60 results about "Transmissible spongiform encephalopathy" patented technology

Methods are disclosed for sterilizing biological materials to reduce the level therein of one or more biological contaminants or pathogens, such as prions, responsible for the disease states known as transmissible spongiform encephalopathies (TSEs) in mammals. These methods involve sterilizing biological materials with irradiation.

A method for extracting prion protein from a biological material, e.g., an animal tissue or product. In a specific example, abnormal prion protein is extracted from homogenized sheep brain with hexafluoro-2-propanol. The hexafluoro-2-propanol is separated from the aqueous brain preparation by increasing the ionic strength of the aqueous solution. Prion protein in the organic extract can be further purified, or the extract can be tested, e.g., by immunoassay, for the presence of prion protein, and more particularly abnormal prion protein. The extraction process permits testing for the presence of abnormal prior protein, e.g., for diagnosis of transmissible spongiform encephalopathies (TSE).

A highly sensitive method is provided for the detection of prions in a sample. These methods may be used to diagnose prion mediated transmissible spongiform encephalopathies such as bovine spongiform encephalopathy, Creutzfeldt-Jakob disease, scrapie, or chronic wasting disease. In particular a method for serial automated cyclic amplification of prion is disclosed. The method is both rapid and highly sensitive making it ideal for high throughput testing.

Provided is a method of detecting transmissible spongiform encephalopathies. The method comprises: selecting a sample from a subject to determine whether the subject has a transmissible spongiform encephalopathy; and detecting spiroplasma-specific 16S rDNA indicative of transmissible spongiform encephalopathies in the sample. The spiroplasma-specific 16S rDNA is preferably detected by contacting the sample with a pair of oligonucleotide primers under polymerase chain reaction conditions and detecting the resulting polymerase chain reaction product, wherein each of the pair of the oligonucleotide primers is complementary to spiroplasma-specific 16S rDNA indicative of transmissible spongiform encephalopathies. Further provided is an oligonucleotide having a nucleotide sequence complementary to spiroplasma-specific 16S rDNA indicative of transmissible spongiform encephalopathies; as well as an oligonucleotide having a nucleotide sequence specific to spiroplasma-specific 16S rDNA indicative of transmissible spongiform encephalopathies.

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.

Heart and brain fatty acid binding proteins (H-FABP, B-FABP) are markers for TSEs, especially CJD. The invention provides a diagnostic assay for either of these markers, preferably by enzyme immunoassay using a specific antibody thereto. Since H-FABP is also a marker for acute myocardial infarction (AMI), to distinguish CJD from AMI requires an assay specific to AMI, e.g. using troponin-1 or CK-MB as a marker, also to be carried out.

The use of Apolipoprotein B, Apolipoprotein E, fragments and mimetics thereof is provided for diagnostic, detection, prognostic and therapeutic applications In prion diseases. More specifically, the invention provides the use of Apolipoprotein B or fragments thereof for modulating or identifying modulators of the prion protein replication which are implicated in the pathogenesis of transmissible spongiform encephalopathics and other prion diseases.

Provided is a safe novel method for detecting Transmissible Spongiform encephalopathies (TSE). The method comprises: selecting a sample from a subject to determine whether the subject has transmissible spongiform encephalopathy; and detecting abnormal prion protein (Prpes) in the sample. The method detects PrP^res without Proteinase-K treatment by disrupting the sample in guanidine thiocyanate lysis solution followed by phenol purification of proteins, and demonstration of the abnormal prion isoform by Western blotting using monoclonal antibodies against prion protein structure. Guanidine salts effectively kill TSE infectivity providing a laboratory safe environment and stabilize biomolecules so TSE samples can be procured in the field and transported to the laboratory in guanidine lysis solution for processing at a later date. This method provides for rapid detection of the abnormal prion isoform diagnostic of TSE and results are easily interpretable based upon very different Western blot patterns for abnormal prion isoform versus the normal prion.

