specific suicide substrate inhibitors
    • Smith T.K., Crossman A., Borissow C.N., Paterson M.J., Dix A., Brimacombe J.S., and Ferguson M.A. Specificity of GlcNAc-PI de-N-acetylase of GPI biosynthesis and synthesis of parasite-specific suicide substrate inhibitors. Embo J. 20 (2001) 3322-3332
    • (2001) Embo J. , vol.20 , pp. 3322-3332
    • Smith, T.K.1    Crossman, A.2    Borissow, C.N.3    Paterson, M.J.4    Dix, A.5    Brimacombe, J.S.6    Ferguson, M.A.7
  • 20
    • 33750998494 scopus 로고    scopus 로고
    • CHO glycosylation mutants: GPI anchor
    • Maeda Y., Ashida H., and Kinoshita T. CHO glycosylation mutants: GPI anchor. Methods Enzymol. 416 (2006) 182-205
    • (2006) Methods Enzymol. , vol.416 , pp. 182-205
    • Maeda, Y.1    Ashida, H.2    Kinoshita, T.3
  • 21
    • 0030039444 scopus 로고    scopus 로고
    • Glycosylphosphatidylinositol toxin of Plasmodium up-regulates intercellular adhesion molecule-1, vascular cell adhesion molecule-1, and E-selectin expression in vascular endothelial cells and increases leukocyte and parasite cytoadherence via tyrosine kinase-dependent signal transduction
    • Schofield L., Novakovic S., Gerold P., Schwarz R.T., McConville M.J., and Tachado S.D. Glycosylphosphatidylinositol toxin of Plasmodium up-regulates intercellular adhesion molecule-1, vascular cell adhesion molecule-1, and E-selectin expression in vascular endothelial cells and increases leukocyte and parasite cytoadherence via tyrosine kinase-dependent signal transduction. J. Immunol. 156 (1996) 1886-1896
    • (1996) J. Immunol. , vol.156 , pp. 1886-1896
    • Schofield, L.1    Novakovic, S.2    Gerold, P.3    Schwarz, R.T.4    McConville, M.J.5    Tachado, S.D.6
  • 22
    • 0035831443 scopus 로고    scopus 로고
    • Plasmodium falciparum glycosylphosphatidylinositol-induced TNF-alpha secretion by macrophages is mediated without membrane insertion or endocytosis
    • Vijaykumar M., Naik R.S., and Gowda D.C. Plasmodium falciparum glycosylphosphatidylinositol-induced TNF-alpha secretion by macrophages is mediated without membrane insertion or endocytosis. J. Biol. Chem. 276 (2001) 6909-6912
    • (2001) J. Biol. Chem. , vol.276 , pp. 6909-6912
    • Vijaykumar, M.1    Naik, R.S.2    Gowda, D.C.3
  • 24
    • 0034026299 scopus 로고    scopus 로고
    • An early step of glycosylphosphatidyl-inositol anchor biosynthesis is abolished in lepidopteran insect cells following baculovirus infection
    • Azzouz N., Kedees M.H., Gerold P., Becker S., Dubremetz J.F., Klenk H.D., Eckert V., and Schwarz R.T. An early step of glycosylphosphatidyl-inositol anchor biosynthesis is abolished in lepidopteran insect cells following baculovirus infection. Glycobiology 10 (2000) 177-183
    • (2000) Glycobiology , vol.10 , pp. 177-183
    • Azzouz, N.1    Kedees, M.H.2    Gerold, P.3    Becker, S.4    Dubremetz, J.F.5    Klenk, H.D.6    Eckert, V.7    Schwarz, R.T.8
  • 26
    • 0036591274 scopus 로고    scopus 로고
    • Plasmodium falciparum: glycosylation status of Plasmodium falciparum circumsporozoite protein expressed in the baculovirus system
    • Kedees M.H., Azzouz N., Gerold P., Shams-Eldin H., Iqbal J., Eckert V., and Schwarz R.T. Plasmodium falciparum: glycosylation status of Plasmodium falciparum circumsporozoite protein expressed in the baculovirus system. Exp. Parasitol. 101 (2002) 64-68
    • (2002) Exp. Parasitol. , vol.101 , pp. 64-68
    • Kedees, M.H.1    Azzouz, N.2    Gerold, P.3    Shams-Eldin, H.4    Iqbal, J.5    Eckert, V.6    Schwarz, R.T.7
  • 27
    • 1942501817 scopus 로고    scopus 로고
    • Subcellular localization and targeting of N-acetylglucosaminyl phosphatidylinositol de-N-acetylase, the second enzyme in the glycosylphosphatidylinositol biosynthetic pathway
