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Volumn 342, Issue 3, 2004, Pages 901-912

Development of a human light chain variable domain (VL) intracellular antibody specific for the amino terminus of huntingtin via yeast surface display

Author keywords

Huntington's disease; intracellular antibody; paratope mapping; single domain antibody; yeast surface display

Indexed keywords

HUNTINGTIN; PROTEIN ANTIBODY;

EID: 4444239017     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2004.07.054     Document Type: Article
Times cited : (85)

References (50)
  • 1
    • 0141483468 scopus 로고    scopus 로고
    • Intrabody-based strategies for inhibition of vascular endothelial growth factor receptor-2: Effects on apoptosis, cell growth, and angiogenesis
    • Y.Y. Wheeler, T.E. Kute, M.C. Willingham, S.Y. Chen, and D.C. Sane Intrabody-based strategies for inhibition of vascular endothelial growth factor receptor-2: effects on apoptosis, cell growth, and angiogenesis FASEB J. 17 2003 1733 1735
    • (2003) FASEB J. , vol.17 , pp. 1733-1735
    • Wheeler, Y.Y.1    Kute, T.E.2    Willingham, M.C.3    Chen, S.Y.4    Sane, D.C.5
  • 2
    • 0037154165 scopus 로고    scopus 로고
    • Effects of intracellular expression of anti-huntingtin antibodies of various specificities on mutant huntingtin aggregation and toxicity
    • A. Khoshnan, J. Ko, and P.H. Patterson Effects of intracellular expression of anti-huntingtin antibodies of various specificities on mutant huntingtin aggregation and toxicity Proc. Natl Acad. Sci. USA 99 2002 1002 1007
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 1002-1007
    • Khoshnan, A.1    Ko, J.2    Patterson, P.H.3
  • 3
    • 18544408628 scopus 로고    scopus 로고
    • A cancer gene therapy approach utilizing an anti-erbB-2 single-chain antibody-encoding adenovirus (AD21): A phase I trial
    • R.D. Alvarez, M.N. Barnes, J. Gomez-Navarro, M. Wang, T.V. Strong, and W. Arafat A cancer gene therapy approach utilizing an anti-erbB-2 single-chain antibody-encoding adenovirus (AD21): a phase I trial Clin. Cancer Res. 6 2000 3081 3087
    • (2000) Clin. Cancer Res. , vol.6 , pp. 3081-3087
    • Alvarez, R.D.1    Barnes, M.N.2    Gomez-Navarro, J.3    Wang, M.4    Strong, T.V.5    Arafat, W.6
  • 4
    • 0035836675 scopus 로고    scopus 로고
    • Human single-chain Fv intrabodies counteract in situ huntingtin aggregation in cellular models of Huntington's disease
    • J.M. Lecerf, T.L. Shirley, Q. Zhu, A. Kazantsev, P. Amersdorfer, and D.E. Housman Human single-chain Fv intrabodies counteract in situ huntingtin aggregation in cellular models of Huntington's disease Proc. Natl Acad. Sci. USA 98 2001 4764 4769
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 4764-4769
    • Lecerf, J.M.1    Shirley, T.L.2    Zhu, Q.3    Kazantsev, A.4    Amersdorfer, P.5    Housman, D.E.6
  • 5
    • 0345549465 scopus 로고    scopus 로고
    • Direct phage to intrabody screening (DPIS): Demonstration by isolation of cytosolic intrabodies against the TES1 site of Epstein Barr virus latent membrane protein 1 (LMP1) that block NF-kappaB transactivation
    • F. Gennari, S. Mehta, Y. Wang, A. St Clair Tallarico, G. Palu, and W.A. Marasco Direct phage to intrabody screening (DPIS): demonstration by isolation of cytosolic intrabodies against the TES1 site of Epstein Barr virus latent membrane protein 1 (LMP1) that block NF-kappaB transactivation J. Mol. Biol. 335 2004 193 207
