메뉴 건너뛰기




Volumn 73, Issue 2, 2010, Pages 113-124

The production, characterisation and enhanced pharmacokinetics of scFv-albumin fusions expressed in Saccharomyces cerevisiae

Author keywords

Albumin fusions; Heterologous protein expression; Saccharomyces cerevisiae; scFv; scFv albumin fusions

Indexed keywords

ALBUMINOID; FLUORESCEIN ISOTHIOCYANATE; FLUORESCENT DYE; HYBRID PROTEIN; SERUM ALBUMIN; SINGLE CHAIN FRAGMENT VARIABLE ANTIBODY;

EID: 77955418625     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2010.05.009     Document Type: Article
Times cited : (40)

References (47)
  • 1
    • 0035970278 scopus 로고    scopus 로고
    • Yeast 2 micron plasmid copy number is elevated by a mutation in the nuclear gene UBC4
    • D. Sleep, C. Finnis, A. Turner, and L. Evans Yeast 2 micron plasmid copy number is elevated by a mutation in the nuclear gene UBC4 Yeast 18 2001 403 421
    • (2001) Yeast , vol.18 , pp. 403-421
    • Sleep, D.1    Finnis, C.2    Turner, A.3    Evans, L.4
  • 2
    • 0032579311 scopus 로고    scopus 로고
    • Disruption of the Saccharomyces cerevisiae YAP3 gene reduces the proteolytic degradation of secreted recombinant human albumin
    • S.M. Kerry-Williams, S.C. Gilbert, L.R. Evans, and D.J. Ballance Disruption of the Saccharomyces cerevisiae YAP3 gene reduces the proteolytic degradation of secreted recombinant human albumin Yeast 14 1998 161 169
    • (1998) Yeast , vol.14 , pp. 161-169
    • Kerry-Williams, S.M.1    Gilbert, S.C.2    Evans, L.R.3    Ballance, D.J.4
  • 5
    • 57449090438 scopus 로고    scopus 로고
    • Modulation of chaperone gene expression in mutagenized Saccharomyces cerevisiae strains developed for recombinant human albumin production results in increased production of multiple heterologous proteins
    • T. Payne, C. Finnis, L.R. Evans, D.J. Mead, S.V. Avery, D.B. Archer, and D. Sleep Modulation of chaperone gene expression in mutagenized Saccharomyces cerevisiae strains developed for recombinant human albumin production results in increased production of multiple heterologous proteins Appl. Environ. Microbiol. 74 2008 7759 7766
    • (2008) Appl. Environ. Microbiol. , vol.74 , pp. 7759-7766
    • Payne, T.1    Finnis, C.2    Evans, L.R.3    Mead, D.J.4    Avery, S.V.5    Archer, D.B.6    Sleep, D.7
  • 12
    • 2942722679 scopus 로고    scopus 로고
    • Antibodies and genetically engineered related molecules: Production and purification
    • A.C. Roque, C.R. Lowe, and M.A. Taipa Antibodies and genetically engineered related molecules: production and purification Biotechnol. Prog. 20 2004 639 654
    • (2004) Biotechnol. Prog. , vol.20 , pp. 639-654
    • Roque, A.C.1    Lowe, C.R.2    Taipa, M.A.3
  • 13
    • 64349107630 scopus 로고    scopus 로고
    • Development trends for therapeutic antibody fragments
    • A.L. Nelson, and J.M. Riechert Development trends for therapeutic antibody fragments Nat. Biotechnol. 27 2009 331 337
    • (2009) Nat. Biotechnol. , vol.27 , pp. 331-337
    • Nelson, A.L.1    Riechert, J.M.2
  • 14
    • 27144432842 scopus 로고    scopus 로고
    • Engineered antibody fragments and the rise of single domains
    • P. Holliger, and P.J. Hudson Engineered antibody fragments and the rise of single domains Nat. Biotechnol. 23 2005 1126 1136
    • (2005) Nat. Biotechnol. , vol.23 , pp. 1126-1136
    • Holliger, P.1    Hudson, P.J.2
  • 15
    • 27144550160 scopus 로고    scopus 로고
    • Arming antibodies: Prospects and challenges for immunoconjugates
