메뉴 건너뛰기




Volumn 7, Issue 7, 2012, Pages

High-affinity target binding engineered via fusion of a single-domain antibody fragment with a ligand-tailored SH3 domain

Author keywords

[No Author keywords available]

Indexed keywords

BINDING PROTEIN; HYBRID PROTEIN; NEF PROTEIN; NEFFIN PROTEIN; UNCLASSIFIED DRUG;

EID: 84863617815     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0040331     Document Type: Article
Times cited : (20)

References (48)
  • 1
    • 0016756272 scopus 로고
    • Continuous cultures of fused cells secreting antibody of predefined specificity
    • Kohler G, Milstein C, (1975) Continuous cultures of fused cells secreting antibody of predefined specificity. Nature 256: 495-497.
    • (1975) Nature , vol.256 , pp. 495-497
    • Kohler, G.1    Milstein, C.2
  • 2
    • 77957361348 scopus 로고    scopus 로고
    • Development trends for human monoclonal antibody therapeutics
    • Nelson AL, Dhimolea E, Reichert JM, (2010) Development trends for human monoclonal antibody therapeutics. Nat Rev Drug Discov 9: 767-774.
    • (2010) Nat Rev Drug Discov , vol.9 , pp. 767-774
    • Nelson, A.L.1    Dhimolea, E.2    Reichert, J.M.3
  • 3
    • 67649851892 scopus 로고    scopus 로고
    • mAbs: a business perspective
    • Scolnik PA, (2009) mAbs: a business perspective. MAbs 1: 179-184.
    • (2009) MAbs , vol.1 , pp. 179-184
    • Scolnik, P.A.1
  • 4
    • 27144432842 scopus 로고    scopus 로고
    • Engineered antibody fragments and the rise of single domains
    • Holliger P, Hudson PJ, (2005) Engineered antibody fragments and the rise of single domains. Nat Biotechnol 23: 1126-1136.
    • (2005) Nat Biotechnol , vol.23 , pp. 1126-1136
    • Holliger, P.1    Hudson, P.J.2
  • 5
    • 0030738617 scopus 로고    scopus 로고
    • New protein engineering approaches to multivalent and bispecific antibody fragments
    • Pluckthun A, Pack P, (1997) New protein engineering approaches to multivalent and bispecific antibody fragments. Immunotechnology 3: 83-105.
    • (1997) Immunotechnology , vol.3 , pp. 83-105
    • Pluckthun, A.1    Pack, P.2
  • 6
    • 0029653368 scopus 로고
    • Kinetic and affinity limits on antibodies produced during immune responses
    • Foote J, Eisen HN, (1995) Kinetic and affinity limits on antibodies produced during immune responses. Proc Natl Acad Sci U S A 92: 1254-1256.
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 1254-1256
    • Foote, J.1    Eisen, H.N.2
  • 7
    • 0034718592 scopus 로고    scopus 로고
    • Breaking the affinity ceiling for antibodies and T cell receptors
    • Foote J, Eisen HN, (2000) Breaking the affinity ceiling for antibodies and T cell receptors. Proc Natl Acad Sci U S A 97: 10679-10681.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 10679-10681
    • Foote, J.1    Eisen, H.N.2
  • 8
    • 0034718615 scopus 로고    scopus 로고
    • Directed evolution of antibody fragments with monovalent femtomolar antigen-binding affinity
    • Boder ET, Midelfort KS, Wittrup KD, (2000) Directed evolution of antibody fragments with monovalent femtomolar antigen-binding affinity. Proc Natl Acad Sci U S A 97: 10701-10705.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 10701-10705
    • Boder, E.T.1    Midelfort, K.S.2    Wittrup, K.D.3
  • 9
    • 50249132634 scopus 로고    scopus 로고
    • Antibody therapeutics, antibody engineering, and the merits of protein stability
    • Demarest SJ, Glaser SM, (2008) Antibody therapeutics, antibody engineering, and the merits of protein stability. Curr Opin Drug Discov Devel 11: 675-687.
    • (2008) Curr Opin Drug Discov Devel , vol.11 , pp. 675-687
    • Demarest, S.J.1    Glaser, S.M.2
  • 10
    • 0037227517 scopus 로고    scopus 로고
    • Biophysical properties of human antibody variable domains
    • Ewert S, Huber T, Honegger A, Pluckthun A, (2003) Biophysical properties of human antibody variable domains. J Mol Biol 325: 531-553.
