Drug – bio-affecting and body treating compositions – In vivo diagnosis or in vivo testing
Reexamination Certificate
2006-05-30
2006-05-30
Swartz, Rodney P (Department: 1645)
Drug, bio-affecting and body treating compositions
In vivo diagnosis or in vivo testing
C424S009200, C424S130100, C424S147100, C435S007100, C435S070100, C435S071100, C436S503000, C436S518000, C436S547000
Reexamination Certificate
active
07052675
ABSTRACT:
Antibodies are disclosed which specifically bind to native PrPScin situ. Preferred antibodies bind only to the native PrPScof a particular species e.g., human, cow, sheep, pig, etc. Particularly preferred antibodies bind specifically to a particular isoform of human PrPSc. Preferred antibodies of the invention are (1) produced by phage display methodology, (2) bind specifically to native PrPSc, (3) neutralizes the infectivity of prions, (4) bind to PrPScin situ and (5) bind 50% or more of PrPScin a liquid flowable sample. Antibodies of the invention can be bound to a substrate and used to assay a sample (which has any PrPcdenatured via proteinase K) for the presence of PrPScof a specific species which PrPScis associated with disease. Antibodies which specifically bind to human PrPSccan be labeled and injected carrying out an in vivo diagnostic test to determine if the human is infected with prions associated with disease. The antibodies are preferably produced using phage display technology wherein the genetic material in the phage expressing the antibody is obtained from a mammal with an ablated endogenous PrP protein gene and an endogenous chimeric PrP gene which mammal had been inoculated with PrPScto induce antibody production.
REFERENCES:
patent: 4806627 (1989-02-01), Wisniewski et al.
patent: 4816567 (1989-03-01), Cabilly et al.
patent: 5223409 (1993-06-01), Ladner et al.
patent: 6290954 (2001-09-01), Prusiner et al.
patent: WO 90/04036 (1990-04-01), None
patent: WO 93/23432 (1993-11-01), None
patent: WO 93/10227 (1995-05-01), None
patent: WO 99/66956 (1999-12-01), None
patent: WO 00/26238 (2000-05-01), None
patent: WO 01/05426 (2001-01-01), None
patent: WO 01/07479 (2001-02-01), None
Barbas et al., “Assembly of Combinatorial Antibody Libraries on Phage Surfaces: the Gene III Site,”Proc. Natl. Acad. Sci. (1991) 88: 7978-82.
Barry, R.A., et al., “Monoclonal Antibodies to the Cellular and Scrapie Prion Proteins,”Journal of Infectious Diseases(1986) 154:518-521.
Basler et al., “Scrapie and Cellular PrP Isoforms Are Encoded by the Same Chromosomal Gene,”Cell, (1986) 46: 417-28.
Bendheim et al., “Scrapie and Creutzfeldt-Jacob Disease Prion Proteins Share Physical Properties and Antigenic Determinants.”Proc. Natl. Acad. Sci. USA(1985) 82:997-1001.
Bobrzecka et al., “The Method of Controlled Rearrangement of Protein Disulphides and Its Use for Synthesis of Chimeric Immunoglobulin G,”Immunology Letters(1980) 2: 151-5.
Bode et al., “Characterization of Antisera Against Scrapie-Associated Fibrils (SAF) from Affected Hamsler and Cross-Reactivity with SAF from Scrapie-Affected Mice and from Patients with Creutzfeldt-Jacob Disease,”J. Gen. Virol. (1985) 66(pt 11):2471-8.
Bolton et al., “Identification of a Protein That Purifies with the Scrapie Prion,”Science(1982) 218: 1309-11.
Brown et al., “Diagnosis of Creutzfeldt-Jacob disease by western blot identification of marker protein in human brain tissue,”New Engl. J. Med. (1986) 314:547-51.
Brown et al., “Friendly Fire' in Medicine: Hormones, Homografts, and Creutzfeldt-Jakob Disease,”Lancet(1992) 340:24-27.
Bruce, et al., “Biological Evidence that Scrapie Agent Has an Independent Genome,”J. Gen. Virol. (1987) 68:79-89.
Buchanan et al., “Mortality, Neoplasia, and Creutzfeldt-Jakob Disease in Patients Treated with Human Pituitary Growth Hormone in the United Kingdom”,BMJ(1991) 302:824-828.
Bucchine et al., “Rearrangement of a chicken Immunoglobulin Gene Occurs in the Lymphoid Lineage of a Transgenic Mouse,”Nature(1987) 326: 409-11.
Bueler et al., “Mice Devoid of PrP are Resistant to Scrapie,”Cell(1993) 73:1339-1347.
Bueler et al., “Normal Development and Behavior of Mice Lacking the Neuronal Cell-surface PrP Protein,”Nature(1992) 356:577-582.
Burton, D.R. 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(1991) 88: 10134-7.
Burton and Barbas, “Human Antibodies from Combinatorial Libraries,”Adv. Immunol. (1994) 57: 191-280.