    • A.M. Wu, and P.D. Senter Arming antibodies: prospects and challenges for immunoconjugates Nat. Biotechnol. 23 2005 1137 1146
    • (2005) Nat. Biotechnol. , vol.23 , pp. 1137-1146
    • Wu, A.M.1    Senter, P.D.2
  • 16
    • 0037160031 scopus 로고    scopus 로고
    • Functional consequences of insertions and deletions in the complementarity-determining regions of human antibodies
    • J. Lantto, and M. Ohlin Functional consequences of insertions and deletions in the complementarity-determining regions of human antibodies J. Biol. Chem. 277 2002 45108 45114
    • (2002) J. Biol. Chem. , vol.277 , pp. 45108-45114
    • Lantto, J.1    Ohlin, M.2
  • 18
    • 0037227517 scopus 로고    scopus 로고
    • Biophysical properties of human antibody variable domains
    • S. Ewert, T. Huber, A. Honegger, and A. Pluckthun Biophysical properties of human antibody variable domains J. Mol. Biol. 325 2003 531 553
    • (2003) J. Mol. Biol. , vol.325 , pp. 531-553
    • Ewert, S.1    Huber, T.2    Honegger, A.3    Pluckthun, A.4
  • 23
    • 15944388634 scopus 로고    scopus 로고
    • Engineered single chain antibody fragments for radioimmunotherapy
    • A. Huhalov, and K.A. Chester Engineered single chain antibody fragments for radioimmunotherapy Q. J. Nucl. Med. Mol. Imaging 48 2004 279 288
    • (2004) Q. J. Nucl. Med. Mol. Imaging , vol.48 , pp. 279-288
    • Huhalov, A.1    Chester, K.A.2
  • 25
    • 34250361507 scopus 로고    scopus 로고
    • Improved pharmacokinetics of recombinant bispecific antibody molecules by fusion to human serum albumin
    • D. Müller, A. Karle, B. Meissburger, I. Höfig, R. Stork, and R.E. Kontermann Improved pharmacokinetics of recombinant bispecific antibody molecules by fusion to human serum albumin J. Biol. Chem. 282 2007 12650 12660
    • (2007) J. Biol. Chem. , vol.282 , pp. 12650-12660
    • Müller, D.1    Karle, A.2    Meissburger, B.3    Höfig, I.4    Stork, R.5    Kontermann, R.E.6
  • 27
    • 0024451883 scopus 로고
    • A novel class of vector for yeast transformation
    • S.A. Chinery, and E. Hinchliffe A novel class of vector for yeast transformation Curr. Genet. 16 1989 21 25
    • (1989) Curr. Genet. , vol.16 , pp. 21-25
    • Chinery, S.A.1    Hinchliffe, E.2
  • 28
    • 0020529962 scopus 로고
    • Transformation of intact yeast cells treated with alkali cations
    • H. Ito, Y. Fukuda, K. Murata, and A. Kimura Transformation of intact yeast cells treated with alkali cations J. Bacteriol. 153 1983 163 168
    • (1983) J. Bacteriol. , vol.153 , pp. 163-168
    • Ito, H.1    Fukuda, Y.2    Murata, K.3    Kimura, A.4
  • 29
  • 30
    • 0342906412 scopus 로고
    • Production of secreted proteins in yeast
    • S.H. Collins Production of secreted proteins in yeast T.J.R. Harris, Protein Production by Biotechnology 1990 Elsevier Barking 61 77
    • (1990) Protein Production by Biotechnology , pp. 61-77
    • Collins, S.H.1
  • 32
    • 0018085303 scopus 로고
    • A non-barbital buffer for immunoelectrophoresis and zone electrophoresis in agarose gels
    • J.F. Monthony, E.G. Wallace, and D.M. Allen A non-barbital buffer for immunoelectrophoresis and zone electrophoresis in agarose gels Clin. Chem. 24 1978 1825 1827
    • (1978) Clin. Chem. , vol.24 , pp. 1825-1827
    • Monthony, J.F.1    Wallace, E.G.2    Allen, D.M.3
  • 33
    • 0031879861 scopus 로고    scopus 로고
    • Increasing the secretory capacity of Saccharomyces cerevisiae for production of single-chain antibody fragments
