메뉴 건너뛰기




Volumn 341, Issue 4, 2004, Pages 1039-1048

Bivalent Fv antibody fragments obtained by substituting the constant domains of a fab fragment with heterotetrameric molybdopterin synthase

Author keywords

antibody engineering; bivalency; catalytic antibodies; Fv fragments; MPTS

Indexed keywords

FV ANTIBODY; IMMUNOGLOBULIN F(AB) FRAGMENT; MOLYBDOPTERIN; MOLYBDOPTERIN SYNTHASE; PEPTIDE; SYNTHETASE; UNCLASSIFIED DRUG;

EID: 3843109039     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2004.06.075     Document Type: Article
Times cited : (12)

References (32)
  • 2
    • 0032822839 scopus 로고    scopus 로고
    • Recombinant antibody constructs in cancer therapy
    • P.J. Hudson Recombinant antibody constructs in cancer therapy Curr. Opin. Immunol. 11 1999 548 557
    • (1999) Curr. Opin. Immunol. , vol.11 , pp. 548-557
    • Hudson, P.J.1
  • 3
    • 0026270455 scopus 로고
    • The minimal antigen-binding fragment of antibodies - Fv fragment
    • D. Givol The minimal antigen-binding fragment of antibodies - Fv fragment Mol. Immunol. 28 1991 1379 1386
    • (1991) Mol. Immunol. , vol.28 , pp. 1379-1386
    • Givol, D.1
  • 4
    • 0029863393 scopus 로고    scopus 로고
    • Comparative properties of the single chain antibody and Fv derivatives of mAb 4-4-20. Relationship between interdomain interactions and the high affinity for fluorescein ligand
    • W.D. Mallender, J. Carrero, and E.W. Voss Jr Comparative properties of the single chain antibody and Fv derivatives of mAb 4-4-20. Relationship between interdomain interactions and the high affinity for fluorescein ligand J. Biol. Chem. 271 1996 5338 5346
    • (1996) J. Biol. Chem. , vol.271 , pp. 5338-5346
    • Mallender, W.D.1    Carrero, J.2    Voss Jr., E.W.3
  • 6
    • 0028216376 scopus 로고
    • Engineering interchain disulfide bonds into conserved framework regions of Fv fragments: Improved biochemical characteristics of recombinant immunotoxins containing disulfide-stabilized Fv
    • Y. Reiter, U. Brinkmann, K.O. Webber, S.H. Jung, B. Lee, and I. Pastan Engineering interchain disulfide bonds into conserved framework regions of Fv fragments: improved biochemical characteristics of recombinant immunotoxins containing disulfide-stabilized Fv Protein Eng. 7 1994 697 704
    • (1994) Protein Eng. , vol.7 , pp. 697-704
    • Reiter, Y.1    Brinkmann, U.2    Webber, K.O.3    Jung, S.H.4    Lee5    Pastan, I.B.6
  • 7
    • 0029766875 scopus 로고    scopus 로고
    • Engineering antibody Fv fragments for cancer detection and therapy: Disulfide-stabilized Fv fragments
    • Y. Reiter, U. Brinkmann, B. Lee, and I. Pastan Engineering antibody Fv fragments for cancer detection and therapy: disulfide-stabilized Fv fragments Nature Biotechnol. 14 1996 1239 1245
    • (1996) Nature Biotechnol. , vol.14 , pp. 1239-1245
    • Reiter, Y.1    Brinkmann, U.2    Lee3    Pastan, I.B.4
  • 8
    • 0033573928 scopus 로고    scopus 로고
    • Human single-chain Fv immunoconjugates targeted to a melanoma-associated chondroitin sulfate proteoglycan mediate specific lysis of human melanoma cells by natural killer cells and complement
    • B. Wang, Y.B. Chen, O. Ayalon, J. Bender, and A. Garen Human single-chain Fv immunoconjugates targeted to a melanoma-associated chondroitin sulfate proteoglycan mediate specific lysis of human melanoma cells by natural killer cells and complement Proc. Natl Acad. Sci. USA 96 1999 1627 1632
