메뉴 건너뛰기




Volumn 12, Issue 1, 2012, Pages 1-13

Rational design and engineering of protein A to obtain the controlled elution profile in monoclonal antibody purification

Author keywords

Antibody affinity purification; Free energy; Molecular mechanics; Protein A; Protein engineering

Indexed keywords


EID: 84862869932     PISSN: 13476297     EISSN: 13470442     Source Type: Journal    
DOI: 10.1273/cbij.12.1     Document Type: Article
Times cited : (7)

References (26)
  • 1
    • 33847660116 scopus 로고    scopus 로고
    • Protein A chromatography for antibody purification
    • Hober, S.; Nord, K.; Linhult, M. Protein A chromatography for antibody purification. J. Chromatogr. B. 2007, 848, 40-47.
    • (2007) J. Chromatogr. B , vol.848 , pp. 40-47
    • Hober, S.1    Nord, K.2    Linhult, M.3
  • 2
    • 33847611596 scopus 로고    scopus 로고
    • Downstream processing of monoclonal antibodies--Application of platform approaches
    • Shukla, A. A.; Hubbard, B.; Tressel, T.; Guhan, S.; Low, D. Downstream processing of monoclonal antibodies--Application of platform approaches. J. Chromatogr. B. 2007, 848, 28-39.
    • (2007) J. Chromatogr. B , vol.848 , pp. 28-39
    • Shukla, A.A.1    Hubbard, B.2    Tressel, T.3    Guhan, S.4    Low, D.5
  • 3
    • 26844510432 scopus 로고    scopus 로고
    • Rational methods for predicting human monoclonal antibodies retention in protein A affinity chromatography and cation exchange chromatography: Structure-based chromatography design for monoclonal antibodies
    • Ishihara, T.; Kadoya, T.; Yoshida, H.; Tamada, T.; Yamamoto, S. Rational methods for predicting human monoclonal antibodies retention in protein A affinity chromatography and cation exchange chromatography: Structure-based chromatography design for monoclonal antibodies. J. Chromatogr. A. 2005, 1093, 126-138.
    • (2005) J. Chromatogr. A , vol.1093 , pp. 126-138
    • Ishihara, T.1    Kadoya, T.2    Yoshida, H.3    Tamada, T.4    Yamamoto, S.5
  • 4
    • 28844477910 scopus 로고    scopus 로고
    • Antibody variable region interactions with Protein A: Implications for the development of generic purification processes
    • Ghose, S.; Allen, M.; Hubbard, B.; Brooks, C.; Cramer, S. M. Antibody variable region interactions with Protein A: Implications for the development of generic purification processes. Biotechnol. Bioengin. 2005, 92, 665-673.
    • (2005) Biotechnol. Bioengin. , vol.92 , pp. 665-673
    • Ghose, S.1    Allen, M.2    Hubbard, B.3    Brooks, C.4    Cramer, S.M.5
  • 6
    • 0030948741 scopus 로고    scopus 로고
    • Staphylococcal protein A binding to VH3 encoded immunoglobulins
    • Potter, K. N.; Li, Y.; Pascual, V.; Capra, J. D. Staphylococcal protein A binding to VH3 encoded immunoglobulins. Int. Rev. Immunol. 1997, 14, 291-308.
    • (1997) Int. Rev. Immunol. , vol.14 , pp. 291-308
    • Potter, K.N.1    Li, Y.2    Pascual, V.3    Capra, J.D.4
  • 7
    • 0030267309 scopus 로고    scopus 로고
    • Staphylococcal protein A simultaneously interacts with framework region 1, complementarity-determining region 2, and framework region 3 on human VH3-encoded Igs
    • Potter, K. N.; Li, Y.; Capra, J. D. Staphylococcal protein A simultaneously interacts with framework region 1, complementarity-determining region 2, and framework region 3 on human VH3-encoded Igs. J. Immunol. 1996, 157, 2982-2988.
    • (1996) J. Immunol. , vol.157 , pp. 2982-2988
    • Potter, K.N.1    Li, Y.2    Capra, J.D.3
  • 8
    • 0030265870 scopus 로고    scopus 로고
    • Differential binding avidities of human IgM for staphylococcal protein A derive from specific germ-line VH3 gene usage
