Functional Intracellular Antibody Fragments Do Not Require Invariant Intra-domain Disulfide Bonds

Journal of Molecular Biology

Volumn 376, Issue 3, 2008, Pages 749-757

  Tanaka, Tomoyuki ^a,b   Rabbitts, Terence H ^a,b  

^a MRC LABORATORY OF MOLECULAR BIOLOGY   (United Kingdom)

^b ST JAMES S UNIVERSITY HOSPITAL   (United Kingdom)

Author keywords

disulfide free; intrabody; RAS; single domains; X ray crystallography

Indexed keywords

ANTIGEN; CELL ANTIBODY;

ANIMAL CELL; ANTIBODY STRUCTURE; ARTICLE; CRYSTAL STRUCTURE; DISULFIDE BOND; DRUG SYNTHESIS; IN VIVO STUDY; LIGHT CHAIN; MOUSE; NONHUMAN; PRIORITY JOURNAL; TECHNOLOGY;

EID: 38649116010     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2007.11.085     Document Type: Article

References (22)

1. Lobato M.N., and Rabbitts T.H. Intracellular antibodies and challenges facing their use as therapeutic agents. Trends Mol. Med. 9 (2003) 390-396
2. Tanaka T., Williams R.L., and Rabbitts T.H. Tumour prevention by a single antibody domain inhibiting binding of signal transduction molecules to activated RAS. EMBO J. 26 (2007) 3250-3259
3. Worn A., and Pluckthun A. Stability engineering of antibody scFv-chain Fv fragments. J. Mol. Biol. 305 (2001) 989-1010
4. Worn A., and Pluckthun A. An intrinsically stable antibody scFv fragment can tolerate the loss of both disulfide bonds and fold correctly. FEBS Lett. 427 (1998) 357-361
5. Proba K., Worn A., Honegger A., and Pluckthun A. Antibody scFv fragments without disulfide bonds made by molecular evolution. J. Mol. Biol. 275 (1998) 245-253
6. Worn A., and Pluckthun A. Different equilibrium stability behavior of ScFv fragments: identification, classification, and improvement by protein engineering. Biochemistry 38 (1999) 8739-8750
7. Visintin M., Settanni G., Maritan A., Graziosi S., Marks J.D., and Cattaneo A. The intracellular antibody capture technology (IACT): towards a consensus sequence for intracellular antibodies. J. Mol. Biol. 317 (2002) 73-83
8. Tse E., Lobato M.N., Forster A., Tanaka T., Chung G.T.Y., and Rabbitts T.H. Intracellular antibody capture technology: application to selection of single chain Fv recognising the BCR-ABL oncogenic protein. J. Mol. Biol. 317 (2002) 85-94
9. Tanaka T., and Rabbitts T.H. Intrabodies based on intracellular capture frameworks that bind the RAS protein with high affinity and impair oncogenic transformation. EMBO J. 22 (2003) 1025-1035
10. Tanaka T., Lobato M.N., and Rabbitts T.H. Single domain intracellular antibodies: a minimal fragment for direct in vivo selection of antigen-specific intrabodies. J. Mol. Biol. 331 (2003) 1109-1120
11. Lefranc M.P., Pommié C., Ruiz M., Giudicelli V., Foulquier E., Truong L., et al. IMGT unique numbering for immunoglobulin and T cell receptor variable domains and Ig superfamily V-like domains. Dev. Comp. Immunol. 27 (2003) 55-77
12. Creighton T.E. Proteins: Structure and Molecular Properties (1983), Freeman, New York
13. Costa G.L., Benson J.M., Seroogy C.M., Achacoso P., Fathman C.G., and Nolan G.P. Targeting rare populations of murine antigen-specific T lymphocytes by retroviral transduction for potential application in gene therapy for autoimmune disease. J. Immunol. 164 (2000) 3581-3589
14. Colby D.W., Chu Y., Cassady J.P., Duennwald M., Zazulak H., Webster J.M., et al. Potent inhibition of Huntington aggregation and cytotoxicity by a disulfide bond-free single-domain intracellular antibody. Proc. Natl Acad. Sci. USA 101 (2004) 17616-17621
15. Ewert S., Honegger A., and Pluckthun A. Stability improvement of antibodies for extracellular and intracellular applications: CDR grafting to stable frameworks and structure-based framework engineering. Methods 34 (2004) 184-199
16. Tanaka T., Chung G.T.Y., Forster A., Lobato M.N., and Rabbitts T.H. De novo production of diverse intracellular antibody libraries. Nucleic Acids Res. 31 (2003) e23
17. Leslie A.G.W. Recent Changes to the MOSFLM Package for Processing Film and Image Plate Data. In Joint CCP4 and ESF-EACMB Newsletter on Protein Crystallography (1992), 26, Daresbury Laboratory, Warrington, UK
18. CCP4. The CCP4 suite: programs for protein crystallography. Acta Crystallogr. Sect. D 50 (1994) 760-763
19. Navaza J. AMoRe: An Automated Package for Molecular Replacement. Acta Crystallogr. Sect. A 50 (1994) 157-163
20. Jones T.A., Zou J.Y., Cowan S.W., and Kjeldgaard M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. Sect. A 47 (1991) 110-119
21. Murshudov G.N., Vagin A.A., and Dodson E.J. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr. Sect. D 53 (1997) 240-255
22. Laskowski R.A., MacArthur M.W., Moss D.S., and Thornton J.M. PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallogr. 26 (1993) 283-291