Abstract: Provided herein are hybrid polypeptides that specifically bind to a disease-associated isoform of a polypeptide involved in diseases of protein aggregation. The hybrid polypeptides can be used for diagnosis and treatment of such diseases. In a particular embodiment, a hybrid protein that specifically binds to the infectious form of a prion (PrPSc) is provided.

Abstract: The present invention discloses methods for generating antibodies to human metapneumovirus (HMPV) polypeptides, including antibodies that immunospecifically bind to a HMPV F-protein. The invention also discloses methods for preventing, treating, or ameliorating symptoms associated with HMPV infection.

Abstract: Provided herein are hybrid polypeptides that specifically bind to a disease-associated isoform of a polypeptide involved in diseases of protein aggregation. The hybrid polypeptides can be used for diagnosis and treatment of such diseases. In a particular embodiment, a hybrid protein that specifically binds to the infectious form of a prion (PrPSc) is provided.

Abstract: The present invention provides antibodies that specifically bind with a high degree of binding affinity to a native ungulate PrPC and/or a denatured ungulate PrPSc, but not to a native ungulate PrPSc. Preferred antibodies find native bovine PrPC and treated PrPSc but not native bovine PrPSc and can be used in an assay to determine if a sample is infected with infectious prions, i.e. PrPSc.

Abstract: The present invention provides a novel method for the identification and clonal isolation of antibodies that bind to unique epitopes. The method is based on the use of antibodies as solid phase capture reagents to bind a known capture antibody epitope, thereby precluding the capture antibody epitope from being presented to a population of antibodies to be screened. The method is particularly suited for screening libraries of cloned antibodies, such as phage display combinatorial antibodies. An antibody specific for herpes simplex virus (HSV), was employed as a model for the assay.

Abstract: Antibodies are disclosed which specifically bind to native PrPSc in situ. Preferred antibodies bind only to the native PrPSc of 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 PrPSc in situ and (5) bind 50% or more of PrPSc in a liquid flowable sample. Antibodies of the invention can be bound to a substrate and used to assay a sample (which has any PrPc denatured via proteinase K) for the presence of PrPSc of a specific species which PrPSc is associated with disease. Antibodies which specifically bind to human PrPSc can be labeled and injected carrying out an in vivo diagnostic test to determine if the human is infected with prions associated with disease.

Abstract: Antibodies are disclosed which specifically bind to native PrPSc in situ. Preferred antibodies bind only to the native PrPSc of 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 PrPSc in situ and (5) bind 50% or more of PrPSc in a liquid flowable sample. Antibodies of the invention can be bound to a substrate and used to assay a sample (which has any PrPc denatured via proteinase K) for the presence of PrPSc of a specific species which PrPSc is associated with disease. Antibodies which specifically bind to human PrPSc can be labeled and injected carrying out an in vivo diagnostic test to determine if the human is infected with prions associated with disease.

Abstract: Antibodies are disclosed which specifically bind to native PrPSc in situ. Preferred antibodies bind only to the native PrPSc of 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 PrPSc in situ and (5) bind 50% or more of PrPSc in a liquid flowable sample. Antibodies of the invention can be bound to a substrate and used to assay a sample (which has any PrPc de-natured via proteinase K) for the presence of PrPSc of a specific species which PrPSc is associated with disease. Antibodies which specifically bind to human PrPSc can be labeled and injected carrying out an in vivo diagnostic test to determine if the human is infected with prions associated with disease.

Abstract: Provided herein are hybrid polypeptides that specifically bind to a disease-associated isoform of a polypeptide involved in diseases of protein aggregation. The hybrid polypeptides can be used for diagnosis and treatment of such diseases. In a particular embodiment, a hybrid protein that specifically binds to the infectious form of a prion (PrPSc) is provided.

Abstract: The present invention provides antibodies that specifically bind with a high degree of binding affinity to a native ungulate PrPC and/or a denatured ungulate PrPSc, but not to a native ungulate PrPSc. Preferred antibodies find native bovine PrPC and treated PrPSc but not native bovine PrPSc and can be used in an assay to determine if a sample is infected with infectious prions, i.e. PrPSc.