    • (2004) J. Mol. Biol. , vol.335 , pp. 193-207
    • Gennari, F.1    Mehta, S.2    Wang, Y.3    St Clair Tallarico, A.4    Palu, G.5    Marasco, W.A.6
  • 6
    • 1542357652 scopus 로고    scopus 로고
    • Inhibiting aggregation of alpha-synuclein with human single chain antibody fragments
    • S. Emadi, R. Liu, B. Yuan, P. Schulz, C. McAllister, and Y. Lyubchenko Inhibiting aggregation of alpha-synuclein with human single chain antibody fragments Biochemistry 43 2004 2871 2878
    • (2004) Biochemistry , vol.43 , pp. 2871-2878
    • Emadi, S.1    Liu, R.2    Yuan, B.3    Schulz, P.4    McAllister, C.5    Lyubchenko, Y.6
  • 7
    • 0036299007 scopus 로고    scopus 로고
    • Intracellular antibody capture technology: Application to selection of intracellular antibodies recognising the BCR-ABL oncogenic protein
    • E. Tse, M.N. Lobato, A. Forster, T. Tanaka, G.T. Chung, and T.H. Rabbitts Intracellular antibody capture technology: application to selection of intracellular antibodies recognising the BCR-ABL oncogenic protein J. Mol. Biol. 317 2002 85 94
    • (2002) J. Mol. Biol. , vol.317 , pp. 85-94
    • Tse, E.1    Lobato, M.N.2    Forster, A.3    Tanaka, T.4    Chung, G.T.5    Rabbitts, T.H.6
  • 8
    • 0037416179 scopus 로고    scopus 로고
    • Intrabodies based on intracellular capture frameworks that bind the RAS protein with high affinity and impair oncogenic transformation
    • T. Tanaka, and T.H. Rabbitts Intrabodies based on intracellular capture frameworks that bind the RAS protein with high affinity and impair oncogenic transformation EMBO J. 22 2003 1025 1035
    • (2003) EMBO J. , vol.22 , pp. 1025-1035
    • Tanaka, T.1    Rabbitts, T.H.2
  • 9
    • 0030994634 scopus 로고    scopus 로고
    • Yeast surface display for screening combinatorial polypeptide libraries
    • E.T. Boder, and K.D. Wittrup Yeast surface display for screening combinatorial polypeptide libraries Nature Biotechnol. 15 1997 553 557
    • (1997) Nature Biotechnol. , vol.15 , pp. 553-557
    • Boder, E.T.1    Wittrup, K.D.2
  • 10
    • 0037318058 scopus 로고    scopus 로고
    • Flow-cytometric isolation of human antibodies from a nonimmune Saccharomyces cerevisiae surface display library
    • M.J. Feldhaus, R.W. Siegel, L.K. Opresko, J.R. Coleman, J.M. Feldhaus, and Y.A. Yeung Flow-cytometric isolation of human antibodies from a nonimmune Saccharomyces cerevisiae surface display library Nature Biotechnol. 21 2003 163 170
    • (2003) Nature Biotechnol. , vol.21 , pp. 163-170
    • Feldhaus, M.J.1    Siegel, R.W.2    Opresko, L.K.3    Coleman, J.R.4    Feldhaus, J.M.5    Yeung, Y.A.6
  • 11
    • 0034718615 scopus 로고    scopus 로고
    • Directed evolution of antibody fragments with monovalent femtomolar antigen-binding affinity
    • E.T. Boder, K.S. Midelfort, and K.D. Wittrup Directed evolution of antibody fragments with monovalent femtomolar antigen-binding affinity Proc. Natl Acad. Sci. USA 97 2000 10701 10705
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 10701-10705
    • Boder, E.T.1    Midelfort, K.S.2    Wittrup, K.D.3
  • 13
    • 0345044918 scopus 로고    scopus 로고
    • Domain interactions in antibody Fv and scFv fragments: Effects on unfolding kinetics and equilibria
