45 results about "Spongiform encephalopathy" patented technology

The invention provides cloned transgenic ungulates (e.g., bovines) in which prion protein activity is reduced by one or more genetically engineered mutations. Desirably, these transgenic bovines are also genetically modified to express xenogenous (e.g., human) antibodies. Because of their resistance to prion-related diseases such as bovine spongiform encephalopy (also known as mad cow disease), these bovines are a safer source of human antibodies for pharmaceutical uses and a safer source of agricultural products.

Assays are provided for rapid detection, with high specificity of the pathogenic form of prion protein responsible for neurodegenerative diseases affecting humans and animals, such as transmissible spongiform encephalopathy in bovine, sheep, and cats. Also provided are assays for testing animal feedstock, such as animal feed, for the presence or concentration of pathogenic prion protein. Results are available in from about 0.5 to about 20 minutes and preferably within from about 5 to about 10 minutes. The assays employ proteinase-K to remove normal prion protein from a biological sample, so that the sample may be analyzed by immunochromatography to determine the presence and concentration of pathogenic prion protein. Because the proteinase-K is immobilized on a solid support for in situ removal of interfering components, the present invention obviates the need for subsequent extraction of the desired analyte. All aspects of the present invention are suitable for quantifying the minimal detectable amount of pathogenic prion protein in a biological sample. Moreover, the simplicity of sample preparation makes the present invention suitable for use in the field.

Short peptides and derivatives or analogs thereof for the treatment or prevention of transmissible spongiform encephalopathies, in particular CJD are herein described. These peptides and / or their derivatives have been designed to block the conformational changes that occur in the prion protein (PrP) and which are implicated in the pathogenesis of transmissible spongiform encephalopathies as well as to dissolve the fibrillar deposits already formed

A process for detecting the forms of the prion pathogens responsible for subacute, transmissible, spongiform encephalopathies, including a macrocyclic adjuvant ligand (AML), free or bound to a support, that is added to a biological sample capable of containing PrPsc, the resulting suspension then being reacted with an anti-PrPsc antibody, and the presence of PrP is then detected.

Disclosed herein are compounds and methods for decreasing PrP and preventing, ameliorating, or treating a prion disease or conformational neurodegenerative disorder, in an individual in need thereof. Examples of disease conditions that can be ameliorated with the administration of antisense compounds targeted to PrP include Creutzfeldt-Jakob disease (CJD); variant Creutzfeldt-Jakob Disease (vCJD); Gerstmann-Straussler-Scheinker syndrome; fatal familial insomnia; kuru; Bovine Spongiform Encephalopathy (BSE), e.g. “mad cow disease”; Chronic Wasting Disease (CWD); scrapie; transmissible mink encephalopathy; feline spongiform encephalopathy; ungulate spongiform encephalopathy; Alzheimer's disease; Parkinson's disease; Huntington's disease; and Amyotrophic Lateral Sclerosis (ALS).

Methods for the detection of the disease associated conformation of the prion protein as an indication of transmissible spongiform encephalopathies (TSEs), including preclinical detection of infected live animals and humans, and post-mortem detection methods are disclosed. In one aspect, the tissue or body fluid sample of a test subject is contacted with an antibody that binds only the disease related conformation of the prion protein under non-denaturing conditions.

The present invention deals with a method of preparing nucleic acids, particularly RNA, from a whole blood sample. The nucleic acids purified by the method of the invention are particularly suited for detection of nucleic acid marker molecules. Preferred are markers for the diagnosis of transmissible spongiform encephalopathy (TSE). Such diagnosis is based on the detection, by means of real-time PCR, of certain mRNAs of the TSE-infected organism. Said mRNAs specifically originate as splicing variants and are isolated from whole blood by the method of the invention.

A highly sensitive method for detecting prions in a sample is provided. These methods can be used to diagnose prion-mediated transmissible spongiform encephalopathy, such as bovine spongiform encephalopathy, Creutzfeldt-Jakob disease, scrapie or chronic wasting disease. In particular, methods for continuous automated cyclic expansion of prions are disclosed. The method is fast and highly sensitive, making it ideal for high-throughput testing.

A process for detecting the forms of the prion pathogens responsible for subacute, transmissible, spongiform encephalopathies, including a macrocyclic adjuvant ligand (AML), free or bound to a support, that is added to a biological sample capable of containing PrPsc, the resulting suspension then being reacted with an anti-PrPsc antibody, and the presence of PrP is then detected.

The invention relates to a monoclonal antibody prepared with genetic engineering and the preparation method and usage thereof. Exactly speaking, the invention relates to monoclonal antibody mab-PrP102-6 of bovine prion protein PrP27-30 and .