    • Hakoda, M.; Kamatani, N.; Hayashimoto-Kurumada, S.; Silverman, G. J.; Yamanaka, H.; Terai, C.; Kashiwazaki, S. Differential binding avidities of human IgM for staphylococcal protein A derive from specific germ-line VH3 gene usage. J. Immunol. 1996, 157, 2976-2981.
    • (1996) J. Immunol. , vol.157 , pp. 2976-2981
    • Hakoda, M.1    Kamatani, N.2    Hayashimoto-Kurumada, S.3    Silverman, G.J.4    Yamanaka, H.5    Terai, C.6    Kashiwazaki, S.7
  • 9
    • 0027163186 scopus 로고
    • The structural basis of germline-encoded VH3 immunoglobulin binding to staphylococcal protein A
    • Hillson, J. L.; Karr, N. S.; Oppliger, I. R.; Mannik, M.; Sasso, E. H. The structural basis of germline-encoded VH3 immunoglobulin binding to staphylococcal protein A. J. Exp. Med. 1993, 178, 331-336.
    • (1993) J. Exp. Med. , vol.178 , pp. 331-336
    • Hillson, J.L.1    Karr, N.S.2    Oppliger, I.R.3    Mannik, M.4    Sasso, E.H.5
  • 11
    • 0031884383 scopus 로고    scopus 로고
    • All individual domains of staphylococcal protein A show Fab binding
    • Jansson, B.; Uhlen, M.; Nygren, P. All individual domains of staphylococcal protein A show Fab binding. FEMS Immunol. Med. Microbiol. 1998, 20, 69-78.
    • (1998) FEMS Immunol. Med. Microbiol. , vol.20 , pp. 69-78
    • Jansson, B.1    Uhlen, M.2    Nygren, P.3
  • 12
    • 0034625113 scopus 로고    scopus 로고
    • Crystal structure of a Staphylococcus aureus protein A domain complexed with the Fab fragment of a human IgM antibody: Structural basis for recognition of B-cell receptors and superantigen activity
    • Graille, M.; Stura, E. A.; Corper, A. L.; Sutton, B. J.; Taussig, M. J.; Charbonnier, J. B.; Silverman, G. J. Crystal structure of a Staphylococcus aureus protein A domain complexed with the Fab fragment of a human IgM antibody: structural basis for recognition of B-cell receptors and superantigen activity. Proc. Natl. Acad. Sci. U S A. 2000, 97, 5399-5404.
    • (2000) Proc. Natl. Acad. Sci. U S A. , vol.97 , pp. 5399-5404
    • Graille, M.1    Stura, E.A.2    Corper, A.L.3    Sutton, B.J.4    Taussig, M.J.5    Charbonnier, J.B.6    Silverman, G.J.7
  • 13
    • 1842530550 scopus 로고    scopus 로고
    • Improving the tolerance of a protein a analogue to repeated alkaline exposures using a bypass mutagenesis approach
    • Linhult, M.; Gulich, S.; Graslund, T.; Simon, A.; Karlsson, M.; Sjoberg, A.; Nord, K.; Hober S. Improving the tolerance of a protein a analogue to repeated alkaline exposures using a bypass mutagenesis approach. Proteins. 2004, 55, 407-416.
    • (2004) Proteins. , vol.55 , pp. 407-416
    • Linhult, M.1    Gulich, S.2    Graslund, T.3    Simon, A.4    Karlsson, M.5    Sjoberg, A.6    Nord, K.7    Hober, S.8
  • 14
    • 0345045570 scopus 로고    scopus 로고
    • Protein engineering of an IgG-binding domain allows milder elution conditions during affinity chromatography
    • Gulich, S.; Uhlen, M.; Hober, S. Protein engineering of an IgG-binding domain allows milder elution conditions during affinity chromatography. J. Biotechnol. 2000, 76, 233-244.
    • (2000) J. Biotechnol. , vol.76 , pp. 233-244
    • Gulich, S.1    Uhlen, M.2    Hober, S.3
  • 15
    • 17844391852 scopus 로고    scopus 로고
    • Highly Active Mutants of Carbonyl Reductase S1 with Inverted Coenzyme Specificity and Production of Optically Active Alcohols
    • Morikawa, S.; Nakai, T.; Yasohara, Y.; Nanba, H.; Kizaki, N.; Hasegawa, J. Highly Active Mutants of Carbonyl Reductase S1 with Inverted Coenzyme Specificity and Production of Optically Active Alcohols. Biosci. Biotechnol. Biochem. 2005, 69, 544-552.
    • (2005) Biosci. Biotechnol. Biochem. , vol.69 , pp. 544-552
    • Morikawa, S.1    Nakai, T.2    Yasohara, Y.3    Nanba, H.4    Kizaki, N.5    Hasegawa, J.6
  • 17
    • 0027804108 scopus 로고
