Self-assembly molecules

Chemistry: molecular biology and microbiology – Measuring or testing process involving enzymes or... – Involving antigen-antibody binding – specific binding protein...

Reexamination Certificate

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C435S007200, C436S517000

Reexamination Certificate

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07655412

ABSTRACT:
There is provided a method of forming a multimeric complex having affinity for a target. The method comprises: obtaining a plurality of self-assembly molecules, said self-assembly molecules including complementary self-assembly units such as verotoxin subunit B, each of which is operatively connected to an interaction domain such as a single domain antibody specific for the target; and combining said self-assembly molecules such that at least three said self-assembly units simultaneously bind to one another so as to permit the single domain antibodies to bind the target.

REFERENCES:
patent: 4208479 (1980-06-01), Zuk et al.
patent: 5744346 (1998-04-01), Chrysler et al.
patent: 5837242 (1998-11-01), Holliger et al.
patent: 5919643 (1999-07-01), Kelley et al.
patent: 5955293 (1999-09-01), Keusch et al.
patent: 6310043 (2001-10-01), Bundle et al.
patent: 6485726 (2002-11-01), Blumberg et al.
patent: 6548066 (2003-04-01), Michaeli et al.
patent: 7385032 (2008-06-01), Tschopp et al.
patent: 2002/0041865 (2002-04-01), Austin et al.
patent: WO 0061183 (2000-10-01), None
patent: WO-0127144 (2001-04-01), None
patent: WO-0149866 (2001-07-01), None
Davies et al. (Protein Engineering 1996, vol. 9, p. 531-537).
Plückthun, A., et al., “New protein engineering approaches to multivalent and bispecific antibody fragments”,Immunotechnology 3(1997) 83-105.
Terskikh, A.V., et al., ““Peptabody”: A new type of high avidity binding protein”,Proc. Natl. Acad. Sci. USA, Biochemistry, Mar. 1997, vol. 94, pp. 1663-1668.
Efimov, V.P., et al., “The thrombospondin-like chains of cartilage oligomeric matrix protein are assembled by a five-stranded α-helical bundle between residues 20 and 83”,FEBS Letters 341(1994) 54-58.
Hudson, P.J., et al., “High avidity scFv multimers; diabodies and triabodies”,Journal of Immunological Methods 231(1999) 177-189.
Kaminski, M.J., et al., “The Role of Homophilic Binding in Anti-tumor Antibody R24 Recognition of Molecular Surfaces”,The Journal of Biological Chemistry, vol. 274, No. 9, Issue of Feb. 26, 1999, pp. 5597-5604.
Soltyk, A,M., et al., A Mutational Analysis of the Glogotriaosylceramide-binding Sites of Verotoxin VT1,The Journal of Biological Chemistry, vol. 277, No. 7, Issue of Feb. 15, 2002, pp. 5351-5359 .
Yang, W., et al., “CDR Walking Mutagenesis for the Affinity Maturation of a Potent Human Anti-HIV-1 Antibody into the Picomolar Range”,J. Mol. Biol.(1995) 254, 392-403.
Schier, R., et al., “Isolation o Picomolar Affinity Anti-c-erbB-2 Single-chain Fv by Molecular Evolution of the Complementarity Determining Regions in the Center of the Antibody Binding Site”,J. Mol. Biol.(1996) 263, 551-567.
Ohlin, M., et al., “Light Chain Shuffling of a High Affinity Antibody results in a Drift in Epitope Recognition”,Molecular Immunology, 1996, vol. 33, No. 1., pp. 47-56.
McCafferty, J., et al., “Phage antibodies: filamentous phage displaying antibody variable domains”,Nature, vol. 348, Dec. 6, 1990, pp. 552-554.
Griffiths, A.D., et al., “Isolation of high affinity human antibodies directly from large synthetic repertoires”,The EMBO Journal, 1994, vol. 13, No. 14, pp. 3245-3260.
Hoogenboom, H.R., et al., “Natural and designer binding sites made by phage display technology”,Immunology Today, Aug. 2000, vol. 21, No. 8, 371-378.
Tanha, J., et al., “Selection by phage display of llama conventional VHfragments with heavy chain antibody VHH properties”,Journal of Immunological Methods 263(2002) 97-109.
Ling, H., et al., “Structure of the Shiga-like Toxin I B-Pentamer Complexed with an Analogue of Its Receptor Gb3”,Biochemistry1998, 37, 1777-1788.
Sambrook, J., et al.,Molecular Cloning—A Laboratory Manual, vol. 3, Third Edition.
Skerra A., et al., “The Functional Expression of Antibody FvFragments inEscherichia coli: Improved Vectors and a Generally Applicable Purification Technique”,Biotechnology, vol. 9, Mar. 1991, 273-278.
Willuda, J., et al., “High Thermal Stability is Essential for Tumor Targeting of Antibody Fragments: Engineering of a Humanized Anti-epithelial Glycoprotein-2 (Epithelial Cell Adhesion Molecule) Single-Chain Fv Fragment”,Cancer Research 59, 5758-5767, Nov. 15, 1999.
Tanha, J., et al., “Optimal Design Features of Camelized Human Single-domain Antibody Libraries”,The Journal of Biological Chemistry, vol. 276, No. 27, Issue of Jul. 6, 2001, pp. 24774-24780.
Kitov, P.I., et al., “Shiga-Like toxins are neutralized by tailored multivalent carbohydrate ligands”,Nature, vol. 403, Feb. 10, 2000, 669-672.
Facchini et al., Experimental Cell Research 269:117-129 (2001).

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