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US7442159: Selection system

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Filing Information

Inventor(s) Lutz Riechmann · Peter Kristensen · Jean-Luc Jestin · Gregory Paul Winter ·
Assignee(s) Domantis Limited ·
Attorney/Agent(s) Kathleen Williams · Edwards Angell Palmer & Dodge LLP ·
Primary Examiner Jon D. Epperson ·
Assistant Examiner Amber D. Steele ·
Application Number US9710444
Filing date 11/10/2000
Issue date 10/28/2008
Predicted expiration date 05/30/2021
Patent term adjustment 748
U.S. Classifications 506/6  · 435/6  · 506/14  · 506/9  ·
International Classifications C12Q168  · C40B2008  · C40B3004  · C40B4002  ·
Kind CodeB1
Related U.S. Application DataThis is a continuation of International Application GB99/01526, with an international filing date of May 13, 1999, now abandoned. The invention relates to a selection system which permits the selection of polypeptides displayed in a phage display system.
Foreign Priority GB9810223.9 - 05/13/1998 · GB9810228.8 - 05/13/1998 ·
21 Claims, 6 Drawings


Abstract

The present invention concerns a method for the selection of a virus comprising the steps of: (a) providing a virus encoding and displaying a fusion polypeptide, said fusion polypeptide comprising a heterologous polypeptide inserted into the sequence of a viral coat protein polypeptide, wherein said virus comprises a cleavable site located within a displayed polypeptide; (b) exposing the virus to a cleaving agent; (c) propagating the virus comprising intact fusion protein.

Independent Claims | See all claims (21)

  1. 1. A method for the selection of a bacteriophage comprising the steps of: (a) providing a plurality of bacteriophage encoding and displaying a fusion polypeptide, said displayed fusion polypeptide comprising a heterologous polypeptide inserted into the sequence of a bacteriophage coat wherein said plurality of bacteriophage comprise a sequence specific protease cleavable site located within the displayed polypeptide and which site is protected by folding of the displayed fusion polypeptide and is either absent from the bacteriophage other than the site specific insertion, or inaccessible to cleavage, or present only in bacteriophage proteins not required after bacteriophage assembly to mediate infection and wherein cleavage of said sequence specific protease cleavable site impairs infection by a said bacteriophage; (b) exposing the bacteriophage to a protease that recognizes said sequence specific protease cleavable site, wherein said protease only cleaves said sequence specific protease cleavable site if said displayed fusion polypeptide is not properly folded, such that said exposing selects against bacteriophage displaying fusion polypeptide that is not properly folded; and (c) propagating a bacteriophage comprising intact displayed fusion polypeptide.

References Cited

U.S. Patent Documents

Document NumberAssigneesInventorsIssue/Pub Date
US5223409* Protein Engineering Corp. Ladner et al. Jun 1993
US5432018* Affymax Technologies N.V. Dower et al. Jul 1995
US5849500* Deutsches Krebsforschungszentrum Stiftung des Offentlichen Rechts Breitling et al. Dec 1998

Foreign Patent Documents

Document NumberAssigneesInventorsIssue/Pub Date
WO199005144May 1990
WO199014430Nov 1990
WO199201047Jan 1992
WO199220791Nov 1992
WO199311236Jun 1993
* cited by examiner

