Chemistry: molecular biology and microbiology – Measuring or testing process involving enzymes or... – Involving nucleic acid
Reexamination Certificate
2006-01-10
2006-01-10
Fredman, Jeffrey (Department: 1637)
Chemistry: molecular biology and microbiology
Measuring or testing process involving enzymes or...
Involving nucleic acid
C435S069700, C435S068100, C435S069100, C435S070100, C435S071100, C530S300000, C530S317000, C536S023100, C536S025300, C536S023400, C536S023530
Reexamination Certificate
active
06984488
ABSTRACT:
Methods of using overlapping peptides for the discovery of discontinuous epitopes, as vaccines, for drug design, for diagnostic purposes and for the elucidation of three-dimensional protein structure. Specifically, these methods can be used to map conformational epitopes using overlapping peptides. The methods are both complete, yet more specific than random phage libraries. They can also be used to develop DNA vaccines which exploit the concept of overlapping peptides in a variety of expression systems. Conformational epitopes prepared with these methods can be used for preparing antibodies, as components of diagnostic tools, and for elucidating three-dimensional protein structure.
REFERENCES:
patent: 5691170 (1997-11-01), Gritz et al.
patent: 5811238 (1998-09-01), Stemmer et al.
patent: 6031071 (2000-02-01), Mandeville et al.
patent: WO 98/05764 (1998-02-01), None
Huse et al “Generation of a large combinatorial library of the immunoglobulin repertoire in pahge lambda” Science, Dec. 8, 1989, 246: 1275-1281.
Marks et al “Molecular evolution of proteins on filamentous phage” The Journal of Biological Chemistry, Aug. 15, 1992, 267(23): 16007-16010.
Wang et al, “Use of a Gene-Targeted Phage Display Random Epitome Library to Map an Antigenic Determinant on the Bluetongue Virus Outer Caspid Protein VP5”,J. Immun. Methods,178: 1-12, 1995.
Ulmer et al, “DNA Vaccines”,Curr. Opin. Immun.,8: 531-536, 1996.
Ulmer et al, “ELI's Coming: Expression Library Immunization and Vaccine Antigen Discovery”,Trends in Microbiology,4(5): 169-170, 1996.
Pasqualini et al, “Organ Targetingin vivoUsing Phage Display Peptide Libraries”,Nature, 380364-366, 1996.
Willis et al, “Immunological Properties of Foreign Peptides in Multiple Display on a Filamentous Bacteriophage”,Gene,128: 79-83, 1993.
Cortese et al, “Epitope Discovery Using Peptide Libraries Displayed on Phage”,TIBTECH,12:262-266, 1994.
Lane et al, “Epitope Mapping Using Bacteriophage Peptide Libraries”,Curr. Opin. Immun.,5: 268-271, 1993.
Baughn et al, “Epitope Mapping of B-Cell Determinants on the 15-Kilodalton Lipoprotein ofTreponema Pallidum(Tpp15) with Synthetic Peptides”,Infection and Immunity,64(7): 2457-2466, 1996.
Dybwad et al, “Identification of New B Cell Epitopes in the Sera of Rheumatoid Arthritis Patients Using a Random Nanopeptide Phage Library”,Eur. J. Immunol.,23: 3189-3193, 1993.
Dybwad et al, “Structural Characterization of Peptides that Bind Synovial Fluid Antibodies from RA Patients: A Novel Strategy for Identification of Disease-Related Epitopes Using a Random Peptide Library”,Clin. Immunol. And Immunopathol.;75(1): 45-50, 1995.
Folgori et al, A General Strategy to Identify Mimotopes of Pathological Antigens Using Only Random Peptide Libraries and Human Sera,The EMBO Journal,13(9): 2236-2243, 1994.
Felici et al, “Selection of Antobody Ligands from a Large Library of Oligopeptides Expressed on a Multivalent Exposition Vector”,J. Moi. Biol.,222: 301-310, 1991.
Mougneau et al, “Expression Cloning of a ProtectiveLeishmaniaAntigen”,Science,268: 563-566, 1995.
Ho et al, “Discontinuous Epitopes on gp120 Important in HIV-1 Neutralization”,Aids Research and Human Retroviruses,8(8): 1337-1339, 1992.
Thali et al, “Characterization of a Discontinuous Human Immunodeficiency Type 1 gp 120 Epitope Recognized by a Broadly Reactive Neutralizing Human Monoclonal Antibody”,J. Virology,pp 6188-6193, 1991.
Oravecz et al, “β-Chemokine Inhibition of Monocytropic HIV-1 Infection”,J. Immunol.,157: 1329-1332, 1996.
Ho et al, “Conformational Epitope on gp 120 Important in CD4 Binding and Human Immunodeficiency Virus Type 1 Neutralization Identified by a Human Monoclonal Antibody”,J. Virology,pp 489-493, 1991.
Bachelder et al, Postbinding Functions of CD4 in HIV Infection,Trends in Microbiology,4(9): 359-363, 1996.
