Modified virus comprising one or more non-native polypeptides

Details Modified virus comprising one or more non-native polypeptides Modified virus comprising one or more non-native polypeptides

2001-07-19

2008-11-25

Mosher, Mary E (Department: 1648)

Chemistry: molecular biology and microbiology

Virus or bacteriophage, except for viral vector or...

C435S239000, C435S325000, C435S320100, C424S093200, C424S199100, C424S233100

Reexamination Certificate

active

07456008

ABSTRACT:
A modified virus including one or more non-native polypeptides, and the use of such viruses in therapy, particularly in the treatment of tumours or other cancerous cells are disclosed. The polypeptides includes one or more framework moieties each containing one or more binding moieties, and is capable of being expressed in the cytoplasm and nucleus of a mammalian host cell in a conformation which is maintained in the absence of a ligand for the binding moieties. The conformation allows the binding moieties subsequently to bind with the ligand, and the polypeptide is capable of transport through the nuclear membrane, wherein the modified virus has an altered tropism conferred by the binding moieties.

REFERENCES:
patent: 5846782 (1998-12-01), Wickham et al.
patent: 6057155 (2000-05-01), Wickham et al.
patent: WO 94/10323 (1994-05-01), None
patent: WO 95/19374 (1995-07-01), None
patent: WO 97/20051 (1997-06-01), None
patent: WO 99/41359 (1999-08-01), None
patent: WO 00/15823 (2000-03-01), None
patent: WO 00/12738 (2000-09-01), None
patent: WO 01/02431 (2001-11-01), None
Harvey et al., “Variability of Human Systemic Humoral Immune Responses to Adenovirus Gene Transfer Vectors Administered to Different Organs,” Journal of Virology., Aug. 1999, pp. 6729-6742.
Hoppe et al., “A parallel three stranded alpha helical bundle at the nucleation site of collagen triple-helix formation,” 1994 Federation of European Biochemical Societies, Letters 344; pp. 191-195.
Nord et al., “A combinatorial library of an alpha-helical baterial receptor domain,” Protein Eng. Jun. 1995;8(6):601-8.
Henry et al., “Characterization of the Knob Domain of the Adenovirus Type 5 Fiber Protein Expressed in theEscherichia coli,” Journal of Virology, vol. 68, No. 8, pp. 5239-5246 (1994).
Xu et al., “Altered Tropism of an Ovine Adenovirus Carrying the Fiber PRotein Cell Binding Domain of Human Adenovirus Type 5,” Virology, 248, pp. 156-163 (1998).
Semple et al (Cancer Research 38:1345-1355, 1978).
Hans-Jurgen Hoppe, et al.; A Parallel three stranded a-helical bundle at the nucleation site of collagen triple-helix formation; 1994 Federation of European Biochemical Societies; XP-001061804; pp. 191-195.
TJ Wickham “Millennium Review Targeting adenovirus”; Gene Therapy 2000; XP001055892; pp. 110-114.
Maria K. Magnusson, et al.; “Genetic Retargeting of Adenovirus: Novel Strategy Employing ‘Deknobbing’ of Fiber”; Journal of Virology, Aug. 2001; pp. 7280-7289; XP-001056142.
Si Michael, et al.; “Addition of a short peptide ligand to the adenovirus fiber protein”; Gene Therapy 1995; pp. 660-668.
Marie-Laure Boudin et al.; “Assembly of Adenovirus Penton Base and Fiber”; Virology 116, pp. 589-604 (1982).
Jozef Hanes, et al.; “In vitro selection and evolution of functional proteins by using ribosome display”; Proc. Natl. Acad. Sci. USA; Vol. 94; pp. 4937-4942, May 1997.
Richard W. Roberts, et al.; “RNA-peptide fusions for the in vitro selection of peptides and proteins”; Proc. Natl. Acad. Sci. USA; vol. 94, pp. 12297-12302; Nov. 1997.
Karin Nord, et al.; “A cominatorial library of an a-helical baterial receptor domain”; Protein Engineering; vol. 8, No. 6; pp. 601-608, 1995.
Thomas J. Wickham, et al.; “Targeted Adenovirus Gene Transfer to Endothelial and Smooth Muscle Cells by Using Bispecfic Antibodies”; Journal of Virology, Oct. 1996; pp. 6831-6838.
Nobuhide Doi, et al.; “Stable: protein-DNA fusion system for screening of combinatorial protein libraries in vitro”; FEBS Letters 457 (1999); pp. 227-230.
Anke Krebber, et al.; “Reliable cloning of functional antibody variable domains from hybridomas and spleen cell repertoires employing a reengineered phage display system”; Journal of Immunological Methods 201 (1997) pp. 35-55.
