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Volumn 87, Issue 8, 2005, Pages 661-667

Improved stability and yield of Fv targeted superantigen by introducing both linker and disulfide bond into the targeting moiety

Author keywords

SAg; SEA(D227A); Single chain disulfide stabilized Fv; Stability; Yield

Indexed keywords

3 (4,5 DIMETHYLTHIAZOL 2 YL) 5 (3 CARBOXYMETHOXYPHENYL) 2 (4 SULFOPHENYL) 2H TETRAZOLIUM; CELL EXTRACT; DISULFIDE; GLYCYLGLYCYLGLYCYLSERYLGLYCYLGLYCYLSERINE; IMMUNOTOXIN; PEPTIDE DERIVATIVE; RECOMBINANT PROTEIN; SINGLE CHAIN FRAGMENT VARIABLE ANTIBODY; STAPHYLOCOCCUS ENTEROTOXIN A; SUPERANTIGEN; TETRAZOLIUM; UNCLASSIFIED DRUG;

EID: 23044488673     PISSN: 03009084     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.biochi.2005.04.005     Document Type: Article
Times cited : (14)

References (24)
  • 1
    • 0032403273 scopus 로고    scopus 로고
    • Recombinant Fv immunotoxins and Fv fragments as novel agents for cancer therapy and diagnosis
    • Y. Reiter, and I. Pastan Recombinant Fv immunotoxins and Fv fragments as novel agents for cancer therapy and diagnosis Trends Biotechnol. 16 1998 513 520
    • (1998) Trends Biotechnol. , vol.16 , pp. 513-520
    • Reiter, Y.1    Pastan, I.2
  • 2
    • 0032489877 scopus 로고    scopus 로고
    • Immunotoxins for targeted cancer therapy
    • R.J. Kreitman, and I. Pastan Immunotoxins for targeted cancer therapy Adv. Drug Deliv. Rev. 31 1998 53 88
    • (1998) Adv. Drug Deliv. Rev. , vol.31 , pp. 53-88
    • Kreitman, R.J.1    Pastan, I.2
  • 3
    • 0028559775 scopus 로고
    • Monoclonal antibody-superantigen fusion proteins: Tumor-specific agents for T-cell-based tumor therapy
    • M. Dohlsten, L. Abrahmsen, and P. Bjork Monoclonal antibody-superantigen fusion proteins: tumor-specific agents for T-cell-based tumor therapy Prac. Natl. Acad. Sci. USA 91 1994 8945 8949
    • (1994) Prac. Natl. Acad. Sci. USA , vol.91 , pp. 8945-8949
    • Dohlsten, M.1    Abrahmsen, L.2    Bjork, P.3
  • 4
    • 0029148195 scopus 로고
    • Immunotherapy of human colon cancer by antibody-targeted superantigens
    • M. Dohlsten, P. Lando, and P. Bjork Immunotherapy of human colon cancer by antibody-targeted superantigens Cancer Immunol. Immunother. 41 1995 162 168
    • (1995) Cancer Immunol. Immunother. , vol.41 , pp. 162-168
    • Dohlsten, M.1    Lando, P.2    Bjork, P.3
  • 5
    • 0036594855 scopus 로고    scopus 로고
    • Targeted therapy against human lung cancer in nude mice by high-affinity recombinant antimesothelin single-chain Fv immunotoxin
    • D. Fan, S. Yano, and H. Shinohara Targeted therapy against human lung cancer in nude mice by high-affinity recombinant antimesothelin single-chain Fv immunotoxin Mol. Cancer Ther. 1 2002 595 600
    • (2002) Mol. Cancer Ther. , vol.1 , pp. 595-600
    • Fan, D.1    Yano, S.2    Shinohara, H.3
  • 6
    • 0029960032 scopus 로고    scopus 로고
    • Antibody engineering of recombinant Fv immunotoxins for improved targeting of cancer: Disulfide-stabilized Fv immunotoxins
    • Y. Reiter, and I. Pastan Antibody engineering of recombinant Fv immunotoxins for improved targeting of cancer: disulfide-stabilized Fv immunotoxins Clin. Cancer Res. 252 1996 245 252
    • (1996) Clin. Cancer Res. , vol.252 , pp. 245-252
    • Reiter, Y.1    Pastan, I.2
  • 7
    • 0030030531 scopus 로고    scopus 로고
    • Antibody-targeted superantigen therapy induces tumor-infiltrating lymphocytes, excessive cytokine production, and apoptosis in human colon carcinoma
    • M.J. Litton, M. Dohisten, and P.A. Lando Antibody-targeted superantigen therapy induces tumor-infiltrating lymphocytes, excessive cytokine production, and apoptosis in human colon carcinoma Eur. J. Immunol. 26 1996 1 9
    • (1996) Eur. J. Immunol. , vol.26 , pp. 1-9
    • Litton, M.J.1    Dohisten, M.2    Lando, P.A.3
  • 8
    • 0035816233 scopus 로고    scopus 로고