    • M. Jager, and A. Pluckthun Domain interactions in antibody Fv and scFv fragments: effects on unfolding kinetics and equilibria FEBS Letters 462 1999 307 312
    • (1999) FEBS Letters , vol.462 , pp. 307-312
    • Jager, M.1    Pluckthun, A.2
  • 14
    • 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
  • 17
    • 0043123378 scopus 로고    scopus 로고
    • Single domain intracellular antibodies: A minimal fragment for direct in vivo selection of antigen-specific intrabodies
    • T. Tanaka, M.N. Lobato, and T.H. Rabbitts Single domain intracellular antibodies: a minimal fragment for direct in vivo selection of antigen-specific intrabodies J. Mol. Biol. 331 2003 1109 1120
    • (2003) J. Mol. Biol. , vol.331 , pp. 1109-1120
    • Tanaka, T.1    Lobato, M.N.2    Rabbitts, T.H.3
  • 18
    • 1042264041 scopus 로고    scopus 로고
    • Gene replacement therapy for non-small cell lung cancer: A review
    • J.A. Roth, and S.F. Grammer Gene replacement therapy for non-small cell lung cancer: a review Hematol. Oncol. Clin. North Am. 18 2004 215 229
    • (2004) Hematol. Oncol. Clin. North Am. , vol.18 , pp. 215-229
    • Roth, J.A.1    Grammer, S.F.2
  • 19
    • 18544400323 scopus 로고    scopus 로고
    • Huntingtin-encoded polyglutamine expansions form amyloid-like protein aggregates in vitro and in vivo
    • E. Scherzinger, R. Lurz, M. Turmaine, L. Mangiarini, B. Hollenbach, and R. Hasenbank Huntingtin-encoded polyglutamine expansions form amyloid-like protein aggregates in vitro and in vivo Cell 90 1997 549 558
    • (1997) Cell , vol.90 , pp. 549-558
    • Scherzinger, E.1    Lurz, R.2    Turmaine, M.3    Mangiarini, L.4    Hollenbach, B.5    Hasenbank, R.6
  • 20
    • 0030752709 scopus 로고    scopus 로고
    • Aggregation of huntingtin in neuronal intranuclear inclusions and dystrophic neurites in brain
    • M. DiFiglia, E. Sapp, K.O. Chase, S.W. Davies, G.P. Bates, J.P. Vonsattel, and N. Aronin Aggregation of huntingtin in neuronal intranuclear inclusions and dystrophic neurites in brain Science 277 1997 1990 1993
    • (1997) Science , vol.277 , pp. 1990-1993
    • Difiglia, M.1    Sapp, E.2    Chase, K.O.3    Davies, S.W.4    Bates, G.P.5    Vonsattel, J.P.6    Aronin, N.7
  • 21
    • 0027480960 scopus 로고
    • A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes
    • The Huntington's Disease Collaborative Research Group
    • The Huntington's Disease Collaborative Research Group A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes Cell 72 1993 971 983
    • (1993) Cell , vol.72 , pp. 971-983
  • 22
    • 0037015081 scopus 로고    scopus 로고
    • Huntington's disease age-of-onset linked to polyglutamine aggregation nucleation
    • S. Chen, F.A. Ferrone, and R. Wetzel Huntington's disease age-of-onset linked to polyglutamine aggregation nucleation Proc. Natl Acad. Sci. USA 99 2002 11884 11889
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 11884-11889
    • Chen, S.1    Ferrone, F.A.2    Wetzel, R.3
  • 23
    • 0035947372 scopus 로고    scopus 로고
    • Impairment of the ubiquitin-proteasome system by protein aggregation
    • N.F. Bence, R.M. Sampat, and R.R. Kopito Impairment of the ubiquitin-proteasome system by protein aggregation Science 292 2001 1552 1555
    • (2001) Science , vol.292 , pp. 1552-1555
    • Bence, N.F.1    Sampat, R.M.2    Kopito, R.R.3
  • 25
    • 0034612220 scopus 로고    scopus 로고