Cann et al., “Antibody fragments to PrP generated using phage display technology,”J. Cell Bichem. Supplement(1994) 18D:T304.
Carlson, G.A., et al., “Prion Isolates Specified Allotypic Interactions Between the Cellular and Scrapie Prion Proteins in Congenic and Transgenic Mice,”Proc. Natl. Acad. Sci. USA(1994) 91:5690-4.
Clackson, T., et al., “Making Antibody Fragments Using Phage Display Libraries,”Nature(1991) 352: 624-8.
Cochius et al., “Creutzfeldt-Jakob Disease in a Recipient of Human Pituitary-Derived Gonadotrophin: A Second Case,”J. Neurol. Neurosurg. Psychiatry(1992) 55:1094-1095.
Cochius et al., “Creutzfeldt-Jakob Disease in a Recipient of Human Pituitary-Derived Gonadotrophin,”Aust. N.Z. J. Med. (1990) 20:592-593.
Collinge et al., “Genetic Predisposition to Latrogenic Creutzfeldt-Jakob Disease,”Lancet(1991) 337:1441-1442.
Ditzel, J., et al., “Neutralizing Recombinany Human Antibodies to a Confromaitonal V2- and CD4-binding Site-Sensitive Epitope of HIV-1 gp120 Isolated by Using an Epitope-Masking Procedure.”J. Immunol. (1995) 154: 893-906.
Gabizon et al., “Immunoaffinity purifiction and neutralization of scrapie prion infectivity,”Proc. Natl. Acad. Sci. USA(1988) 85:6617-6621.
Gabriel et al., “Molecular Cloning of a Candidate Chicken Prion Protein,”Proc. Natl. Acad. Sci. USA(1992) 89:9097-9101.
Gajdusek, D.C., “Unconventional Viruses and the Origin and Disappearance of Kuru,”Science(1977) 197:943-960.
Gibbs, Jr. et al., “Creutzfeldt-Jakob Disease Infectivity of Growth Hormone Derived from Human Pituitary Glands,”N. Engl. J. Med. (1993) 328:358-359.
Goldfarb et al., “Fatal Familial Insomnia and Familial Creutzfeldt-Jakob Disease: Disease Phenotype Determined by a DNA Polymorphism,”Science(1992) 258:806-808.
Goldmann et al., “Two Alleles of a Neural Protein Gene Linked to Scrapie in Sheep,”Proc. Natl. Sci. USA(1990) 87:2476:2480.
Goldman et al., “Different Forms of the Bovine PrP Gene Have Five or Six Copies of a Short, G-C Rich Element within the protein-coding Exon,”J. Gen. Virol. (1991) 72:201-204.
Goodhardt, et al., “Rearrangement and Expression of Rabbit Immunoglobulin κ Light Chain Gene in Transgenic Mice,”Proc. Natl. Acad. Sci. USA(1987) 84: 4229-33.
Harris et al., “A Prion-like Protein from Chicken Brain Copurifies with an Acetylcholline Receptor-Inducing Activity,”Proc. Natl. Acad. Sci. USA(1991) 88:7664-7668.
Healy et al., “Creutzfeldt-Jakob Disease After Pituitary Gonadotrophin: The Prion is the Problem,”BMJ(1993) 307:517-518.
Hecker et al., “Replication of Distinct Scrapie Prion Isolates is Region Specific in Brains of Transgenic Mice and Hamsters,”Genes Dev. (1992) 6:1213-1228.
Horiuchi, “Interaction between Gene II Protein and the DNA Replication Origin of Bacteriophage f1,”J. Mol. Biol., (1986) 188:215-223.
Hsaio et al., “Linkage of a Prion Protein Missense Variant to Gertsmann-Straussler Syndrome,”Nature(1989) 383:342-345.
Hsaio et al., “A Prion Protein Variant in a Family with the a Telencephalic Form of Gerstmann-Strussler-Scheinker Syndrome,”Neurology(1991) 41:681-684.
Huse et al., “Generation of a Large Combinatorial Library of the Immunoglobulin Repertoire in Phage Lambda (see comments),”Science(1989) 246: 1275-81.
Kascsak, R.J., et al., “Mouse Polyclonal and Monoclonal Antibody to Scrapie-Associated Fibril Proteins”Journal of Virology(1987) 61:3688-3693.
Kellings et al., “Further Analysis of Nucleic Acids in Purified Scrapie Prion Preparation by Improved Return Refocusing Gel Electrophoresis,”J.
Burton Dennis R.
Prusiner Stanley B.
Williamson R. Anthony
Bozicevic Karl
Bozicevic Field & Francis LLP
Swartz Rodney P
The Regents of the University of California
The Scripps Research Institute
LandOfFree
Antibodies specific for native PrP Sc does not yet have a rating. At this time, there are no reviews or comments for this patent.
If you have personal experience with Antibodies specific for native PrP Sc, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Antibodies specific for native PrP Sc will most certainly appreciate the feedback.
Profile ID: LFUS-PAI-O-3539858