    • Therapy of human non-small-cell lung carcinoma using antibody targeting of a modified superantigen
    • G. Forsberg, L. Ohlsson, and T. Brodln Therapy of human non-small-cell lung carcinoma using antibody targeting of a modified superantigen Br. J. Cancer 85 2001 129 136
    • (2001) Br. J. Cancer , vol.85 , pp. 129-136
    • Forsberg, G.1    Ohlsson, L.2    Brodln, T.3
  • 9
    • 0031422492 scopus 로고    scopus 로고
    • A form of anti-Tac(Fv) which is both single-chain and disulfide-stabilized: Comparison with its single-chain and disulfide-stabilized homologs
    • V. Rajagopal, I. Pastan, and R.J. Kreitman A form of anti-Tac(Fv) which is both single-chain and disulfide-stabilized: comparison with its single-chain and disulfide-stabilized homologs Protein Eng. 10 1997 1453 1459
    • (1997) Protein Eng. , vol.10 , pp. 1453-1459
    • Rajagopal, V.1    Pastan, I.2    Kreitman, R.J.3
  • 10
    • 0031961152 scopus 로고    scopus 로고
    • Similarities in the biodistribution of Iodine-labeled anti-Tac single-chain disulfide-stabilized Fv fragment
    • H. Kobayashi, E.S. Han, and I.S. Kim Similarities in the biodistribution of Iodine-labeled anti-Tac single-chain disulfide-stabilized Fv fragment Nucl. Med. Biol. 25 1998 387 393
    • (1998) Nucl. Med. Biol. , vol.25 , pp. 387-393
    • Kobayashi, H.1    Han, E.S.2    Kim, I.S.3
  • 11
    • 0029557830 scopus 로고
    • Thermal stabilization of a single-chain Fv antibody fragment by introduction of a disulphide bond
    • N.M. Young, and C.R. Mackenzie Thermal stabilization of a single-chain Fv antibody fragment by introduction of a disulphide bond FEBS Lett. 377 1995 135 139
    • (1995) FEBS Lett. , vol.377 , pp. 135-139
    • Young, N.M.1    MacKenzie, C.R.2
  • 12
    • 0030951016 scopus 로고    scopus 로고
    • Genetically engineeered superantigens as tolerable antitumor agents
    • J. Hansson, L. Ohlsson, and R. Persson Genetically engineeered superantigens as tolerable antitumor agents Proc. Natl. Acad. Sci. USA 94 1997 2489 2494
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 2489-2494
    • Hansson, J.1    Ohlsson, L.2    Persson, R.3
  • 13
    • 0028275293 scopus 로고
    • Design of interchain disulfide bonds in the framework region of the Fv of the monoclonal antibody B3
    • S.-H. Jung, I. Pastan, and B.K. Lee Design of interchain disulfide bonds in the framework region of the Fv of the monoclonal antibody B3 Proteins Struct. Funct. Genet. 19 1994 35 47
    • (1994) Proteins Struct. Funct. Genet. , vol.19 , pp. 35-47
    • Jung, S.-H.1    Pastan, I.2    Lee, B.K.3
  • 15
    • 0026792807 scopus 로고
    • A method for increasing the yield of properly folded recombinant fusion proteins: Single-chain immunotoxins from renaturation of bacterial inclusion bodies
    • J. Buchner, I. Pastan, and U. Brinkmann A method for increasing the yield of properly folded recombinant fusion proteins: single-chain immunotoxins from renaturation of bacterial inclusion bodies Anal. Biochem. 205 1992 263 270
    • (1992) Anal. Biochem. , vol.205 , pp. 263-270
    • Buchner, J.1    Pastan, I.2    Brinkmann, U.3
  • 16
    • 0032191701 scopus 로고    scopus 로고
    • Highly efficient recovery of functional single-chain Fv fragments from inclusion bodies overexpressed in Escherichia coli by controlled introduction of oxidizing reagent-application to a human single-chain Fv fragment
    • K. Tsumoto, K. Shinoki, and H. Kondo Highly efficient recovery of functional single-chain Fv fragments from inclusion bodies overexpressed in Escherichia coli by controlled introduction of oxidizing reagent-application to a human single-chain Fv fragment J. Immunol. Methods 219 1998 119 129
    • (1998) J. Immunol. Methods , vol.219 , pp. 119-129
    • Tsumoto, K.1    Shinoki, K.2    Kondo, H.3
  • 17
    • 0036296338 scopus 로고    scopus 로고
    • Production of functional single-chain Fv antibodies in the cytoplasm of Escherichia coli