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 1627-1632
    • Wang, B.1    Chen, Y.B.2    Ayalon, O.3    Bender4    Garen, A.J.5
  • 9
    • 0029890636 scopus 로고    scopus 로고
    • Minibody: A novel engineered anti-carcinoembryonic antigen antibody fragment (single-chain Fv-CH3) which exhibits rapid, high-level targeting of xenografts
    • S. Hu, L. Shively, A. Raubitschek, M. Sherman, L.E. Williams, and J.Y. Wong Minibody: a novel engineered anti-carcinoembryonic antigen antibody fragment (single-chain Fv-CH3) which exhibits rapid, high-level targeting of xenografts Cancer Res. 56 1996 3055 3061
    • (1996) Cancer Res. , vol.56 , pp. 3055-3061
    • Hu, S.1    Shively, L.2    Raubitschek, A.3    Sherman, M.4    Williams5    Wong, J.Y.L.E.6
  • 10
    • 0026528230 scopus 로고
    • Miniantibodies: Use of amphipathic helices to produce functional, flexibly linked dimeric FV fragments with high avidity in Escherichia coli
    • P. Pack, and A. Pluckthun Miniantibodies: use of amphipathic helices to produce functional, flexibly linked dimeric FV fragments with high avidity in Escherichia coli Biochemistry 31 1992 1579 1584
    • (1992) Biochemistry , vol.31 , pp. 1579-1584
    • Pack1    Pluckthun, A.P.2
  • 11
    • 0027442660 scopus 로고
    • Improved bivalent miniantibodies, with identical avidity as whole antibodies, produced by high cell density fermentation of Escherichia coli
    • P. Pack, M. Kujau, V. Schroeckh, U. Knupfer, R. Wenderoth, D. Riesenberg, and A. Pluckthun Improved bivalent miniantibodies, with identical avidity as whole antibodies, produced by high cell density fermentation of Escherichia coli Biotechnology (NY) 11 1993 1271 1277
    • (1993) Biotechnology (NY) , vol.11 , pp. 1271-1277
    • Pack, P.1    Kujau, M.2    Schroeckh, V.3    Knupfer, U.4    Wenderoth, R.5    Riesenberg6    Pluckthun, A.D.7
  • 12
    • 0027197493 scopus 로고
    • "Diabodies": Small bivalent and bispecific antibody fragments
    • P. Holliger, T. Prospero, and G. Winter "Diabodies": small bivalent and bispecific antibody fragments Proc. Natl Acad. Sci. USA 90 1993 6444 6448
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 6444-6448
    • Holliger, P.1    Prospero2    Winter, G.T.3
  • 13
    • 0035793208 scopus 로고    scopus 로고
    • Stability engineering of antibody single-chain Fv fragments
    • A. Worn, and A. Pluckthun Stability engineering of antibody single-chain Fv fragments J. Mol. Biol. 305 2001 989 1010
    • (2001) J. Mol. Biol. , vol.305 , pp. 989-1010
    • Worn1    Pluckthun, A.A.2
  • 14
    • 0033506366 scopus 로고    scopus 로고
    • High avidity scFv multimers; Diabodies and triabodies
    • P.J. Hudson, and A.A. Kortt High avidity scFv multimers; diabodies and triabodies J. Immunol. Methods 231 1999 177 189
    • (1999) J. Immunol. Methods , vol.231 , pp. 177-189
    • Hudson1    Kortt, A.A.P.J.2
  • 15
    • 0027500718 scopus 로고
    • The biosynthesis of molybdopterin in Escherichia coli. Purification and characterization of the converting factor
    • D.M. Pitterle, and K.V. Rajagopalan The biosynthesis of molybdopterin in Escherichia coli. Purification and characterization of the converting factor J. Biol. Chem. 268 1993 13499 13505
    • (1993) J. Biol. Chem. , vol.268 , pp. 13499-13505
    • Pitterle1    Rajagopalan, K.V.D.M.2
  • 16
    • 0027490597 scopus 로고
    • In vitro synthesis of molybdopterin from precursor Z using purified converting factor. Role of protein-bound sulfur in formation of the dithiolene