Other Publications

Smith, G. P., 1985, Filamentous Phage: Novel Expression Vectors that Display Cloned Antigens on the Virion Surface, Science, vol. 228, pp. 1315-1317.*
Sieber et al., Oct. 1998, Nature Biotechnology, vol. 16, pp. 955-960, Selecting proteins with improved stability by a phage-based method.*
Kristensen and Winter, Jul. 1998, Folding & Design, vol. 3, pp. 321-328, Proteolytic selection for protein folding using filamentous bacteriophage.*
Rubingh, D.N. (1997). Protein engineering from a bioindustrial point of view. Current Opinion in Biotechnology. 8, 417-422.
Fersht, A.R. (1993). Protein folding and stability: the pathway of folding of barnase. FEBS Letters. 325, 5-16.
Zhao, H., et al. (1998). Molecular evolution by staggered extension process (StEP) in vitro recombination. Nature Biotechnology. 16, 258-261.
Patten, P.A., R.J. Howard, and W.P.C. Stemmer. (1997). Applications of DNA shuffling to pharmaceuticals and vaccines. Current Opinion in Biotechnology. 8, 724-733.
Sauer, R.T. (1996). Protein folding from a combinatorial perspective. Folding & Design. 1, R27-R30.
Dahiyat, B.I., C.A. Sarisky, and S.L. Mayo. (1997). Dc Novo Protein Design: Towards Fully Automated Sequence Selection. Journal of Molecular Biology. 273, 789-796.
Riddle, D.S., et al. (1997). Functional rapidly folding proteins from simplified amino acid sequences. Nature Structural Biology. 4(10), 805-809.
Hoogenboom, H.R. and G. Winter. (1992). By-passing Immunisation. Human Antibodies from Synthetic Repertoires of Germline VH Gene Segments Rearranged in Vitro. Journal of Molecular Biology. 227, 381-388.
Winter, G., et al. (1994). Making Antibodies by Phage Display Technology. Annual Review of Immunology. 12, 433-455.
Braisted, A.C. and J.A. Wells. (1996). Minimizing a binding domain from protein A. Proc. Natl. Acad. Sci. USA. 93, 5688-5692.
Gu, H., et al. (1995). A phage display system for studying the sequence determinants of protein folding. Protein Science. 4, 1108-1117.
Hubbard, S.J., F. Eisenmenger, and J.M. Thornton. (1994). Modeling studies of the change in conformation required for cleavage of limited proteolytic sites. Protein Science. 3, 757-768.
Fontana, A., et al. (1997). Probing the partly folded states of proteins by limited proteolysis. Folding & Design. 2, R17-R26.
Kamtekar, S., et al. (1993). Protein Design by Binary Patterning of Polar and Nonpolar Amino Acids. Science. 262, 1680-1685.
Davidson, A.R. and R.T. Sauer. (1994). Folded proteins occur frequently in libraries of random amino acid sequences. Proc. Natl. Acad. Sci. USA. 91, 2146-2150.
Davidson, A.R., K.J. Lumb, and R.T. Sauer. (1995). Cooperatively folded proteins in random sequence libraries. Nature Structural Biology. 2(10), 856-864.
Matthews, D.J. and J.A. Wells. (1993). Substrate Phage: Selection of Protease Substrates by Monovalent Phage Display. Science. 260, 1113-1117.
Riechmann, L. and P. Holliger. (1997). The C-Terminal Domain of TolA Is the Coreceptor for Filamentous Phage Infection of E. coli. Cell. 90, 351-360.
Smith, G.P. (1985). Filamentous Fusion Phage: Novel Expression Vectors That Display Cloned Antigens on the Virion Surface. Science. 228, 1315-1317.
Krebber, C., et al. (1997). Selectively-infective Phage (SIP): A Mechanistic Dissection of a Novel in vivo Selection for Protein-ligand Interactions. Journal of Molecular Biology. 268, 607-618.
Stengele, I., et al. (1990). Dissection of Functional Domains in Phage fd Adsorption Protein. Discrimination between Attachment and Penetration. Journal of Molecular Biology. 212, 143-149.
Gray, C.W., R.S. Brown, and D.A. Marvin. (1981). Adsorption complex of Filamentous fd virus. Journal of Molecular Biology. 146, 621-627.
Hoogenboom, H.R., et al. (1991). Multi-subunit proteins on the surface of filamentous phage: methodologies for displaying antibody (Fab) heavy and light chains. Nucleic Acids Research. 19, 4133-4137.
Bass, S., R. Greene, and J.A. Wells. (1990). Hormone Phage: An Enrichment Method for Variant Proteins With Altered Binding Properties. Proteins. 8, 309-314.
Nissim, A., et al. (1994). Antibody fragments from a “single pot” phage display library as immunochemical reagents. The EMBO Journal. 13, 692-698.
Marzari, R., et al. (1997). Extending filamentous phage host range by the grafting of a heterologous receptor binding domain. Gene. 185, 27-33.