Abstract: Antibodies are disclosed which specifically bind to native PrPSc in situ. Preferred antibodies bind only to the native PrPSc of 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 PrPSc in situ and (5) bind 50% or more of PrPSc in a liquid flowable sample. Antibodies of the invention can be bound to a substrate and used to assay a sample (which has any PrPc denatured via proteinase K) for the presence of PrPSc of a specific species which PrPSc is associated with disease. Antibodies which specifically bind to human PrPSc can be labeled and injected carrying out an in vivo diagnostic test to determine if the human is infected with prions associated with disease.

Abstract: The present invention provides antibodies that specifically bind with a high degree of binding affinity to a native ungulate PrPC and/or a denatured ungulate PrPSc, but not to a native ungulate PrPSc. Preferred antibodies find native bovine PrPC and treated PrPSc but not native bovine PrPSc and can be used in an assay to determine if a sample is infected with infectious prions, i.e. PrPSc.

Abstract: The present invention provides a novel method for the identification and clonal isolation of antibodies that bind to unique epitopes. The method is based on the use of antibodies as solid phase capture reagents to bind a known capture antibody epitope, thereby precluding the capture antibody epitope from being presented to a population of antibodies to be screened. The method is particularly suited for screening libraries of cloned antibodies, such as phage display combinatorial antibodies. An antibody specific for herpes simplex virus (HSV), was employed as a model for the assay.

Abstract: Antibodies are disclosed which specifically bind to native PrPSc in situ. Preferred antibodies bind only to the native PrPSc of 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 PrPSc in situ and (5) bind 50% or more of PrPSc in a liquid flowable sample. Antibodies of the invention can be bound to a substrate and used to assay a sample (which has any PrPc denatured via proteinase K) for the presence of PrPSc of a specific species which PrPSc is associated with disease. Antibodies which specifically bind to human PrPSc can be labeled and injected carrying out an in vivo diagnostic test to determine if the human is infected with prions associated with disease.

Abstract: The present invention provides a novel method for the identification and clonal isolation of antibodies that bind to unique epitopes. The method is based on the use of antibodies as solid phase capture reagents to bind a known capture antibody epitope, thereby precluding the capture antibody epitope from being presented to a population of antibodies to be screened. The method is particularly suited for screening libraries of cloned antibodies, such as phage display combinatorial antibodies. An antibody specific for herpes simplex virus (HSV), was employed as a model for the assay.

Abstract: Antibodies are disclosed which specifically bind to native PrPSc in situ. Preferred antibodies bind only to the native PrPSc of 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 PrPSc in situ and (5) bind 50% or more of PrPSc in a liquid flowable sample. Antibodies of the invention can be bound to a substrate and used to assay a sample (which has any PrPSc denatured via proteinase K) for the presence of PrPSc of a specific species which PrPSc is associated with disease. Antibodies which specifically bind to human PrPSc can be labeled and injected carrying out an in vivo diagnostic test to determine if the human is infected with prions associated with disease.

Abstract: Antibodies are disclosed which specifically bind to native PrPSc in situ. Preferred antibodies bind only to the native PrPSc of 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 PrPSc in situ and (5) bind 50% or more of PrPSc in a liquid flowable sample. Antibodies of the invention can be bound to a substrate and used to assay a sample (which has any PrPc denatured via proteinase K) for the presence of PrPSc of a specific species which PrPSc is associated with disease. Antibodies which specifically bind to human PrPSc can be labeled and injected carrying out an in vivo diagnostic test to determine if the human is infected with prions associated with disease.

Abstract: Antibodies are disclosed which specifically bind to native PrP.sup.Sc in situ. Preferred antibodies bind only to the native PrP.sup.Sc of a particular species e.g., human, cow, sheep, pig, etc. Particularly preferred antibodies bind specifically to a particular isoform of human PrP.sup.Sc. Preferred antibodies of the invention are (1) produced by phage display methodology, (2) bind specifically to native PrP.sup.Sc, (3) neutralizes the infectivity of prions, (4) bind to PrP.sup.Sc in situ and (5) bind 50% or more of PrP.sup.Sc in a liquid flowable sample. Antibodies of the invention can be bound to a substrate and used to assay a sample (which has any PrP.sup.c denatured via proteinase K) for the presence of PrP.sup.Sc of a specific species which PrP.sup.Sc is associated with disease. Antibodies which specifically bind to human PrP.sup.Sc can be labeled and injected carrying out an in vivo diagnostic test to determine if the human is infected with prions associated with disease.