    • D.M. Pitterle, J.L. Johnson, and K.V. Rajagopalan In vitro synthesis of molybdopterin from precursor Z using purified converting factor. Role of protein-bound sulfur in formation of the dithiolene J. Biol. Chem. 268 1993 13506 13509
    • (1993) J. Biol. Chem. , vol.268 , pp. 13506-13509
    • Pitterle, D.M.1    Johnson2    Rajagopalan, K.V.J.L.3
  • 17
    • 0035167185 scopus 로고    scopus 로고
    • Crystal structure of molybdopterin synthase and its evolutionary relationship to ubiquitin activation
    • M.J. Rudolph, M.M. Wuebbens, K.V. Rajagopalan, and H. Schindelin Crystal structure of molybdopterin synthase and its evolutionary relationship to ubiquitin activation Nature Struct. Biol. 8 2001 42 46
    • (2001) Nature Struct. Biol. , vol.8 , pp. 42-46
    • Rudolph, M.J.1    Wuebbens, M.M.2    Rajagopalan3    Schindelin, H.K.V.4
  • 18
    • 0037515652 scopus 로고    scopus 로고
    • Structural studies of molybdopterin synthase provide insights into its catalytic mechanism
    • M.J. Rudolph, M.M. Wuebbens, O. Turque, K.V. Rajagopalan, and H. Schindelin Structural studies of molybdopterin synthase provide insights into its catalytic mechanism J. Biol. Chem. 278 2003 14514 14522
    • (2003) J. Biol. Chem. , vol.278 , pp. 14514-14522
    • Rudolph, M.J.1    Wuebbens, M.M.2    Turque, O.3    Rajagopalan4    Schindelin, H.K.V.5
  • 19
    • 0037230075 scopus 로고    scopus 로고
    • Comparison of three microbial hosts for the expression of an active catalytic scFv
    • S. Robin, K. Petrov, T. Dintinger, A. Kujumdzieva, C. Tellier, and M. Dion Comparison of three microbial hosts for the expression of an active catalytic scFv Mol. Immunol. 39 2003 729 738
    • (2003) Mol. Immunol. , vol.39 , pp. 729-738
    • Robin, S.1    Petrov, K.2    Dintinger, T.3    Kujumdzieva, A.4    Tellier5    Dion, M.C.6
  • 22
    • 0025823716 scopus 로고
    • Identical V region amino acid sequences and segments of sequences in antibodies of different specificities. Relative contributions of VH and VL genes, minigenes, and complementarity-determining regions to binding of antibody-combining sites
    • E.A. Kabat, and T.T. Wu Identical V region amino acid sequences and segments of sequences in antibodies of different specificities. Relative contributions of VH and VL genes, minigenes, and complementarity-determining regions to binding of antibody-combining sites J. Immunol. 147 1991 1709 1719
    • (1991) J. Immunol. , vol.147 , pp. 1709-1719
    • Kabat1    Wu, T.T.E.A.2
  • 23
    • 0033598777 scopus 로고    scopus 로고
    • Efficient folding of proteins with multiple disulfide bonds in the Escherichia coli cytoplasm
    • P.H. Bessette, F. Aslund, J. Beckwith, and G. Georgiou Efficient folding of proteins with multiple disulfide bonds in the Escherichia coli cytoplasm Proc. Natl Acad. Sci. USA 96 1999 13703 13708
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 13703-13708
    • Bessette, P.H.1    Aslund, F.2    Beckwith3    Georgiou, G.J.4
  • 24
    • 0035860726 scopus 로고    scopus 로고
    • Characterization of Escherichia coli MoeB and its involvement in the activation of molybdopterin synthase for the biosynthesis of the molybdenum cofactor
    • S. Leimkuhler, M.M. Wuebbens, and K.V. Rajagopalan Characterization of Escherichia coli MoeB and its involvement in the activation of molybdopterin synthase for the biosynthesis of the molybdenum cofactor J. Biol. Chem. 276 2001 34695 34701