    • (2003) J Mol Biol , vol.325 , pp. 531-553
    • Ewert, S.1    Huber, T.2    Honegger, A.3    Pluckthun, A.4
  • 11
    • 38449112154 scopus 로고    scopus 로고
    • Engineering antibodies for stability and efficient folding
    • Honegger A, (2008) Engineering antibodies for stability and efficient folding. Handb Exp Pharmacol pp. 47-68.
    • (2008) Handb Exp Pharmacol , pp. 47-68
    • Honegger, A.1
  • 12
    • 0033214755 scopus 로고    scopus 로고
    • In vitro folding and thermodynamic stability of an antibody fragment selected in vivo for high expression levels in Escherichia coli cytoplasm
    • Martineau P, Betton JM, (1999) In vitro folding and thermodynamic stability of an antibody fragment selected in vivo for high expression levels in Escherichia coli cytoplasm. J Mol Biol 292: 921-929.
    • (1999) J Mol Biol , vol.292 , pp. 921-929
    • Martineau, P.1    Betton, J.M.2
  • 13
    • 27144511241 scopus 로고    scopus 로고
    • Engineering novel binding proteins from nonimmunoglobulin domains
    • Binz HK, Amstutz P, Pluckthun A, (2005) Engineering novel binding proteins from nonimmunoglobulin domains. Nat Biotechnol 23: 1257-1268.
    • (2005) Nat Biotechnol , vol.23 , pp. 1257-1268
    • Binz, H.K.1    Amstutz, P.2    Pluckthun, A.3
  • 14
    • 67649872364 scopus 로고    scopus 로고
    • Engineered protein scaffolds as next-generation antibody therapeutics
    • Gebauer M, Skerra A, (2009) Engineered protein scaffolds as next-generation antibody therapeutics. Curr Opin Chem Biol 13: 245-255.
    • (2009) Curr Opin Chem Biol , vol.13 , pp. 245-255
    • Gebauer, M.1    Skerra, A.2
  • 15
    • 24944450680 scopus 로고    scopus 로고
    • Artificial, non-antibody binding proteins for pharmaceutical and industrial applications
    • Hey T, Fiedler E, Rudolph R, Fiedler M, (2005) Artificial, non-antibody binding proteins for pharmaceutical and industrial applications. Trends Biotechnol 23: 514-522.
    • (2005) Trends Biotechnol , vol.23 , pp. 514-522
    • Hey, T.1    Fiedler, E.2    Rudolph, R.3    Fiedler, M.4
  • 16
    • 43549101411 scopus 로고    scopus 로고
    • Alternative binding proteins: affibody binding proteins developed from a small three-helix bundle scaffold
    • Nygren PA, (2008) Alternative binding proteins: affibody binding proteins developed from a small three-helix bundle scaffold. FEBS J 275: 2668-2676.
    • (2008) FEBS J , vol.275 , pp. 2668-2676
    • Nygren, P.A.1
  • 17
    • 34547457742 scopus 로고    scopus 로고
    • Monobodies: antibody mimics based on the scaffold of the fibronectin type III domain
    • Koide A, Koide S, (2007) Monobodies: antibody mimics based on the scaffold of the fibronectin type III domain. Methods Mol Biol 352: 95-109.
    • (2007) Methods Mol Biol , vol.352 , pp. 95-109
    • Koide, A.1    Koide, S.2
  • 18
    • 48149098354 scopus 로고    scopus 로고
    • DARPins: a new generation of protein therapeutics
    • Stumpp MT, Binz HK, Amstutz P, (2008) DARPins: a new generation of protein therapeutics. Drug Discov Today 13: 695-701.
    • (2008) Drug Discov Today , vol.13 , pp. 695-701
    • Stumpp, M.T.1    Binz, H.K.2    Amstutz, P.3
  • 19
    • 0035749903 scopus 로고    scopus 로고
    • Implications of SH3 domain structure and dynamics for protein regulation and drug design
    • Gmeiner WH, Horita DA, (2001) Implications of SH3 domain structure and dynamics for protein regulation and drug design. Cell Biochem Biophys 35: 127-140.