The present invention relates to a soluble hybrid protein, comprising at least a first polypeptide sequence derived from a prion protein PrPc that is capable of binding a protein responsible for transmissible spongiform encephalitis (PrPSc), and a second polypeptide sequence (tag), wherein said hybrid protein does not comprise a functional membrane anchor moiety. Also, the present invention is directed to the use of said hybrid proteins for the diagnosis of transmissible spongiform encephalopathies. In addition, the present invention relates to the use of said hybrid protein, a nucleic acid encoding said hybrid protein, a vector, and / or a host cell comprising a nucleic acid encoding said hybrid protein for the preparation of a medicament for the prevention or treatment of transmissible spongiform encephalopathies (TSEs). Furthermore, the present invention is directed to a process for producing said hybrid proteins and it also relates to transgenic animals stably expressing said hybrid protein, the bone marrow of said transgenic animals and the use of said bone marrow for the treatment of transmissible spongiform encephalopathies (TSEs).

The present invention relates to a medium composition for production of botulinum toxin and, more particularly, to a medium composition for culture of Clostridium sp. capable of producing botulinum toxin. The medium composition of the present invention comprises at least one plant-derived peptone selected from the group consisting of a garden pea hydrolysate, a cotton seed hydrolysate and a wheat gluten hydrolysate. When the medium according to the present invention, which contains plant-derived peptones and minerals, is used for culture of Clostridium botulinum, the growth rate of the bacterium in the medium is about 1.5-2 times higher than that in the medium that is in current use. In addition, when botulinum toxin is produced by culturing the bacterium in the medium, infection with transmissible spongiform encephalopathy (TSE) or the like can be prevented by blocking introduction of animal-derived components.

Embodiments of the present invention include methods and systems for designing inhibitors of amyloidosis in humans, domesticated animals, and wild animals as well as inhibitors of amyloidosis designed by the methods and systems. Methods and systems for designing inhibitors of amyloidosis are largely computational, in nature, and are directed to designing various types of polymers, small-molecule organic compounds, organometallic compounds, or non-chemical physical processes that can target the extended-α-strand and α-sheet regions of amyloidogenic protein and polypeptide intermediates in order to prevent aggregation of those intermediates into protofibrils and fibrils that, in turn, recruit additional native-conformation proteins and polypeptides into amyloidogenic intermediates and that additionally aggregate to form higher-order structures, such as plaques observed in the brains of patients suffering from the various spongiform encephalopathies.

The present invention deals with a method of preparing nucleic acids, particularly RNA, from a whole blood sample. The nucleic acids purified by the method of the invention are particularly suited for detection of nucleic acid marker molecules. Preferred are markers for the diagnosis of transmissible spongiform encephalopathy (TSE). Such diagnosis is based on the detection, by means of real-time PCR, of certain mRNAs of the TSE-infected organism. Said mRNAs specifically originate as splicing variants and are isolated from whole blood by the method of the invention.

The invention is related to diagnostic methods for detecting transmissible spongiform encephalopathies (TSEs) such as BSE and scrapie and related disease in humans. The invention provides use of guanidine thiocyanate (gdnSCN), or a functional equivalent thereof, for treating at least one sample derived from a mammal, including humans, for reducing the risk of scoring a false-positive test result in testing the sample for the presence or absence of aberrant prion protein.

The present invention relates to a method for preparing a bone graft substitute using bovine bone, and more particularly to a method for preparing a safe bone graft substitute which does not have the risk of infection with bovine spongiform encephalopathy, the method comprising treating bovine bone with sodium hypochlorite and treating the treated bone at a high temperature of more than 600° C. The bone graft substitute does not cause an immune response, because it is prepared by effectively removing lipids and organic substances from bovine bone having a structure very similar to that of the human bone. Also, it has excellent osteoconductivity, and is free of prion, and thus it does not have the risk of infection with bovine spongiform encephalopathy. According to the disclosed invention, the bone graft substitute having such advantages can be prepared in a simple manner.

The invention relates to a mutant prion protein (PrP), the globular domain of which comprises an engineered second disulfide bond in a similar position as in the human doppel protein (hDpl). In an embodiment, the prion protein has an engineered extra disulfide bond in the presumed ‘factor X’ binding epitope and is accommodated with slight, strictly localized conformational changes to inhibit prion propagation in human and animals. Also disclosed is the use of a mutant prion protein (PrP), the globular domain of which comprises at least one engineered additional disulfide bond in a similar position as in the human doppel protein, or fragments thereof for therapeutic treatment or for the manufacture of a medicament for therapeutic treatment of proteins causing disease after a conformational transition, e.g. Tranmissible Spongiform Encephalopathy (TSE), variant forms of Creutzfeldt-Jakob disease (CJD), fatal familial insomnia (FFI), and Gerstmann-Sträussler-Scheinker syndrome (GSS) in human. Further, the use of the PrP mutant protein for in vivo generation of disulfide mutants of prion proteins or fragments thereof is carried out in order to enable an intended ther-apy of TSE in animals, e.g. by somatic gene therapy with lentiviral vector, where TSE includes bovine spongiform encephalopathy (BSE), scrapie in sheep, feline spongiform encephalopathy (FSE), and chronic wasting disease (CWD) in elk and deer.