    • Pottekat A., and Menon A.K. Subcellular localization and targeting of N-acetylglucosaminyl phosphatidylinositol de-N-acetylase, the second enzyme in the glycosylphosphatidylinositol biosynthetic pathway. J. Biol. Chem. 279 (2004) 15743-15751
    • (2004) J. Biol. Chem. , vol.279 , pp. 15743-15751
    • Pottekat, A.1    Menon, A.K.2
  • 29
    • 0023737790 scopus 로고
    • Molecular analysis of the gene encoding the major surface antigen of Toxoplasma gondii
    • Burg J.L., Perelman D., Kasper L.H., Ware P.L., and Boothroyd J.C. Molecular analysis of the gene encoding the major surface antigen of Toxoplasma gondii. J. Immunol. 141 (1988) 3584-3591
    • (1988) J. Immunol. , vol.141 , pp. 3584-3591
    • Burg, J.L.1    Perelman, D.2    Kasper, L.H.3    Ware, P.L.4    Boothroyd, J.C.5
  • 30
    • 0027310836 scopus 로고
    • Transient transfection and expression in the obligate intracellular parasite Toxoplasma gondii
    • Soldati D., and Boothroyd J.C. Transient transfection and expression in the obligate intracellular parasite Toxoplasma gondii. Science 260 (1993) 349-352
    • (1993) Science , vol.260 , pp. 349-352
    • Soldati, D.1    Boothroyd, J.C.2
  • 31
    • 0027976238 scopus 로고
    • Conformationally appropriate expression of the Toxoplasma antigen SAG1 (p30) in CHO cells
    • Kim K., Bulow R., Kampmeier J., and Boothroyd J.C. Conformationally appropriate expression of the Toxoplasma antigen SAG1 (p30) in CHO cells. Infect. Immun. 62 (1994) 203-209
    • (1994) Infect. Immun. , vol.62 , pp. 203-209
    • Kim, K.1    Bulow, R.2    Kampmeier, J.3    Boothroyd, J.C.4
  • 32
    • 0033119014 scopus 로고    scopus 로고
    • Mammalian PIG-L and its yeast homologue Gpi12p are N-acetylglucosaminylphosphatidylinositol de-N-acetylases essential in glycosylphosphatidylinositol biosynthesis
    • Watanabe R., Ohishi K., Maeda Y., Nakamura N., and Kinoshita T. Mammalian PIG-L and its yeast homologue Gpi12p are N-acetylglucosaminylphosphatidylinositol de-N-acetylases essential in glycosylphosphatidylinositol biosynthesis. Biochem. J. 339 Pt 1 (1999) 185-192
    • (1999) Biochem. J. , vol.339 , Issue.PART 1 , pp. 185-192
    • Watanabe, R.1    Ohishi, K.2    Maeda, Y.3    Nakamura, N.4    Kinoshita, T.5
  • 33
    • 0025287959 scopus 로고
    • Venom and viral expression products of the endoparasitic wasp Campoletis sonorensis share epitopes and related sequences
    • Webb B.A., and Summers M.D. Venom and viral expression products of the endoparasitic wasp Campoletis sonorensis share epitopes and related sequences. Proc. Natl. Acad. Sci. USA 87 (1990) 4961-4965
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 4961-4965
    • Webb, B.A.1    Summers, M.D.2
  • 34
    • 0019887744 scopus 로고
    • Phase separation of integral membrane proteins in Triton X-114 solution
    • Bordier C. Phase separation of integral membrane proteins in Triton X-114 solution. J. Biol. Chem. 256 (1981) 1604-1607
    • (1981) J. Biol. Chem. , vol.256 , pp. 1604-1607
    • Bordier, C.1
  • 35
    • 0029877528 scopus 로고    scopus 로고
    • Glycosylation in lepidopteran insect cells: identification of a beta 1→4-N-acetylgalactosaminyltransferase involved in the synthesis of complex-type oligosaccharide chains
    • van Die I., van Tetering A., Bakker H., van den Eijnden D.H., and Joziasse D.H. Glycosylation in lepidopteran insect cells: identification of a beta 1→4-N-acetylgalactosaminyltransferase involved in the synthesis of complex-type oligosaccharide chains. Glycobiology 6 (1996) 157-164
    • (1996) Glycobiology , vol.6 , pp. 157-164
    • van Die, I.1    van Tetering, A.2    Bakker, H.3    van den Eijnden, D.H.4    Joziasse, D.H.5


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