Production of stabilized scFv antibody fragments in the E. coli bacterial cytoplasm

Methods in Molecular Biology

Volumn 1060, Issue , 2014, Pages 171-184

  Vaks, Lilach ^a   Benhar, Itai ^a  

^a TEL AVIV UNIVERSITY   (Israel)

Author keywords

Maltose binding protein (MBP); Single chain variable fragment (scFv); Tobacco etch virus (TEV)

Indexed keywords

HYBRID PROTEIN; MALTOSE BINDING PROTEIN; NITRILOTRIACETATE NICKEL; SINGLE CHAIN FRAGMENT VARIABLE ANTIBODY;

ANTIBODY PRODUCTION; ARTICLE; BACTERIAL CYTOPLASM; BACTERIAL GROWTH; CARBOXY TERMINAL SEQUENCE; CELL INCLUSION; CODON USAGE; CYTOPLASM; DISULFIDE BOND; ESCHERICHIA COLI; GEL PERMEATION CHROMATOGRAPHY; GENE EXPRESSION SYSTEM; NONHUMAN; PRIORITY JOURNAL; PROTEIN CLEAVAGE; PROTEIN EXPRESSION; PROTEIN PURIFICATION; PROTEIN REFOLDING; PLASMID;

BACTERIA (MICROORGANISMS); TOBACCO ETCH VIRUS;

ANIMALS; CYTOPLASM; ESCHERICHIA COLI; GENETIC VECTORS; HUMANS; PROTEIN ENGINEERING; RECOMBINANT FUSION PROTEINS; SINGLE-CHAIN ANTIBODIES;

EID: 84931262211     PISSN: 10643745     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-1-62703-586-6_10     Document Type: Article

References (18)

1. Hagemeyer CE, von Zur Muhlen C, von Elverfeldt D, Peter K (2009) Single-chain antibodies as diagnostic tools and therapeutic agents. Thromb Haemost 101:1012-1
2. Green LL (1999) Antibody engineering via genetic engineering of the mouse: XenoMouse strains are a vehicle for the facile generation of therapeutic human monoclonal antibodies. J Immunol Methods 231:11-2
3. Tomizuka K, Shinohara T, Yoshida H, Uejima H, Ohguma A, Tanaka S, Sato K, Oshimura M, Ishida I (2000) Double trans- chromosomic mice: maintenance of two individual human chromosome fragments containing Ig heavy and kappa loci and expression of fully human antibodies. Proc Natl Acad Sci USA 97:722-7
4. Terness P, Welschof M, Moldenhauer G, Jung M, Moroder L, Kirchhoff F, Kipriyanov S, Little M, Opelz G (1997) Idiotypic vaccine for treatment of human B-cell lymphoma. Construction of IgG variable regions from single malignant B cells. Hum Immunol 56: 17-2
5. Hakim R, Benhar I (2009) "Inclonals": IgGs and IgG-enzyme fusion proteins produced in an E. coli expression-refolding system. MAbs 1:281-2
6. Kipriyanov SM (2003) Generation of antibody molecules through antibody engineering. Methods Mol Biol 207:3-2
7. Bird RE, Hardman KD, Jacobson JW, Johnson S, Kaufman BM, Lee SM, Lee T, Pope SH, Riordan GS, Whitlow M (1988) Single-chain antigen-binding proteins. Science 242:423-4
8. Kim SJ, Park Y, Hong HJ (2005) Antibody engineering for the development of therapeutic antibodies. Mol Cells 20:17-2
9. Olafsen T, Sirk SJ, Betting DJ, Kenanova VE, Bauer KB, Ladno W, Raubitschek AA, Timmerman JM, Wu AM (2010) ImmunoPET imaging of B-cell lymphoma using 124I-anti-CD20 scFv dimers (diabodies). Protein Eng Des Sel 23:243-249
10. Yokota T, Milenic DE, Whitlow M, Schlom J (1992) Rapid tumor penetration of a singlechain Fv and comparison with other immunoglobulin forms. Cancer Res 52:3402-3408
11. Kipriyanov S (2002) High-level periplasmic expression and purification of scFvs. In: O'Brien PM, Aitken R (eds) Antibody phage display. Humana, New Jersey, pp 333-341
12. Bach H, Mazor Y, Shaky S, Shoham-Lev A, Berdichevsky Y, Gutnick DL, Benhar I (2001) Escherichia coli maltose-binding protein as a molecular chaperone for recombinant intracellular cytoplasmic single-chain antibodies. J Mol Biol 312:79-93
13. Kapust RB, Waugh DS (2000) Controlled intracellular processing of fusion proteins by TEV protease. Protein Expr Purif 19:312-318
14. Kapust RB, Waugh DS (1999) Escherichia coli maltose-binding protein is uncommonly effective at promoting the solubility of polypeptides to which it is fused. Protein Sci 8:1668-1674
15. Huston JS, Levinson D, Mudgett-Hunter M, Tai MS, Novotny J, Margolies MN, Ridge RJ, Bruccoleri RE, Haber E, Crea R et al (1988) Protein engineering of antibody binding sites: recovery of specific activity in an anti-digoxin single-chain Fv analogue produced in Escherichia coli . Proc Natl Acad Sci USA 85:5879-5883
16. Lei X, Ahn K, Zhu L, Ubarretxena-Belandia I, Li YM (2008) Soluble oligomers of the intramembrane serine protease YqgP are catalytically active in the absence of detergents. Biochemistry 47:11920-11929
17. Zanier K, Nomine Y, Charbonnier S, Ruhlmann C, Schultz P, Schweizer J, Trave G (2007) Formation of well-defined soluble aggregates upon fusion to MBP is a generic property of E6 proteins from various human papillomavirus species. Protein Expr Purif 51:59-70
18. Nomine Y, Ristriani T, Laurent C, Lefevre JF, Weiss E, Trave G (2001) Formation of soluble inclusion bodies by hpv e6 oncoprotein fused to maltose-binding protein. Protein Expr Purif 23:22-32