Transmissible spongiform encephalopathy (TSE) is diagnosed in a subject by using mass spectrometry to observe a polypeptide in a sample of body fluid taken from the subject. The polypeptide is differentially contained in the body fluid of TSE-infected subjects and non-infected subjects, and has a molecular weight in the range of from 1000 to 100000.

The purpose of the present invention is to evaluate the quality of feed for ruminants and consequently, avoid the transmission of TSEs through the detection of animal proteins in these foods. This purpose is embodied in the form of a method for detecting proteins of animal origin in complex mixtures comprising the stages of: (i) extraction of the proteic matter in high concentration from a sample of the initial complex mixture in a manner as to substantially remove all interferents; (ii) preparation of the matrix-analyte in a manner as to maintain low levels of impurities and an adequate matrix-analyte molar rate; (iii) analysis of the material obtained in the prior stage by MALDI-TOF mass spectrometry; (iv) optionally, fractionation of the samples or isolation of the components by RP-HPLC and identification of the components by means of automatic sequencing of the N-terminal region and sequencing of its peptidic fragments by liquid chromatography coupled to mass spectrometry (LC/MS/MS). The present invention also contemplates the use of this method in the detection of proteins of animal origin in feed for ruminants, which permits the interruption of transmission of Transmittable Spongiform Encephalopathies, and more particularly Bovine Spongiform Encephalopathies (BSE).

The invention is related to the treatment of prion-related diseases such as the transmissible spongiform encephalopathies (TSEs) in mammals by administering chaotropic agents to or inducing a hyperthermia state in the affected mammals.

Methods for diagnosing altered neuropathology in an animal are disclosed, wherein said methods comprise imaging brain, spinal cord, or other neural tissue of the animal, analyzing the appearance of the tissue, and determining whether the appearance of the tissue is altered relative to corresponding unaltered tissue. Also disclosed are methods for diagnosing spongiform encephalopathies in an animal, wherein said methods comprise imaging brain, spinal cord, or other neural tissues of the animal, analyzing the appearance of vacuoles in the tissue, and determining whether the appearance of the vacuoles in the tissue is altered relative to corresponding spongiform encephalopathy-free tissue. Also disclosed are automated methods for diagnosing altered neuropathy and spongiform encephalopathies.

Methods and compositions are provided comprising a therapeutically effective amount of a compound of formula I

wherein R^1-4, W, X, Y and Z are as defined in the specification, for inhibiting and treating diseases and disorders associated with pathogenic proteins causing neurodegenerative diseases and amyloid diseases, such as protease resistant prion proteins (PrP^Sc) and those associated with transmissible spongiform encephalopathies (TSEs), Alzheimer's Disease, amyloidosis, and the like.

Disclosed is a method for identifying transmissible spongiform encephalopathy in livestock via an electroretinogram, the method comprises producing a biphasic electroretinogram waveform having an a-wave and b-wave from livestock retina in response to photic stimulus, measuring the amplitude of the b-wave, wherein the amplitude is measured from the trough of the a-wave to the peak of the b-wave, measuring the implicit time of the b-wave, wherein the implicit time is measured from onset of photic stimulus to b-wave peak; and comparing said produced waveform to a comparative waveform of livestock known not to have transmissible spongiform encephalopathy, wherein the produced waveform having a decrease b-wave amplitude and increased b-wave implicit time being indicative of livestock having transmissible spongiform encephalopathy.

In the present invention, we described the use of anti-DNA antibody for the detection of prions and diagnosis of Transmissible Spongiform Encephalopathies (TSE) diseases in animals and humans.

The present invention relates to the diagnosis of transmissible spongiform encephalopathies (TSEs). It especially teaches the production of a soluble prion protein (PrP)-chaperone complex and the advantageous use of such chaperone-PrP complex, especially in the detection of PrP in an immunoassay, as well as its use as and immunogen.

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.