    • Inhibition of huntingtin fibrillogenesis by specific antibodies and small molecules: Implications for Huntington's disease therapy
    • V. Heiser, E. Scherzinger, A. Boeddrich, E. Nordhoff, R. Lurz, and N. Schugardt Inhibition of huntingtin fibrillogenesis by specific antibodies and small molecules: implications for Huntington's disease therapy Proc. Natl Acad. Sci. USA 97 2000 6739 6744
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 6739-6744
    • Heiser, V.1    Scherzinger, E.2    Boeddrich, A.3    Nordhoff, E.4    Lurz, R.5    Schugardt, N.6
  • 26
    • 1242351323 scopus 로고    scopus 로고
    • A single-chain Fv intrabody provides functional protection against the effects of mutant protein in an organotypic slice culture model of Huntington's disease
    • R.C. Murphy, and A. Messer A single-chain Fv intrabody provides functional protection against the effects of mutant protein in an organotypic slice culture model of Huntington's disease Brain Res. Mol. Brain Res. 121 2004 141 145
    • (2004) Brain Res. Mol. Brain Res. , vol.121 , pp. 141-145
    • Murphy, R.C.1    Messer, A.2
  • 27
    • 0033779619 scopus 로고    scopus 로고
    • Antineoplastic effect of anti-erbB-2 intrabody is not correlated with scFv affinity for its target
    • W. Arafat, J. Gomez-Navarro, J. Xiang, G.P. Siegal, R.D. Alvarez, and D.T. Curiel Antineoplastic effect of anti-erbB-2 intrabody is not correlated with scFv affinity for its target Cancer Gene Ther. 7 2000 1250 1256
    • (2000) Cancer Gene Ther. , vol.7 , pp. 1250-1256
    • Arafat, W.1    Gomez-Navarro, J.2    Xiang, J.3    Siegal, G.P.4    Alvarez, R.D.5    Curiel, D.T.6
  • 28
    • 0035980086 scopus 로고    scopus 로고
    • Intracellular stability of anti-caspase-3 intrabodies determines efficacy in retargeting the antigen
    • A. Rajpal, and T.G. Turi Intracellular stability of anti-caspase-3 intrabodies determines efficacy in retargeting the antigen J. Biol. Chem. 276 2001 33139 33146
    • (2001) J. Biol. Chem. , vol.276 , pp. 33139-33146
    • Rajpal, A.1    Turi, T.G.2
  • 29
    • 0033499632 scopus 로고    scopus 로고
    • Extended half-life and elevated steady-state level of a single-chain Fv intrabody are critical for specific intracellular retargeting of its antigen, caspase-7
    • Q. Zhu, C. Zeng, A. Huhalov, J. Yao, T.G. Turi, and D. Danley Extended half-life and elevated steady-state level of a single-chain Fv intrabody are critical for specific intracellular retargeting of its antigen, caspase-7 J. Immunol. Methods 231 1999 207 222
    • (1999) J. Immunol. Methods , vol.231 , pp. 207-222
    • Zhu, Q.1    Zeng, C.2    Huhalov, A.3    Yao, J.4    Turi, T.G.5    Danley, D.6
  • 30
    • 0033748716 scopus 로고    scopus 로고
    • Yeast surface display for directed evolution of protein expression, affinity, and stability
    • E.T. Boder, and K.D. Wittrup Yeast surface display for directed evolution of protein expression, affinity, and stability Methods Enzymol. 328 2000 430 444
    • (2000) Methods Enzymol. , vol.328 , pp. 430-444
    • Boder, E.T.1    Wittrup, K.D.2
  • 32
    • 2342510292 scopus 로고    scopus 로고
    • Shuffled antibody libraries created by in vivo homologous recombination and yeast surface display
    • J.S. Swers, B.A. Kellogg, and K.D. Wittrup Shuffled antibody libraries created by in vivo homologous recombination and yeast surface display Nucl. Acids Res. 32 2004 e36