    • An Effective Solvation Term Based on Atomic Occupancies for Use in Protein Simulations
    • Stouten, P. W.; Froemmel, C.; Nakamura, H.; Sander, C. An Effective Solvation Term Based on Atomic Occupancies for Use in Protein Simulations. Mol. Simul. 1993, 10, 97-120.
    • (1993) Mol. Simul. , vol.10 , pp. 97-120
    • Stouten, P.W.1    Froemmel, C.2    Nakamura, H.3    Sander, C.4
  • 18
    • 0000484499 scopus 로고
    • Hydrophobic parameters of amino-acid side chains from the partitioning of N-acetyl-amino-acid amides
    • Fauchère, J.-L.; Pliska, V. Hydrophobic parameters of amino-acid side chains from the partitioning of N-acetyl-amino-acid amides. Eur. J. Med. Chem.-Chim. Ther. 1983, 18, 369-375.
    • (1983) Eur. J. Med. Chem.-Chim. Ther. , vol.18 , pp. 369-375
    • Fauchère, J.-L.1    Pliska, V.2
  • 19
    • 0022596727 scopus 로고
    • Solvation energy in protein folding and binding
    • Eisenberg, D.; McLachlan, A. D. Solvation energy in protein folding and binding. Nature. 1986, 319, 199-203.
    • (1986) Nature. , vol.319 , pp. 199-203
    • Eisenberg, D.1    McLachlan, A.D.2
  • 20
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling
    • Guex, N.; Peitsch, M. C. SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling. Electrophoresis. 1997, 18, 2714-2723.
    • (1997) Electrophoresis. , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 21
    • 0026589733 scopus 로고
    • The dead-end elimination theorem and its use in protein side-chain positioning
    • Desmet, J.; Hazes, B.; Lasters, I. The dead-end elimination theorem and its use in protein side-chain positioning. Nature. 1992, 356, 539-542.
    • (1992) Nature. , vol.356 , pp. 539-542
    • Desmet, J.1    Hazes, B.2    Lasters, I.3
  • 22
    • 0028826985 scopus 로고
    • Enhanced dead-end elimination in the search for the global minimum energy conformation of a collection of protein side chains
    • Lasters, I.; Maeyer, M. D.; Desmet, J. Enhanced dead-end elimination in the search for the global minimum energy conformation of a collection of protein side chains. Prot. Engin. 1995, 8, 815-822.
    • (1995) Prot. Engin. , vol.8 , pp. 815-822
    • Lasters, I.1    Maeyer, M.D.2    Desmet, J.3
  • 23
    • 70349084150 scopus 로고    scopus 로고
    • Selective Covalent Protein Immobilization: Strategies and Applications
    • Wong, L. S.; Khan, F.; Micklefield, J. Selective Covalent Protein Immobilization: Strategies and Applications. Chem. Rev. 2009, 109, 4025-4053.
    • (2009) Chem. Rev. , vol.109 , pp. 4025-4053
    • Wong, L.S.1    Khan, F.2    Micklefield, J.3
  • 25
    • 0026709329 scopus 로고
    • Alpha-Helix stability in proteins: I. Empirical correlations concerning substitution of side-chains at the N and C-caps and the replacement of alanine by glycine or serine at solvent-exposed surfaces
    • Serrano, L.; Sancho, J.; Hirshberg, M.; Fersht, A. R. Alpha-Helix stability in proteins: I. Empirical correlations concerning substitution of side-chains at the N and C-caps and the replacement of alanine by glycine or serine at solvent-exposed surfaces. J. Mol. Biol. 1992, 227, 544-559.
    • (1992) J. Mol. Biol. , vol.227 , pp. 544-559
    • Serrano, L.1    Sancho, J.2    Hirshberg, M.3    Fersht, A.R.4
  • 26
    • 84857435187 scopus 로고    scopus 로고
    • Improved Protein-A separation of V(H)3 Fab from Fc after Papain Digestion of Antibodies
    • Seldon, T. A.; Hughes, K. E.; Munster, D. J.; Chin, D. Y.; Jones, M. L. Improved Protein-A separation of V(H)3 Fab from Fc after Papain Digestion of Antibodies. J. Biomol. Tech. 2011, 22, 50-52.
    • (2011) J. Biomol. Tech. , vol.22 , pp. 50-52
    • Seldon, T.A.1    Hughes, K.E.2    Munster, D.J.3    Chin, D.Y.4    Jones, M.L.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.