    • (2001) Cell Biochem Biophys , vol.35 , pp. 127-140
    • Gmeiner, W.H.1    Horita, D.A.2
  • 20
    • 42649119825 scopus 로고    scopus 로고
    • The SH3 domain-a family of versatile peptide- and protein-recognition module
    • Kaneko T, Li L, Li SS, (2008) The SH3 domain-a family of versatile peptide- and protein-recognition module. Front Biosci 13: 4938-4952.
    • (2008) Front Biosci , vol.13 , pp. 4938-4952
    • Kaneko, T.1    Li, L.2    Li, S.S.3
  • 21
    • 34047244187 scopus 로고    scopus 로고
    • A novel, non-immunogenic Fyn SH3-derived binding protein with tumor vascular targeting properties
    • Grabulovski D, Kaspar M, Neri D, (2007) A novel, non-immunogenic Fyn SH3-derived binding protein with tumor vascular targeting properties. J Biol Chem 282: 3196-3204.
    • (2007) J Biol Chem , vol.282 , pp. 3196-3204
    • Grabulovski, D.1    Kaspar, M.2    Neri, D.3
  • 22
    • 0033550310 scopus 로고    scopus 로고
    • SH3 domains with high affinity and engineered ligand specificities targeted to HIV-1 Nef
    • Hiipakka M, Poikonen K, Saksela K, (1999) SH3 domains with high affinity and engineered ligand specificities targeted to HIV-1 Nef. J Mol Biol 293: 1097-1106.
    • (1999) J Mol Biol , vol.293 , pp. 1097-1106
    • Hiipakka, M.1    Poikonen, K.2    Saksela, K.3
  • 23
    • 34247166258 scopus 로고    scopus 로고
    • Versatile retargeting of SH3 domain binding by modification of non-conserved loop residues
    • Hiipakka M, Saksela K, (2007) Versatile retargeting of SH3 domain binding by modification of non-conserved loop residues. FEBS Lett 581: 1735-1741.
    • (2007) FEBS Lett , vol.581 , pp. 1735-1741
    • Hiipakka, M.1    Saksela, K.2
  • 24
    • 0024461313 scopus 로고
    • Binding activities of a repertoire of single immunoglobulin variable domains secreted from Escherichia coli
    • Ward ES, Gussow D, Griffiths AD, Jones PT, Winter G, (1989) Binding activities of a repertoire of single immunoglobulin variable domains secreted from Escherichia coli. Nature 341: 544-546.
    • (1989) Nature , vol.341 , pp. 544-546
    • Ward, E.S.1    Gussow, D.2    Griffiths, A.D.3    Jones, P.T.4    Winter, G.5
  • 25
    • 0035715877 scopus 로고    scopus 로고
    • Single domain camel antibodies: current status
    • Muyldermans S, (2001) Single domain camel antibodies: current status. J Biotechnol 74: 277-302.
    • (2001) J Biotechnol , vol.74 , pp. 277-302
    • Muyldermans, S.1
  • 27
    • 0344395582 scopus 로고    scopus 로고
    • Beneficial properties of single-domain antibody fragments for application in immunoaffinity purification and immuno-perfusion chromatography
    • Verheesen P, ten Haaft MR, Lindner N, Verrips CT, de Haard JJ, (2003) Beneficial properties of single-domain antibody fragments for application in immunoaffinity purification and immuno-perfusion chromatography. Biochim Biophys Acta 1624: 21-28.
    • (2003) Biochim Biophys Acta , vol.1624 , pp. 21-28
    • Verheesen, P.1    ten Haaft, M.R.2    Lindner, N.3    Verrips, C.T.4    de Haard, J.J.5
  • 28
    • 68349117269 scopus 로고    scopus 로고
    • Single domain antibodies: promising experimental and therapeutic tools in infection and immunity
    • Wesolowski J, Alzogaray V, Reyelt J, Unger M, Juarez K, et al. (2009) Single domain antibodies: promising experimental and therapeutic tools in infection and immunity. Med Microbiol Immunol 198: 157-174.
    • (2009) Med Microbiol Immunol , vol.198 , pp. 157-174
    • Wesolowski, J.1    Alzogaray, V.2    Reyelt, J.3    Unger, M.4    Juarez, K.5
  • 30
    • 0028945817 scopus 로고
    • High-affinity antigen binding by chelating recombinant antibodies (CRAbs)
    • Neri D, Momo M, Prospero T, Winter G, (1995) High-affinity antigen binding by chelating recombinant antibodies (CRAbs). J Mol Biol 246: 367-373.
