Bacteriophage displaying aβ epitopes and method of use

Details Bacteriophage displaying aβ epitopes and method of use Bacteriophage displaying aβ epitopes and method of use

2005-07-19

2005-07-19

Kemmerer, Elizabeth C. (Department: 1647)

Drug, bio-affecting and body treating compositions

Whole live micro-organism, cell, or virus containing

Genetically modified micro-organism, cell, or virus

C424S093600, C435S320100

Reexamination Certificate

active

06919075

ABSTRACT:
A method of immunizing against plaque forming diseases using display technology is provided. The method utilize novel agents, or pharmaceutical compositions for vaccination against plaque forming diseases which rely upon presentation of an antigen or epitope on a display vehicle. The method further includes agents, or pharmaceutical compositions for vaccination against plaque forming diseases, which rely upon presentation of an antibody, or an active portion thereof, on a display vehicle. Whether antigens or antibodies are employed, disaggregation of plaques results from the immunization.

REFERENCES:
patent: 5811093 (1998-09-01), Merril et al.
patent: 6703015 (2004-03-01), Solomon et al.
patent: 2002/0052311 (2002-05-01), Solomon et al.
patent: 2004/0013647 (2004-01-01), Solomon et al.
patent: WO 92/07077 (1992-04-01), None
Skolnick & Fetrow (2000) “From genes to protein structure and function: novel applications of computational approaches in the genomic era.” Trends in Biotech. 18(1): 34-39.
Jobling & Holmes (1991) “Analysis of structure and function of the B Subunit of cholera toxin by the use of site-directed mutagenesis.” Molecular Microbiology 5(7): 1755-67.
Goldsby et al. (2002) Kuby Immunology Chapter 18 “Vaccines” (pp. 449-465).
Tobin & Signer (Dec. 2000) “Huntington's disease: the challenge for cell biologists.” Trends in Cell Biology 10(12): 531-536.
Su et al. (Feb. 6, 1999) “Intravascular infusions of soluble b-amyloid compromise the blood-brain barrier, activate CNS glia cells and induce peripheral hemorrhage.” Brain Research 818(1): 105-117.
Goldfarb and Brown (1995) “The Transmissible Spongiform Encephalopathies.” Annu. Rev. Med. 46: 57-66.
Kovács et al. (2002) “Mutations of the Prion Protein Gene.” J. Neurol. 249: 1567-1582.
Elan Press Releases (Jan. 18, 2002 and Mar. 1, 2002).
Singh (1997) “Neuroautoimmunity: Pathologic Implications for Alzheimer's Disease.” Gerontology 43:79-94.
Castillo et al. (1995) “Amylin/Islet Amyloid Polypeptide: Biochemistry, Physiology, Patho-Physiology.” Diabete et Metbolisme 213-25.
Frenkel et al. (1998) “N-terminal EFRH sequence of Alzheimer's b-amyloid peptide represents the epiptope of its anti-aggregating antibodies.” Journal of Neuroimmunology 88: 85-90.
Smith, “Surface presentation of protein epitopes using bacteriophage expression systems”,Current Opinion in Biotechnology,2:668-673 (1991).
Renauld-Mongenie et al., “Induction of mucosal immune responses against a heterologous antigen fused to filamentous hemagglutinin after intranasal immunization with recombinantBordetella pertussis”, Proc. Natl. Acad. Sci. USA,93:7944-7949 (1996).
Cesareni et al., “Minireview Peptides display on filamentous phage capsids a new powerful tool to study protein ligand interaction”,FEBS Letters,307:66-70 (1992).
Huse et al., “Application of a filamentous phage pVIII fusion protein system suitable for efficient production screening, and mutagenesis of F(ab) antibody fragments”,The Journal of Immunology, (1992).
Jones et al., “Display of antibody chains on filamentous bacteriophage”,Methods in Molecular Biology,80:449-459, (1998).
Chang et al., “Expression of antibody Fab domains on bacteriophage surfaces potential use for antibody selection”,Journal of Immunology,147:3610-3614 (1991).
Glaser et al., “Antibody engineering by codon-based mutagenesis in a filamentous phage vector system”,The Journal of Immunology,149:3903-3913 (1992).
Hoogenboom et al., “Building antibodies from their genes”,Immunological Reviews,130-41-68 (1992).
Barbas et al., “Semisynthetic combinatorial antibody libraries: a chemical solution to the diversity problem”,Natl. Acad. Sci. USA, 4457:4461 (1992).
Marks et al., “Molecular evolution of proteins on filamentous phage”,The Journal of Biological Chemistry,267:16007-16010 (1992).