Mossakowska, D.E., K. Nyberg, and A.R. Fresht. (1989). Kinetic Characterisation of the Recombinant Ribonuclease from Bacillus amyloliquefaciens (Barnese) and Investigation of Key Residues in Catalysis by Site-Directed Mutagenesis. Biochemistry. 28, 3843-3850.
Meiering, E.M., L. Serrano, and A.R. Fersht. (1992). Effect of Active Site Residues in Barnase on Activity and Stability, Journal of Molecular Biology. 225, 585-589.
Serrano, L., et al. (1992). The Folding of an Enzyme. II Substructure of Barnase and the Contribution of Different Interactions to Protein Stability. Journal of Molecular Biology. 224, 783-804.
McKnight, C.J., P.T. Matsudaira, and P.S. Kim. (1997). NMR structure of the 35-residue villin headpiece subdomain. Nature Structural Biology. 4(3), 180-184.
McKnight, C.J., et al. (1996). A Thermostable 35-Residue Subdomain within Villin Headpiece. Journal of Molecular Biology. 260, 126-134.
Xu, D. and R. Nussinov. (1997). Favorable domain size in proteins. Folding & Design. 3, 11-17.
Kippen, A.D. and AR. Fersht. (1995). Analysis of the Mechanism of Assembly of Cleaved Barnase from Two Peptide Fragments and Its Relevance to the Folding Pathway of Uncleaved Barnase. Biochemistry. 34, 1464-1468.
Gay, G.d.P. and A.R. Fersht. (1994). Generation of a Family of Protein Fragments for Structure-Folding Studies. 1. Folding Complementation of Two Fragments of Chymostrypsin Inhibitor-2 Formed by Cleavage at Its Unique Methionine Residue. Biochemistry. 33, 7957-7963.
Wu, L.C., R. Grandori, and J. Carey. (1994). Autonomous subdomains in protein folding. Protein Science. 3, 369-371.
Kwon, W.S., N.A.D. Silva, and J.T. Kellis. (1996). Relationships between thermal stability, degradation rate and expression yield of barnase variants in the periplasm of Escherichia coli. Protein Engineering. 9(12), 1197-1202.
Axe, D.D., N.W. Foster, and A.R. Fersht. (1996). Active barnase variants with completely random hydrophobic cores. Proc. Natl. Acad. Sci. USA. 93, 5590-5594.
Waldburger, C.D., J.F. Schildbach, and R.T. Sauer. (1995). Are buried salt bridges important for protein stability and conformational specificity? Nature Structural Biology. 2(2), 122-128.
Roy, S., et al. (1997). A Protein Designed by Binary Patterning of Polar and Nonpolar Amino Acids Displays Native-like Properties. Journal of the American Chemical Society. 119, 5302-5306.
Clackson, T., et al. (1991). Making antibody fragments using phage display libraries. Nature. 352, 624-628.
McCafferty, J., et al. (1990). Phage antibodies: filamentous phage displaying antibody variable domains. Nature. 348, 552-554.
Fisch, I., et al. (1996). A strategy of exon shuffling for making large peptide repertoires displayed on filamentous bacteriophage. Proc. Natl. Acad. Sci. USA. 93, 7761-7766.
Matouschek, A., et al. (1989). Mapping the transition state and pathway of protein folding by protein engineering. Nature. 340, 122-126.
Laemmli, U.K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227, 680-685.
Schatz, G. and Dobberstein, B. (1996). Common principles of protein translocation across membranes. Science. 271, 1519-1526.
Von Heijne, G. (1998). Life and death of a signal peptide. Nature. 396, 111-113.
Sprengart, M.L., Fuchs, E. and Porter, A.G. (1996). The downstream box: an efficient and independent translation initiation signal in E.coli. The EMBO Journal. 15, 665-674.
Perlman, D. and Halvorson, H.O. (1983). A putative signal peptidase recognition site and sequence in eukaryotic and prokaryotic signal peptides. Journal of Molecular Biology. 167, 391-409.
Von Heijne, G. (1983). Patterns of amino acids near signal-sequence cleavage sites. Eur. J. Biochem. 133, 17-21.
Pedersen, H., Hölder, S., Sutherlin, D.P., Schwitter, U., King, D.S., Schultz, P.G. (1998). Proc. Natl. Acad. Sci. USA. 95, 10523-10528.
Clackson et al., “In vitro selection from protein and peptide libraries,” TIBTECH (1994) 12:173-184.
McConnell et al., “Construction and screening of M13 phage libraries displaying long random peptides,” Molecular Diversity, 1 (1995) 165-176.
Ward et al., “Retrieval of human antibodies from phage-display libraries using enzymatic cleavage,” J. of Immunological Methods 189 (1996), 73-82.
* cited by examiner

Referenced By

The current document is not referenced by other documents.