    • E.V. Shusta, R.T. Raines, A. Pluckthun, and K.D. Wittrup Increasing the secretory capacity of Saccharomyces cerevisiae for production of single-chain antibody fragments Nat. Biotechnol. 16 1998 773 777
    • (1998) Nat. Biotechnol. , vol.16 , pp. 773-777
    • Shusta, E.V.1    Raines, R.T.2    Pluckthun, A.3    Wittrup, K.D.4
  • 34
    • 24044505375 scopus 로고    scopus 로고
    • Analysis of unfolded protein response during single-chain antibody expression in Saccharomyces cerevisiae reveals different roles for BiP and PDI in folding
    • P. Xu, D. Raden, F.J. Doyle 3rd., and A.S. Robinson Analysis of unfolded protein response during single-chain antibody expression in Saccharomyces cerevisiae reveals different roles for BiP and PDI in folding Metab. Eng. 7 2005 269 279
    • (2005) Metab. Eng. , vol.7 , pp. 269-279
    • Xu, P.1    Raden, D.2    Doyle III, F.J.3    Robinson, A.S.4
  • 35
    • 33744499696 scopus 로고    scopus 로고
    • Engineering of Pichia pastoris for improved production of antibody fragments
    • B. Gasser, M. Maurer, J. Gach, R. Kunert, and D. Mattanovich Engineering of Pichia pastoris for improved production of antibody fragments Biotechnol. Bioeng. 94 2006 353 361
    • (2006) Biotechnol. Bioeng. , vol.94 , pp. 353-361
    • Gasser, B.1    Maurer, M.2    Gach, J.3    Kunert, R.4    Mattanovich, D.5
  • 36
    • 33846841181 scopus 로고    scopus 로고
    • Co-overexpression of chaperones for enhanced secretion of a single-chain antibody fragment in Pichia pastoris
    • L.M. Damasceno, K.A. Anderson, G. Ritter, J.M. Cregg, L.J. Old, and C.A. Batt Co-overexpression of chaperones for enhanced secretion of a single-chain antibody fragment in Pichia pastoris Appl. Microbiol. Biotechnol. 74 2007 381 389
    • (2007) Appl. Microbiol. Biotechnol. , vol.74 , pp. 381-389
    • Damasceno, L.M.1    Anderson, K.A.2    Ritter, G.3    Cregg, J.M.4    Old, L.J.5    Batt, C.A.6
  • 37
    • 0031657285 scopus 로고    scopus 로고
    • Comparison of expression systems in the yeasts Saccharomyces cerevisiae, Hansenula polymorpha, Klyveromyces lactis, Schizosaccharomyces pombe and Yarrowia lipolytica. Cloning of two novel promoters from Yarrowia lipolytica
    • S. Müller, T. Sandal, P. Kamp-Hansen, and H. Dalbøge Comparison of expression systems in the yeasts Saccharomyces cerevisiae, Hansenula polymorpha, Klyveromyces lactis, Schizosaccharomyces pombe and Yarrowia lipolytica. Cloning of two novel promoters from Yarrowia lipolytica Yeast 14 1998 1267 1283
    • (1998) Yeast , vol.14 , pp. 1267-1283
    • Müller, S.1    Sandal, T.2    Kamp-Hansen, P.3    Dalbøge, H.4
  • 38
    • 0037394871 scopus 로고    scopus 로고
    • Effects of inactivation and constitutive expression of the unfolded-protein response pathway on protein production in the yeast Saccharomyces cerevisiae
    • M. Valkonen, M. Penttilä, and M. Saloheimo Effects of inactivation and constitutive expression of the unfolded-protein response pathway on protein production in the yeast Saccharomyces cerevisiae Appl. Environ. Microbiol. 69 2003 2065 2072
    • (2003) Appl. Environ. Microbiol. , vol.69 , pp. 2065-2072
    • Valkonen, M.1    Penttilä, M.2    Saloheimo, M.3
  • 39
    • 0000695553 scopus 로고    scopus 로고
    • Applications of yeast in biotechnology: Protein production and genetic analysis
    • G.P. Cereghino, and J.M. Cregg Applications of yeast in biotechnology: protein production and genetic analysis Curr. Opin. Biotechnol. 10 1999 422 427