    • (2001) J. Biol. Chem. , vol.276 , pp. 34695-34701
    • Leimkuhler, S.1    Wuebbens2    Rajagopalan, K.V.M.M.3
  • 26
    • 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
    • Jager1    Pluckthun, A.M.2
  • 27
    • 0035823140 scopus 로고    scopus 로고
    • Helix-stabilized Fv (hsFv) antibody fragments: Substituting the constant domains of a Fab fragment for a heterodimeric coiled-coil domain
    • K.M. Arndt, K.M. Muller, and A. Pluckthun Helix-stabilized Fv (hsFv) antibody fragments: substituting the constant domains of a Fab fragment for a heterodimeric coiled-coil domain J. Mol. Biol. 312 2001 221 228
    • (2001) J. Mol. Biol. , vol.312 , pp. 221-228
    • Arndt, K.M.1    Muller2    Pluckthun, A.K.M.3
  • 28
    • 0030738617 scopus 로고    scopus 로고
    • New protein engineering approaches to multivalent and bispecific antibody fragments
    • A. Pluckthun, and P. Pack New protein engineering approaches to multivalent and bispecific antibody fragments Immunotechnology 3 1997 83 105
    • (1997) Immunotechnology , vol.3 , pp. 83-105
    • Pluckthun1    Pack, P.A.2
  • 29
    • 0037436345 scopus 로고    scopus 로고
    • The crystal structure of an anti-CEA scFv diabody assembled from T84.66 scFvs in V(L)-to-V(H) orientation: Implications for diabody flexibility
    • J.A. Carmichael, B.E. Power, T.P. Garrett, P.J. Yazaki, J.E. Shively, and A.A. Raubischek The crystal structure of an anti-CEA scFv diabody assembled from T84.66 scFvs in V(L)-to-V(H) orientation: implications for diabody flexibility J. Mol. Biol. 326 2003 341 351
    • (2003) J. Mol. Biol. , vol.326 , pp. 341-351
    • Carmichael, J.A.1    Power, B.E.2    Garrett, T.P.3    Yazaki, P.J.4    Shively5    Raubischek, A.A.J.E.6
  • 30
    • 0028774708 scopus 로고
    • Crystal structure of a diabody, a bivalent antibody fragment
    • O. Perisic, P.A. Webb, P. Holliger, G. Winter, and R.L. Williams Crystal structure of a diabody, a bivalent antibody fragment Structure 2 1994 1217 1226
    • (1994) Structure , vol.2 , pp. 1217-1226
    • Perisic, O.1    Webb, P.A.2    Holliger, P.3    Winter4    Williams, R.L.G.5
  • 31
    • 0033979551 scopus 로고    scopus 로고
    • Bivalency and epitope specificity of a high-affinity IgG3 monoclonal antibody to the Streptococcus group a carbohydrate antigen. Molecular modeling of a Fv fragment
    • J.B. Pitner, W.F. Beyer, T.M. Venetta, C. Nycz, M.J. Mitchell, and S.L. Harris Bivalency and epitope specificity of a high-affinity IgG3 monoclonal antibody to the Streptococcus group A carbohydrate antigen. Molecular modeling of a Fv fragment Carbohydr. Res. 324 2000 17 29
    • (2000) Carbohydr. Res. , vol.324 , pp. 17-29
    • Pitner, J.B.1    Beyer, W.F.2    Venetta, T.M.3    Nycz, C.4    Mitchell5    Harris, S.L.M.J.6
  • 32
    • 0033364822 scopus 로고    scopus 로고
    • Human molybdopterin synthase gene: Identification of a bicistronic transcript with overlapping reading frames
    • B. Stallmeyer, G. Drugeon, J. Reiss, A.L. Haenni, and R.R. Mendel Human molybdopterin synthase gene: identification of a bicistronic transcript with overlapping reading frames Am. J. Hum. Genet. 64 1999 698 705
    • (1999) Am. J. Hum. Genet. , vol.64 , pp. 698-705
    • Stallmeyer, B.1    Drugeon, G.2    Reiss, J.3    Haenni4    Mendel, R.R.A.L.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.