    • (2004) Nucl. Acids Res. , vol.32
    • Swers, J.S.1    Kellogg, B.A.2    Wittrup, K.D.3
  • 33
    • 0037359054 scopus 로고    scopus 로고
    • Rapid method for measuring ScFv thermal stability by yeast surface display
    • B.A. Orr, L.M. Carr, K.D. Wittrup, E.J. Roy, and D.M. Kranz Rapid method for measuring ScFv thermal stability by yeast surface display Biotechnol. Prog. 19 2003 631 638
    • (2003) Biotechnol. Prog. , vol.19 , pp. 631-638
    • Orr, B.A.1    Carr, L.M.2    Wittrup, K.D.3    Roy, E.J.4    Kranz, D.M.5
  • 34
    • 0033536626 scopus 로고    scopus 로고
    • Yeast polypeptide fusion surface display levels predict thermal stability and soluble secretion efficiency
    • E.V. Shusta, M.C. Kieke, E. Parke, D.M. Kranz, and K.D. Wittrup Yeast polypeptide fusion surface display levels predict thermal stability and soluble secretion efficiency J. Mol. Biol. 292 1999 949 956
    • (1999) J. Mol. Biol. , vol.292 , pp. 949-956
    • Shusta, E.V.1    Kieke, M.C.2    Parke, E.3    Kranz, D.M.4    Wittrup, K.D.5
  • 36
    • 0033976101 scopus 로고    scopus 로고
    • Fine affinity discrimination by yeast surface display and flow cytometry
    • J.J. VanAntwerp, and K.D. Wittrup Fine affinity discrimination by yeast surface display and flow cytometry Biotechnol. Prog. 16 2000 31 37
    • (2000) Biotechnol. Prog. , vol.16 , pp. 31-37
    • Vanantwerp, J.J.1    Wittrup, K.D.2
  • 38
    • 1942520362 scopus 로고    scopus 로고
    • Domain-level antibody epitope mapping through yeast surface display of epidermal growth factor receptor fragments
    • J.R. Cochran, Y.S. Kim, M.J. Olsen, R. Bhandari, and K.D. Wittrup Domain-level antibody epitope mapping through yeast surface display of epidermal growth factor receptor fragments J. Immunol. Methods 287 2004 147 158
    • (2004) J. Immunol. Methods , vol.287 , pp. 147-158
    • Cochran, J.R.1    Kim, Y.S.2    Olsen, M.J.3    Bhandari, R.4    Wittrup, K.D.5
  • 39
    • 3142657314 scopus 로고    scopus 로고
    • Identification of the epitope for the EGFR-specific monoclonal antibody 806 reveals that it preferentially recognizes an untethered form of the receptor
    • T.G. Johns, T.E. Adams, J.R. Cochran, N.E. Hall, P.A. Hoyne, and M.J. Olsen Identification of the epitope for the EGFR-specific monoclonal antibody 806 reveals that it preferentially recognizes an untethered form of the receptor J. Biol. Chem. 279 2004 30375 30384
    • (2004) J. Biol. Chem. , vol.279 , pp. 30375-30384
    • Johns, T.G.1    Adams, T.E.2    Cochran, J.R.3    Hall, N.E.4    Hoyne, P.A.5    Olsen, M.J.6
  • 40
    • 0036295439 scopus 로고    scopus 로고
    • Comprehensive functional maps of the antigen-binding site of an anti-ErbB2 antibody obtained with shotgun scanning mutagenesis
    • F.F. Vajdos, C.W. Adams, T.N. Breece, L.G. Presta, A.M. de Vos, and S.S. Sidhu Comprehensive functional maps of the antigen-binding site of an anti-ErbB2 antibody obtained with shotgun scanning mutagenesis J. Mol. Biol. 320 2002 415 428
    • (2002) J. Mol. Biol. , vol.320 , pp. 415-428
    • Vajdos, F.F.1    Adams, C.W.2    Breece, T.N.3    Presta, L.G.4    De Vos, A.M.5    Sidhu, S.S.6
  • 41
    • 0035066602 scopus 로고    scopus 로고
    • ASEdb: A database of alanine mutations and their effects on the free energy of binding in protein interactions