    • (1995) J Mol Biol , vol.246 , pp. 367-373
    • Neri, D.1    Momo, M.2    Prospero, T.3    Winter, G.4
  • 31
    • 77952944052 scopus 로고    scopus 로고
    • Designing customized cell signalling circuits
    • Lim WA, (2010) Designing customized cell signalling circuits. Nat Rev Mol Cell Biol 11: 393-403.
    • (2010) Nat Rev Mol Cell Biol , vol.11 , pp. 393-403
    • Lim, W.A.1
  • 32
    • 0037453510 scopus 로고    scopus 로고
    • Assembly of cell regulatory systems through protein interaction domains
    • Pawson T, Nash P, (2003) Assembly of cell regulatory systems through protein interaction domains. Science 300: 445-452.
    • (2003) Science , vol.300 , pp. 445-452
    • Pawson, T.1    Nash, P.2
  • 33
    • 44349104094 scopus 로고    scopus 로고
    • Design of protein function leaps by directed domain interface evolution
    • Huang J, Koide A, Makabe K, Koide S, (2008) Design of protein function leaps by directed domain interface evolution. Proc Natl Acad Sci U S A 105: 6578-6583.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 6578-6583
    • Huang, J.1    Koide, A.2    Makabe, K.3    Koide, S.4
  • 34
    • 28644436100 scopus 로고    scopus 로고
    • Multivalent avimer proteins evolved by exon shuffling of a family of human receptor domains
    • Silverman J, Liu Q, Bakker A, To W, Duguay A, et al. (2005) Multivalent avimer proteins evolved by exon shuffling of a family of human receptor domains. Nat Biotechnol 23: 1556-1561.
    • (2005) Nat Biotechnol , vol.23 , pp. 1556-1561
    • Silverman, J.1    Liu, Q.2    Bakker, A.3    To, W.4    Duguay, A.5
  • 36
    • 0035919704 scopus 로고    scopus 로고
    • Inhibition of cellular functions of HIV-1 Nef by artificial SH3 domains
    • Hiipakka M, Huotari P, Manninen A, Renkema GH, Saksela K, (2001) Inhibition of cellular functions of HIV-1 Nef by artificial SH3 domains. Virology 286: 152-159.
    • (2001) Virology , vol.286 , pp. 152-159
    • Hiipakka, M.1    Huotari, P.2    Manninen, A.3    Renkema, G.H.4    Saksela, K.5
  • 37
    • 79956336664 scopus 로고    scopus 로고
    • Molecular design, functional characterization and structural basis of a protein inhibitor against the HIV-1 pathogenicity factor Nef
    • Breuer S, Schievink SI, Schulte A, Blankenfeldt W, Fackler OT, et al. (2011) Molecular design, functional characterization and structural basis of a protein inhibitor against the HIV-1 pathogenicity factor Nef. PloS one 6: e20033.
    • (2011) PloS One , vol.6
    • Breuer, S.1    Schievink, S.I.2    Schulte, A.3    Blankenfeldt, W.4    Fackler, O.T.5
  • 38
    • 79958770579 scopus 로고    scopus 로고
    • Conformation of the dileucine-based sorting motif in HIV-1 Nef revealed by intermolecular domain assembly
    • Horenkamp FA, Breuer S, Schulte A, Lulf S, Weyand M, et al. (2011) Conformation of the dileucine-based sorting motif in HIV-1 Nef revealed by intermolecular domain assembly. Traffic 12: 867-877.
    • (2011) Traffic , vol.12 , pp. 867-877
    • Horenkamp, F.A.1    Breuer, S.2    Schulte, A.3    Lulf, S.4    Weyand, M.5
  • 39
    • 1842787056 scopus 로고    scopus 로고
    • Characterizing high-affinity antigen/antibody complexes by kinetic- and equilibrium-based methods
    • Drake AW, Myszka DG, Klakamp SL, (2004) Characterizing high-affinity antigen/antibody complexes by kinetic- and equilibrium-based methods. Anal Biochem 328: 35-43.
    • (2004) Anal Biochem , vol.328 , pp. 35-43
    • Drake, A.W.1    Myszka, D.G.2    Klakamp, S.L.3
  • 40
    • 0030039913 scopus 로고    scopus 로고
    • Competition BIAcore for measuring true affinities: large differences from values determined from binding kinetics
    • Nieba L, Krebber A, Pluckthun A, (1996) Competition BIAcore for measuring true affinities: large differences from values determined from binding kinetics. Analytical biochemistry 234: 155-165.