    • (1999) Curr. Opin. Biotechnol. , vol.10 , pp. 422-427
    • Cereghino, G.P.1    Cregg, J.M.2
  • 40
    • 0033955337 scopus 로고    scopus 로고
    • Heterologous protein expression in the methylotrophic yeast Pichia pastoris
    • J.L. Cereghino, and J.M. Cregg Heterologous protein expression in the methylotrophic yeast Pichia pastoris FEMS Microbiol. Rev. 24 2000 45 66
    • (2000) FEMS Microbiol. Rev. , vol.24 , pp. 45-66
    • Cereghino, J.L.1    Cregg, J.M.2
  • 42
    • 3543069439 scopus 로고    scopus 로고
    • An optimized fermentation process for high-level production of a single-chain Fv antibody fragment in Pichia pastoris
    • L.M. Damasceno, I. Pla, H.J. Chang, L. Cohen, G. Ritter, L.J. Old, and C.A. Batt An optimized fermentation process for high-level production of a single-chain Fv antibody fragment in Pichia pastoris Protein Expr. Purif. 37 2004 18 26
    • (2004) Protein Expr. Purif. , vol.37 , pp. 18-26
    • Damasceno, L.M.1    Pla, I.2    Chang, H.J.3    Cohen, L.4    Ritter, G.5    Old, L.J.6    Batt, C.A.7
  • 43
    • 27644474730 scopus 로고    scopus 로고
    • Expression of the major olive pollen allergen Ole e 10 in the yeast Pichia pastoris: Evidence of post-translational modifications
    • P. Barral, E. Batanero, M. Villalba, and R. Rodríguez Expression of the major olive pollen allergen Ole e 10 in the yeast Pichia pastoris: evidence of post-translational modifications Protein Expr. Purif. 44 2005 147 154
    • (2005) Protein Expr. Purif. , vol.44 , pp. 147-154
    • Barral, P.1    Batanero, E.2    Villalba, M.3    Rodríguez, R.4
  • 44
    • 47749104481 scopus 로고    scopus 로고
    • Increasing the homogeneity, stability and activity of human serum albumin and interferon-alpha2b fusion protein by linker engineering
    • H.L. Zhao, X.Q. Yao, C. Xue, Y. Wang, X.H. Xiong, and Z.M. Liu Increasing the homogeneity, stability and activity of human serum albumin and interferon-alpha2b fusion protein by linker engineering Protein Expr. Purif. 61 2008 73 77
    • (2008) Protein Expr. Purif. , vol.61 , pp. 73-77
    • Zhao, H.L.1    Yao, X.Q.2    Xue, C.3    Wang, Y.4    Xiong, X.H.5    Liu, Z.M.6
  • 45
    • 4644348208 scopus 로고    scopus 로고
    • Recombinant expression systems in the pharmaceutical industry
    • F.R. Schmidt Recombinant expression systems in the pharmaceutical industry Appl. Microbiol. Biotechnol. 65 2004 363 372
    • (2004) Appl. Microbiol. Biotechnol. , vol.65 , pp. 363-372
    • Schmidt, F.R.1
  • 46
    • 14744285206 scopus 로고    scopus 로고
    • Expression of heterologous proteins in Pichia pastoris: A useful experimental tool in protein engineering and production
    • R. Daly, and M.T. Hearn Expression of heterologous proteins in Pichia pastoris: a useful experimental tool in protein engineering and production J. Mol. Recognit. 18 2005 119 138
    • (2005) J. Mol. Recognit. , vol.18 , pp. 119-138
    • Daly, R.1    Hearn, M.T.2
  • 47
    • 0033180105 scopus 로고    scopus 로고
    • Expressions of recombinant venom allergen, antigen 5 of yellowjacket (Vespula vulgaris) and paper wasp (Polistes annularis), in bacteria or yeast
    • R.I. Monsalve, G. Lu, and T.P. King Expressions of recombinant venom allergen, antigen 5 of yellowjacket (Vespula vulgaris) and paper wasp (Polistes annularis), in bacteria or yeast Protein Expr. Purif. 16 1999 410 416
    • (1999) Protein Expr. Purif. , vol.16 , pp. 410-416
    • Monsalve, R.I.1    Lu, G.2    King, T.P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.