    • K.S. Thorn, and A.A. Bogan ASEdb: a database of alanine mutations and their effects on the free energy of binding in protein interactions Bioinformatics 17 2001 284 285
    • (2001) Bioinformatics , vol.17 , pp. 284-285
    • Thorn, K.S.1    Bogan, A.A.2
  • 42
    • 0030580057 scopus 로고    scopus 로고
    • Antibody-antigen interactions: Contact analysis and binding site topography
    • R.M. MacCallum, A.C. Martin, and J.M. Thornton Antibody-antigen interactions: contact analysis and binding site topography J. Mol. Biol. 262 1996 732 745
    • (1996) J. Mol. Biol. , vol.262 , pp. 732-745
    • MacCallum, R.M.1    Martin, A.C.2    Thornton, J.M.3
  • 44
    • 0028606741 scopus 로고
    • Antibody-antigen interactions: New structures and new conformational changes
    • I.A. Wilson, and R.L. Stanfield Antibody-antigen interactions: new structures and new conformational changes Curr. Opin. Struct. Biol. 4 1994 857 867
    • (1994) Curr. Opin. Struct. Biol. , vol.4 , pp. 857-867
    • Wilson, I.A.1    Stanfield, R.L.2
  • 45
    • 0027325038 scopus 로고
    • Crystal structure of a human immunodeficiency virus type 1 neutralizing antibody, 50.1, in complex with its V3 loop peptide antigen
    • J.M. Rini, R.L. Stanfield, E.A. Stura, P.A. Salinas, A.T. Profy, and I.A. Wilson Crystal structure of a human immunodeficiency virus type 1 neutralizing antibody, 50.1, in complex with its V3 loop peptide antigen Proc. Natl Acad. Sci. USA 90 1993 6325 6329
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 6325-6329
    • Rini, J.M.1    Stanfield, R.L.2    Stura, E.A.3    Salinas, P.A.4    Profy, A.T.5    Wilson, I.A.6
  • 46
    • 0033538557 scopus 로고    scopus 로고
    • Removal of the conserved disulfide bridges from the scFv fragment of an antibody: Effects on folding kinetics and aggregation
    • K. Ramm, P. Gehrig, and A. Pluckthun Removal of the conserved disulfide bridges from the scFv fragment of an antibody: effects on folding kinetics and aggregation J. Mol. Biol. 290 1999 535 546
    • (1999) J. Mol. Biol. , vol.290 , pp. 535-546
    • Ramm, K.1    Gehrig, P.2    Pluckthun, A.3
  • 47
    • 0029185449 scopus 로고
    • Structure and properties of human immunoglobulin light-chain dimers
    • F.J. Stevens, and M. Schiffer Structure and properties of human immunoglobulin light-chain dimers Methods Mol. Biol. 51 1995 51 81
    • (1995) Methods Mol. Biol. , vol.51 , pp. 51-81
    • Stevens, F.J.1    Schiffer, M.2
  • 49
    • 0002009016 scopus 로고
    • Protein migration and accumulation in nuclei
    • (Busch, H., ed.), Academic Press, New York, NY.
    • Bonner, W. M. (1978). Protein migration and accumulation in nuclei. In The Cell Nucleus (Busch, H., ed.), vol. 6, part C, pp. 97-148, Academic Press, New York, NY.
    • (1978) The Cell Nucleus , vol.6 , Issue.PART C , pp. 97-148
    • Bonner, W.M.1
  • 50
    • 0032893534 scopus 로고    scopus 로고
    • General method for plasmid construction using homologous recombination
    • C.K. Raymond, T.A. Pownder, and S.L. Sexson General method for plasmid construction using homologous recombination Biotechniques 26 1999 134 138 140-141
    • (1999) Biotechniques , vol.26 , pp. 134-138
    • Raymond, C.K.1    Pownder, T.A.2    Sexson, S.L.3


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