    • (1996) Analytical Biochemistry , vol.234 , pp. 155-165
    • Nieba, L.1    Krebber, A.2    Pluckthun, A.3
  • 41
    • 77953263435 scopus 로고    scopus 로고
    • The role of mass transport limitation and surface heterogeneity in the biophysical characterization of macromolecular binding processes by SPR biosensing
    • Schuck P, Zhao H, (2010) The role of mass transport limitation and surface heterogeneity in the biophysical characterization of macromolecular binding processes by SPR biosensing. Methods Mol Biol 627: 15-54.
    • (2010) Methods Mol Biol , vol.627 , pp. 15-54
    • Schuck, P.1    Zhao, H.2
  • 42
    • 0031017838 scopus 로고    scopus 로고
    • Activation of the Src-family tyrosine kinase Hck by SH3 domain displacement
    • Moarefi I, LaFevre-Bernt M, Sicheri F, Huse M, Lee CH, et al. (1997) Activation of the Src-family tyrosine kinase Hck by SH3 domain displacement. Nature 385: 650-653.
    • (1997) Nature , vol.385 , pp. 650-653
    • Moarefi, I.1    LaFevre-Bernt, M.2    Sicheri, F.3    Huse, M.4    Lee, C.H.5
  • 44
    • 54849403487 scopus 로고    scopus 로고
    • Single-domain antibodies as building blocks for novel therapeutics
    • Saerens D, Ghassabeh GH, Muyldermans S, (2008) Single-domain antibodies as building blocks for novel therapeutics. Curr Opin Pharmacol 8: 600-608.
    • (2008) Curr Opin Pharmacol , vol.8 , pp. 600-608
    • Saerens, D.1    Ghassabeh, G.H.2    Muyldermans, S.3
  • 45
    • 0036933055 scopus 로고    scopus 로고
    • Capacity of simian immunodeficiency virus strain mac Nef for high-affinity Src homology 3 (SH3) binding revealed by ligand-tailored SH3 domains
    • Hiipakka M, Saksela K, (2002) Capacity of simian immunodeficiency virus strain mac Nef for high-affinity Src homology 3 (SH3) binding revealed by ligand-tailored SH3 domains. The Journal of general virology 83: 3147-3152.
    • (2002) The Journal of General Virology , vol.83 , pp. 3147-3152
    • Hiipakka, M.1    Saksela, K.2
  • 46
    • 0032566903 scopus 로고    scopus 로고
    • SH3-Domain binding function of HIV-1 Nef is required for association with a PAK-related kinase
    • Manninen A, Hiipakka M, Vihinen M, Lu W, Mayer BJ, et al. (1998) SH3-Domain binding function of HIV-1 Nef is required for association with a PAK-related kinase. Virology 250: 273-282.
    • (1998) Virology , vol.250 , pp. 273-282
    • Manninen, A.1    Hiipakka, M.2    Vihinen, M.3    Lu, W.4    Mayer, B.J.5
  • 47
    • 33745835407 scopus 로고    scopus 로고
    • The HIV-1 pathogenicity factor Nef interferes with maturation of stimulatory T-lymphocyte contacts by modulation of N-Wasp activity
    • Haller C, Rauch S, Michel N, Hannemann S, Lehmann MJ, et al. (2006) The HIV-1 pathogenicity factor Nef interferes with maturation of stimulatory T-lymphocyte contacts by modulation of N-Wasp activity. J Biol Chem 281: 19618-19630.
    • (2006) J Biol Chem , vol.281 , pp. 19618-19630
    • Haller, C.1    Rauch, S.2    Michel, N.3    Hannemann, S.4    Lehmann, M.J.5
  • 48
    • 0030561202 scopus 로고    scopus 로고
    • Biophysical methods for the determination of antibody-antigen affinities
    • Neri D, Montigiani S, Kirkham PM, (1996) Biophysical methods for the determination of antibody-antigen affinities. Trends Biotechnol 14: 465-470.
    • (1996) Trends Biotechnol , vol.14 , pp. 465-470
    • Neri, D.1    Montigiani, S.2    Kirkham, P.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.