249 results about "Proteinaceous infectious particle" 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.

The use of collagen as a biomedical implant raises safety issues towards viruses and prions. The physicochemical changes and the in vitro and in vivo biocompatibility of collagen treated with heat, and by formic acid (FA), trifluoroacetic acid (TFA), tetrafluoroethanol (TFE) and hexafluoroiso-propanol (HFIP) were investigated. FA and TFA resulted in extensive depurination of nucleic acids while HFIP and TFE did so to a lesser degree. The molecules of FA, and most importantly of TFA, remained within collagen. Although these two acids induced modification in the secondary structure of collagen, resistance to collagenase was not affected and, in vitro, cell growth was not impaired. Severe dehydrothermal treatment, for example 110° C. for 1-3 days under high vacuum, also succeeded in removing completely nucleic acids. Since this treatment also leads to slight cross-linking, it could be advantageously used to eliminate prion and to stabilize gelatin products. Finally, prolonged treatment with TFA provides a transparent collagen, which transparency is further enhanced by adding glycosaminoglycans or proteoglycans, particularly hyaluronic acid. All the above treatments could offer a safe and biocompatible collagen-derived material for diverse biomedical uses, by providing a virus or prion-free product.

Disclosed are pharmaceutical compositions and methods for preventing or treating a number of amyloid diseases, including Alzheimer's disease, prion diseases, familial amyloid neuropathies and the like. The pharmaceutical compositions include immunologically reactive amounts of amyloid fibril components, particularly fibril-forming peptides or proteins. Also disclosed are therapeutic compositions and methods which use immune reagents that react with such fibril components.

A method of preparing a fixed biological tissue includes, shaping the biological tissue, cross-linking the biological tissue, sterilizing the biological tissue, and inactivating prions in the biological tissue.

Devices such as flow through columns, substrates such as spherical polymer beads, and methods of using such to remove prions from any liquid sample are disclosed. A surface of a substrate is coated with a prion complexing agent, such as a salt of phosphotungstic acid. Blood or plasma passing through a column containing beads coated with prion complexing agent are rendered prion free.

Catalytic monoclonal antibodies (abzymes) with selective protease activity in the pathologies characterized by the presence of plaques and fibrillar aggregates with protein component; methods for the preparation thereof and the use thereof as medicaments in the treatment of pathologies such as Alzheimer's disease, amyloidosis, atherosclerosis, prions diseases.

The present invention provides methods and systems for conditioning cerebrospinal fluid (CSF). The methods provide for efficiently removing target compounds from CSF. The systems provide for a multilumen flow path and exchange of a majority volume portion of CSF in the CSF space. The removal and/or delivery of specific compounds can be tailored to the pathology of the specific disease. The removal is targeted and specific, for example, through the use of specific size-exclusion thresholds, antibodies against specific toxins, and other chromatographic techniques, as well as delivery and/or removal of targeted therapeutic agents. The invention finds use as a diagnostic, therapeutic and drug delivery platform for a variety of diseases affecting the CNS by accessing the CSF space. Exemplified disease conditions treatable by the present CSF processing systems and methods include, but are not limited to: Cerebral Vasospasm, Guillain Bane Syndrome, illustrating multi-lumen lumbar approach Alzheimer's, Parkinson's, Huntington's, Multiple Sclerosis, Amyotrophic Lateral Sclerosis, Spinal Cord Injury, Traumatic Brain Injury, Stroke, Cancer affecting the brain or spinal cord, Prion disease, Encephalitis from various causes, Meningitis from various causes, diseases secondary to enzymatic or metabolic imbalances, Biological Warfare, etc. For the first time, the present invention offers patients a disease-modifying, disruptive technology treatment platform that addresses the known disease pathogenesis of a number of neurologic conditions to which there are presently limited and ineffective treatment options.

Methods and compositions comprising GnRH-I and GnRH-II, GnRH-I and GnRH-II antibodies, anti-receptor antibodies, polynucleotide constructs and GnRH-I and GnRH-II analogs for immune enhancement and suppression, prevention and treatment of diseases and conditions characterized by abnormal T-cell activity, treatment of viral and prion-related diseases, and treatment of T-cell related neoplastic diseases are disclosed.

<heading lvl="0">Abstract of Disclosure</heading> A method of forming and preserving a bioremodelable, biopolymer scaffold material by subjecting animal tissue, particularly fetal or neo-natal tissue, to chemical and mechanical processing. The process includes, but is not limited t, harvesting the tissue, optionally extracting growth and differentiation factors from the tissue, inactivating infective agents of the tissue, mechanically expressig undesirable components frm the tissue, delipidizing the tissue, washing the tissue, optionally drying the tissue, and optionally cross-linking the tissue not necessarily in the order described. The resulting product, EBM, is characterized by its microbial, fungal, viral and prion inactivated state. EBM is storng, bioremodelable, drapable and does not undergo calicification. EBM supplants previous inventions because of its unique method of preparation and broad applicability in tissue reengineering

Prion protein binding materials and methods for using the binding materials to detect or remove a prion protein from a sample, such as a biological fluid or an environmental sample. The binding materials are capable of binding to one or more forms of prion protein including cellular prion protein (PrPc), infectious prion protein (PrPsc), recombinant prion protein (PrPr), and proteinase resistant prion protein (PrPres). Prions from various species, including humans and hamsters, are bound by the binding materials.

The present invention relates to immunogenic but non-depositing-forming polypeptides or peptides homologous to amyloid β, prion, amylin or α-synuclein which can be used alone or conjugated to an immunostimulatory molecule in an immunizing composition for inducing an immune response to amyloid β peptides and amyloid deposits, to prion protein and prion deposits, to amylin and amylin deposits, to α-synuclein and deposits containing α-synuclein, or to polyglutamine repeats and deposits of proteins containing polyglutamine repeats. Described are also antibodies directed against such peptides, their generation, and their use in methods of passive immunization to such peptides and deposits.

The invention provides methods and kits for detecting conformationally altered proteins and prions in a sample. In one embodiment, the conformationally altered proteins and prions are associated with amyloidogenic diseases.

Peptide reagents that interact preferentially with the PrP^sc form of the prion protein are described. Methods of using the reagents or antibodies to the reagents for detection, diagnosis, purification, therapy and prophylaxis for prions and prion-associated diseases are also described.

Methods are disclosed for sterilizing biological materials to reduce the level of one or more biological contaminants or pathogens therein, such as viruses, bacteria (including inter- and intracellular bacteria, such as mycoplasmas, ureaplasmas, nanobacteria, chlamydia, rickettsias), yeasts, molds, fungi, single or multicellular parasites, and/or prions or similar agents responsible, alone or in combination, for TSEs. These methods involve the use of stabilizer mixtures in methods of sterilizing biological materials with irradiation.

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.