    • P. Jurado, D. Ritz, and J. Beckwith Production of functional single-chain Fv antibodies in the cytoplasm of Escherichia coli J. Mol. Biol. 320 2002 1 10
    • (2002) J. Mol. Biol. , vol.320 , pp. 1-10
    • Jurado, P.1    Ritz, D.2    Beckwith, J.3
  • 18
    • 0030054910 scopus 로고    scopus 로고
    • Recombinant single-chain and disulfide-stabilized Fv-immunotoxins that cause complete regression of a human colon cancer xenograft in nude mice
    • Y. Reiter, A.F. Wright, and D.W. Tonge Recombinant single-chain and disulfide-stabilized Fv-immunotoxins that cause complete regression of a human colon cancer xenograft in nude mice Int. J. Cancer 67 1996 113 123
    • (1996) Int. J. Cancer , vol.67 , pp. 113-123
    • Reiter, Y.1    Wright, A.F.2    Tonge, D.W.3
  • 19
    • 0036174958 scopus 로고    scopus 로고
    • A mutated superantigen SEA D227A fusion diabody specific to MUC1 and CD3 in targeted cancer immunotherapy for bile duct carcinoma
    • S. Takemura, T. Kudo, and R. Asano A mutated superantigen SEA D227A fusion diabody specific to MUC1 and CD3 in targeted cancer immunotherapy for bile duct carcinoma Cancer Immunol. Immunother. 51 2002 33 44
    • (2002) Cancer Immunol. Immunother. , vol.51 , pp. 33-44
    • Takemura, S.1    Kudo, T.2    Asano, R.3
  • 20
    • 0030965970 scopus 로고    scopus 로고
    • Disrupting the hydrophobic patches at the antibody variable/constant domain interface: Improved in vivo folding and physical characterization of an engineered ScFv fragment
    • L. Neiba, A. Honeggar, C. Krebber, and A. Pluckthum Disrupting the hydrophobic patches at the antibody variable/constant domain interface: improved in vivo folding and physical characterization of an engineered ScFv fragment Protein Eng. 10 1997 435 444
    • (1997) Protein Eng. , vol.10 , pp. 435-444
    • Neiba, L.1    Honeggar, A.2    Krebber, C.3    Pluckthum, A.4
  • 21
    • 0030916353 scopus 로고    scopus 로고
    • Murtin, Two amino acid mutations in an anti-human CD3 single-chain Fv antibody fragment that affect the yield on bacterial secretion but not the affinity
    • S.M. Kipriyanov, and G. Moldenhauer Murtin, Two amino acid mutations in an anti-human CD3 single-chain Fv antibody fragment that affect the yield on bacterial secretion but not the affinity Protein Eng. 10 1997 445 453
    • (1997) Protein Eng. , vol.10 , pp. 445-453
    • Kipriyanov, S.M.1    Moldenhauer, G.2
  • 22
    • 0032483392 scopus 로고    scopus 로고
    • Improved stability and yield of a Fv-toxin fusion protein by computer design and protein engineering of the Fv
    • P.S. Chowdhury, G. Vasmatzis, and R. Beers Improved stability and yield of a Fv-toxin fusion protein by computer design and protein engineering of the Fv J. Mol. Biol. 281 1998 917 928
    • (1998) J. Mol. Biol. , vol.281 , pp. 917-928
    • Chowdhury, P.S.1    Vasmatzis, G.2    Beers, R.3
  • 23
    • 0028951128 scopus 로고
    • Preparation and characterization of a disulfide-stabilized Fv fragment of the anti-Tac antibody: Comparison with its single-chain analog
    • K.O. Webber, Y. Reiter, and U. Brinkmann Preparation and characterization of a disulfide-stabilized Fv fragment of the anti-Tac antibody: comparison with its single-chain analog Mol. Immunol. 32 1995 249 258
    • (1995) Mol. Immunol. , vol.32 , pp. 249-258
    • Webber, K.O.1    Reiter, Y.2    Brinkmann, U.3
  • 24
    • 0037205497 scopus 로고    scopus 로고
    • Formation of disulfide bridges by a single-chain Fv antibody in the reducing ectopic environment of the plant cytosol
    • A. Schouten, J. Roosien, J. Bakker, and A. Schots Formation of disulfide bridges by a single-chain Fv antibody in the reducing ectopic environment of the plant cytosol J. Biol. Chem. 277 2002 19339 19345
    • (2002) J. Biol. Chem. , vol.277 , pp. 19339-19345
    • Schouten, A.1    Roosien, J.2    Bakker, J.3    Schots, A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.