R. Miller, et al.; “Editorial: Towards the use of replicative adenoviral vectors for cancer gene therapy”; Gene Therapy (1996); pp. 557-559.
C. Chartier, et al.; “Efficient Generation of Recombinant Adenovirus Vectors by Homologous Recombination inEscherichia coli”; Journal of Virology, Jul. 1996, pp. 4805-4810.
Karl Proba, et al.; “Antibody scFv Fragments Without Disulfide Bonds Made by Molecular Evolution”; J. Mol. Biol. (1998); pp. 245-253.
Ying Tang, et al.; “Selection of Linkers for a Catalytic Single-chain Antibody Using Phage Display Technology”; The Journal of Biological Chemistry; vol. 271, No. 26, Issue of Jun. 28, pp. 15682-15686, 1996.
Alvano, et al.; “PCR-Ligation-PCR Mutagenesis: A Protocol for Creating Gene Fusions and Mutations”; Benchmarks; vol. 18; No. 5; 1995; pp. 746-752.
“Discussion and Preliminary Reports”; pp. 782-783, date not available.
Paul A. Kitts, et al.; “A Method for Producing Recombinant Baculovirus Expression Vectors at High Frequency”; Research Report; vol. 14, No. 5 (1993); pp. 810-817.
Robert McArn Horton, et al.; “Recombination and mutagenesis of DNA sequences using PCR”; R.M. Horton and L.R. Pease; pp. 217-247, date not available.
Pierre Martineau, et al.; “In vitro Folding and Thermodynamic Stablility of an Antibody Fragment Selected in Vivo for High Expression Levels inEscherichia coliCytoplasm”; 1999 Academic Press; Article No. jmbi. 1999.3105; J.Mol. Biol. 1999; pp. 292, 921-929.
Bruce C. Trapnell, et al.; “Gene Therapy using adenoviral vectors” Current Biology Ltd ISSN 0958-1669; PP. 617-625, date not available.
Anotonio Cattaneo, et al.; “The selection of intracellular antibodies”; Tibtech Mar. 1999 (vol. 17); pp. 115-121.
Silvia Biocca, et al.; “Redox State of Single Chain FV Fragments Targeted to the Endoplasmic Reticulum, Cytosol and Mitochondria”; Bio/Technology vol. 13; Oct. 1995; pp. 1110-1115.
Stephen C. Emery, et al.; “Strategies for Humanizing Antibodies”; Antibody Engineering; Chapter 6; pp. 159-183, date not availabe.
Per-Ake Nygren, et al.; “Scaffolds for engineering novel binding sites in proteins”; Current Opinion in Structural Biology 1997, pp. 463-469.
Philip A. Walker, et al.; “Efficient and Rapid Affinity Purification of Proteins Using Recombinant Fusion Proteases”; Bio/Technology, vol. 12 Jun. 1994; pp. 601-605.
Marianne Hansson, et al.; “An in vitro selected vinding protein (affibody) shows conformation-dependent recognition of the respiratory syncytial virus (RSV) G protein”; Immunotechnology 4 (1999); pp. 237-252.
Igor Dmitriev, et al.; “An Adenovirus Vector with Genetically Modified Fibers Demonstrates Expanded Tropism via Utilization of a Coxsackievirus and Adenovirus Receptor-Independent Cell Entry Mechanism”; Journal of Virology, Dec. 1998, pp. 9706-9713.
Nicola Gargano, et al.; “Rescue of a Neutralizing anti-viral antibody fragment from an intracellular polyclonal repertoire expressed in mammalian cells”; FEBS Letters 414, 1997; pp. 537-540.
Bjorn Nilsson, et al.; “A synthetic IgG-binding domain based on staphylococcal protein A”; Protein Engineering; vol. 1, No. 2, 1987; pp. 107-113.
James M. Clark; “Novel non-templated necleotide addition reactions catalyzed by procaryotic and eucaryotic DNA polymerases”; Nucleic Acids Research; vol. 16, No. 20, 1988.
Tim Clakson, et al.; “General applications of PCR to gene cloning and manipulation”; pp. 187-214, date not available.
Carolyn Cohen, et al.; “a-Helical Coiled Coils: More Facts and Better Predictions”; Science, vol. 263; Jan. 28, 1994; pp. 488-489.
George Smith, et al.; “Libraries of Peptides and Proteins Displayed on Filamentous Phage”; Method in Enzymology, vol. 217; pp. 228-259, date not available.
Jacqueline L. Harrisson, et al.; “Screening of Phage Antibody Libraries”; Methods in Enzymology; vol. 267; pp. 83-109, date not available.
Eli

Affiliated with

Also associated with

Rating

Modified virus comprising one or more non-native polypeptides does not yet have a rating. At this time, there are no reviews or comments for this patent.

If you have personal experience with Modified virus comprising one or more non-native polypeptides, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Modified virus comprising one or more non-native polypeptides will most certainly appreciate the feedback.

Rate now

Comments { 0 }

Profile ID: LFUS-PAI-O-4030580