Ho et al, “Another Discontinuous Epitope on glycoprotein gp120 that is Important in Human Immunodeficiency Virus Type 1 Neutralization is Identified by a Monoclonal Antibody”,Proc. Natl. Acad. Sci. USA,88: 8949-8952, 1991.
Thali et al, “Discontinuous, Conserved Neutralization Epitopes Overlapping the CD4-Binding Region of Human Immunodeficiency Virus Type 1gp120 Envelope Glycoprotein”,J. Virology,pp 5635-5641, 1992.
Stemmer, WPC, “Rapid Evolution of a Proteinin vitroby DNA Shuffling”,Nature,p389, 1994.
Matsumura et al, “DNA Shuffling Brightens Prospects for GFP”,Nature Biotechnol.,14: 366, 1996.
Crameri et al, “Improved Green Fluorescent Protein by Molecular Evolution Using DNA Shuffling”,Nature Biotechnol.,14: 313, 1996.
Cortese et al, “Identification of Biologically Active Peptides Using Random Libraries Displayed on Phage”,Curr. Opinion in Biotechnol.6: 73-80, 1995.
Oldenburg et al, “Peptide Ligands for a Sugar-Binding Protein Isolated from a Random Peptide Library”,Proc. Natl. Acad. Sci. USA,89: 5393-5397, 1992.
Scott et al, A Family of Concanavalin A-Binding Peptides from a Hexapeptide Epitope Library,Proc. Natl. Acad. Sci. USA,89: 5398-5402, 1992.
Hoess et al, “Identification of a Peptide Which Binds to the Carbohydrate-Specific Monoclonal Antibody”,Gene,128: 43-49, 1993.
Greenwood et al, “Multiple Display of Foreign Peptides on a Filamentos Bacteriophage”, J. Mol. Biol. 320: 821-827, 1991.
Falt et al, “Epitope Mapping of Six Monoclonal Antibodies Recognizing theShigella DysenteriaeType O-Antigenic Repeating Unit Expressed inEscherichia ColiK-12”,Microbial. Pathenogenesis,16: 27-41, 1994.
Sioud et al, Characterization of Naturally Occurring Autoantibodies Against Tumoour Necrosis Factor-Alpha (TNF-α:in vitroFunction and Precise Epitope Mapping by Phage Epitope Library,Clin. Exp. Immunol.,98: 520-525, 1994.
Gao et al, “Multiple Interactive Residues of Recognition”,J. Immunol.,157: 183-188, 1996.
Launois et al, “T-Cell—Epitope Mapping of the Major Secreted Mycobacterial Antigen Ag85A in Tuberculosis and Leprosy”,Infection and Immunity,pp. 2679-3687, 1994.
Putkonen et al, “Prevention of HIV-2 and SIVsmInfection by Passive Immunization in Cynomolgus Monkeys”, Nature, 253: 436-437, 1991.
de la Cruz et al, “Immunogenicity and Epitope Mapping of Foreign Sequences via Genetically Engineered Filamentous Phage”,J. Biological Chem.263(9): 4318-4322, 1988.
Luzzaga et al, “Mimicking of Discontinuous Epitopes by Phage-Displayed Peptides, I. Epitope Mapping of Human H Ferritin Using a Phage Library of Constrained Peptides”, Gene, 1993, pp 51-57.
Maliszewski et al, “The CD39 Lymphoid Cell Activation Antigen”,J. Immunol.,153:3574-3583, 1994.
Graf et al, “Random circular permutation of genes and expressed polypeptide chains: application of the method to the catalytic chains of aspartate transcarbamoylase”,Proc Natl Acad Sci USA93(21):11591-11596 (1996).
Nagesha et al, “Application of linker-ligation-PCR for construction of phage display epitope libraries”,J Virol Methods60(2):147-154 (1996).
Crameri et al, “Display of expression products of cDNA libraries on phage surfaces. A versatile screening system for selective isolation of genes by specific gene-product/ligand interaction”,Eur J Biochem226(1):53-68 (1994).
Du Plessis et al, “Identification of an antigenic peptide specific for bluetongue virus using phage display expression of NS1 sequences,”Immunotechnology1(3-4):221-230 (1995).
Jacobsson et al, “Cloning of ligand-binding domains of bacterial receptors by phage display”,Biotechniques18(5):878-885 (1995).
Jacobsson et al, “Phage display shot-gun cloning of ligand-binding domains of prokaryotic receptors approaches 100% correct clones”,Biotechniques20(6): 1070-1076, 1078, 1080-108
Enshel David
Gershoni Jonathan M.
Browdy and Neimark PLLC
Fredman Jeffrey
Ramot at Tel-Aviv University Ltd.
LandOfFree
Determination and control of bimolecular interactions does not yet have a rating. At this time, there are no reviews or comments for this patent.
If you have personal experience with Determination and control of bimolecular interactions, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Determination and control of bimolecular interactions will most certainly appreciate the feedback.
Profile ID: LFUS-PAI-O-3530076