Hawkins et al., “Selection of phage antibodies by binding affinity mimicking affinity maturation”,J. Mol. Biol.,226:889-896 (1992).
Wetzel, “Commentary learning from the immune system laboratory methods for creating and refining molecular diversity in polypeptides”,Protein Engineering, 4:371-374 (1991).
Lerner et al., “Antibodies without immunization”,Science, 258:1313-1314 (1992).
Barbas et al., “Recombinant human Fab fragments neutralize human type 1 immunodeficiency virus in vitro”,Proc. Natl. Acad. Sci. USA, 89:9339-9343 (1992).
Zebedee et al., “Human combinatorial antibody libraries to hepatitis B surface antigen”,Proc. Natl. Acad. Sci. USA, 89:3175-3179 (1992).
Gram et al., “In vitro selection and affinity maturation of antibodies from a naïve combinatorial immunoglobulin library”,Proc. Natl. Acad. Sci. USA, 89:3576-3580 (1992).
Kang et al., “Antibody redesign by chain shuffling from random combinatorial immunoglobulin libraries”,Proc. Natl. Acad. Sci. USA, 88:11120-11123 (1991).
Garrard et al., “Assembly and enrichment in a monovalent phage display system”,Biotechnology, 9:1373-1377 (1991).
Goessling et al., “Enhanced degradation of the ferritin repressor protein during induction of ferritin messenger RNA translation”,Science, 256:670 (1992).
Marks et al., “By-passing immunization human antibodies from V-gene libraries displayed on phage”,J. Mol. Biol.,222:581-597 (1991).
Clackson et al., “Letters to nature making antibody fragments using phage display libraries”,Nature, 352:624-628 (1991).
Barbas et al., “Assembly of combinatorial antibody libraries on phage surfaces: The gene III site”,Proc. Natl. Acad. Sci. USA, 88:7978-7982 (1991).
McCafferty et al., “Letters to nature phage antibodies: filamentous phage displaying antibody variable domains”,Nature, 348:552-554 (1990).
Kang et al., “Linkage of recognition and replication functions by assembling combinatorial antibody Fab libraries along phage surfaces”,Proc. Natl. Acad. Sci. USA, 88:4363-4366 (1991).
Burtion et al., “A large array of human monoclonal antibodies to type 1 human immunodeficiency virus from combinatorial libraries of asymptomatic seropositive individuals”,Proc. Natl. Acad. Sci. USA, 88:10134-10137 (1991).
Breitling et al., “Ad surface expression vector for antibody screening”,Gene, 104:147-153 (1991).
Hoogenboom et al., “Multi-subunit proteins on the surface of filamentous phage: methodologies for displaying antibody (Fab) heavy and light chains”,Nucleic Acids Research, 19:4133-4137 (1991).
Barbas et al., “Human monoclonal Fab fragments derived from a combinatorial library bind to respiratory syncytial virus F glycoprotein and neutralize infectivity”,Proc. Natl. Acad. Sci. USA, 89:10164-10168 (1992).
Somerville et al., “Immunodetection of PrPSCin spleens of some scrapie-infected sheep but not BSE-infected cows”,Journal of General Virology,7:2389-2396 (1997).
Frenkel et al., “N-terminal EFRH sequence of Alzheimer's β-amyloid peptide represents the epitope of its anti-aggregating antibodies”,Journal of Neroimmunology,88:85-90 (1998).
Schenk et al., “Letters of nature immunization with amyloid-β attenuates Alzheimer-disease-like pathology in the PDDAPP mouse”,Nature,400:173-177 (1999).
Solomon et al., “Monoclonal antibodies inhibit in vitro fibrillar aggregation of the Alzheimer β-amyloid peptide”,Proc. Natl. Acad. Sci. USA,93:452-455 (1996).
Solomon et al., “Disaggregation of Alzheimer β-amyloid by site-directed mAb”,Proc. Natl. Acad. Sci. USA.94:4109-4112 (1997).
Motti et al., “Recognition by human sera and immunogenicity of HbsAg mimotopes selected from an M13 phage display library”,Gene, 146:191-198 (1994).
Hanan et al.,

Affiliated with

Also associated with

Rating

Bacteriophage displaying aβ epitopes and method of use does not yet have a rating. At this time, there are no reviews or comments for this patent.

If you have personal experience with Bacteriophage displaying aβ epitopes and method of use, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Bacteriophage displaying aβ epitopes and method of use will most certainly appreciate the feedback.

Rate now

Comments { 0 }

Profile ID: LFUS-PAI-O-3408703