Government-Owned Inventions; Availability for Licensing, 12934-12935 [2020-04535]

Download as PDF 12934 Federal Register / Vol. 85, No. 44 / Thursday, March 5, 2020 / Notices khammond on DSKJM1Z7X2PROD with NOTICES commercialization of results of federally-funded research and development. Foreign patent applications are filed on selected inventions to extend market coverage for companies and may also be available for licensing. FOR FURTHER INFORMATION CONTACT: Jeffrey Thruston at 301–594–5179 or jeffrey.thruston@nih.gov. Licensing information may be obtained by communicating with the Technology Transfer and Intellectual Property Office, National Institute of Allergy and Infectious Diseases, 5601 Fishers Lane, Rockville, MD 20852; tel. 301–496– 2644. A signed Confidential Disclosure Agreement will be required to receive copies of unpublished information related to the invention. SUPPLEMENTARY INFORMATION: Technology description follows: A Rapid Ultrasensitive Assay for Detecting Prions Based on the Seeded Polymerization of Recombinant Normal Prion Protein (rPrP-sen) Description of Technology Prion diseases are neurodegenerative diseases of great public concern as humans may either develop disease spontaneously or, more rarely, due to mutations in their prion protein gene or exposures to external sources of infection. Prion disease is caused by the accumulation in the nervous system of abnormal aggregates of prion protein. This technology enables rapid, economical, and ultrasensitive detection of disease-associated forms of prion protein. Specifically, prion aggregates (contained in a biological sample) seed the polymerization of recombinant, monomeric prion protein (rPrP-sen) and the polymerized product is detected as a highly amplified indicator of infectious prions in the sample. This assay differs from the proteinmisfolding cyclic amplification assay (PMCA) because it enables the effective use of bacterially expressed rPrP-sen and does not require multiple amplification rounds. In its current embodiment, this assay can be used to detect prions in tissues or fluids from humans (Creutzfeldt-Jakob disease (CJD)), sheep (scrapie), cattle (bovine spongiform encephalopathy), and deer (chronic wasting disease (CWD)). For example, analyses of cerebrospinal fluid and/or nasal brushings from living sporadic CJD patients has allowed for nearly 100% accurate diagnosis. This technology is available for licensing for commercial development in accordance with 35 U.S.C. 209 and 37 CFR part 404. Potential Commercial Applications: VerDate Sep<11>2014 16:20 Mar 04, 2020 Jkt 250001 • A test/screen for infectious prions in live animals and food products • Cervid CWD monitoring • A human diagnostic for early detection of prion diseases • Medical equipment screening • A monitor for effectiveness of treatments or disease progression • A high through-put screen for inhibitors of prion replication Competitive Advantages: • Uses a consistent, concentrated source of normal prion protein (rPrP-sen) • Prions are detectable to low levels after a single amplification round • Demonstrated to be effective at detecting prions from different species • May be applicable to blood products, nasal brushings, skin, eye components and other accessible biospecimens • Economical and rapid Development Stage: • Research Use Inventors: Ryuichiro Atarashi (NIAID), Roger Moore (NIAID), Byron Caughey (NIAID). Publications: Atarashi, Ryuichiro et al. ‘‘Simplified ultrasensitive prion detection by recombinant PrP conversion with shaking.’’ Nature Methods 5, pages 211–212 (2008). Licensing Contact: To license this technology, please contact Jeffrey Thruston at 301–594–5179 or jeffrey.thruston@nih.gov, and reference E–109–2007–0. Dated: February 25, 2020. Wade W. Green, Acting Deputy Director, Technology Transfer and Intellectual Property Office, National Institute of Allergy and Infectious Diseases. [FR Doc. 2020–04536 Filed 3–4–20; 8:45 am] BILLING CODE 4140–01–P DEPARTMENT OF HEALTH AND HUMAN SERVICES National Institutes of Health Government-Owned Inventions; Availability for Licensing AGENCY: National Institutes of Health, HHS. ACTION: Notice. The invention listed below is owned by an agency of the U.S. Government and is available for licensing to achieve expeditious commercialization of results of federally-funded research and development. Foreign patent applications are filed on selected inventions to extend market coverage SUMMARY: PO 00000 Frm 00049 Fmt 4703 Sfmt 4703 for companies and may also be available for licensing. FOR FURTHER INFORMATION CONTACT: Jeffrey Thruston at 301–594–5179 or jeffrey.thruston@nih.gov. Licensing information may be obtained by communicating with the Technology Transfer and Intellectual Property Office, National Institute of Allergy and Infectious Diseases, 5601 Fishers Lane, Rockville, MD 20852; tel. 301–496– 2644. A signed Confidential Disclosure Agreement will be required to receive copies of unpublished information related to the invention. SUPPLEMENTARY INFORMATION: Technology description follows: Tau RT-QuIC: Ultrasensitive Assays for the Detection of Tau Seeding Activity Associated With Tauopathies Description of Technology: Tauopathies are a category of neurodegenerative diseases defined by the abnormal accumulation of misfolded tau protein aggregates (often in the form of amyloid filaments) within the brain. Tau proteins exist in six isoforms, three of which contain three microtubule binding regions (3R), and the remainder contain four microtubule binding regions (4R). Tauopathies are characterized, in part, based on the ratio of 3R/4R misfolded tau proteins that make up the aggregates. This technology enables rapid, ultrasensitive and economical differentiation of selfpropagating tau aggregates associated with tauopathies in crude biospecimens. The assays use recombinant, truncated 3R, 4R, or 3R+4R tau protein substrates as indicators of tau aggregates. Specifically, misfolded tau aggregates (contained in a biological sample) seed the polymerization of either 3R, 4R, or 3R+4R tau substrates, and the polymers (amyloid fibrils) are detected as an amplified indicator of even extremely low concentrations of tau aggregates within the biological sample and aid in identification of the tauopathy. In its current embodiment, this assay has been used to detect tau seeds in brain tissue from patients with Alzheimer’s disease, Pick disease, chronic traumatic encephalopathy, corticobasal degeneration, progressive supranuclear palsy, certain frontotemporal dementias, and other tauopathies. For several of these diseases, tau RT-QuIC assays have also detected tau seeding activity in patients’ cerebrospinal fluid. This technology is available for licensing for commercial development in accordance with 35 U.S.C. 209 and 37 CFR part 404. Potential Commercial Applications: • Diagnosis of tauopathies, including: Alzheimer’s disease, Pick disease, E:\FR\FM\05MRN1.SGM 05MRN1 Federal Register / Vol. 85, No. 44 / Thursday, March 5, 2020 / Notices corticobasal degeneration, chronic traumatic encephalopathy, progressive supranuclear palsy, and frontotemporal dementias with tau deposition. • Measurement of levels of pathological tau aggregates in biospecimens. • Analysis of tauopathy-associated disease progression • Clinical trial/drug development companion diagnostic Competitive Advantages: • Uses a consistent, concentrated source of truncated tau protein • Rapid and economical • Highly sensitive and specific Development Stage: • Research Use. Inventors: Byron Caughey (NIAID), Eri Saijo (NIAID), Allison Kraus (NIAID), Michael Metrick II (NIAID). Publications: Saijo, Eri et al. ‘‘Ultrasensitive and selective detection of 3-repeat tau seeding activity in Pick disease brain and cerebrospinal fluid’’. Acta Neuropathologica vol. 133 (2017):751–765. Kraus, Allison et al. ‘‘Seeding selectivity and ultrasensitive detection of tau aggregate conformers of Alzheimer disease’’. Acta Neuropathologica vol. 137, 4 (2019): 585–598. Metrick II Michael et al., ‘‘Million-fold sensitivity enhancement in proteopathic seed amplification assays for biospecimens by Hofmeister ion comparisons’’. Proc Natl Acad Sci USA vol. 116, 46 (2019):23029–23039. Saijo, Eri et al. ‘‘4-repeat tau seeds and templating subtypes as brain and CSF biomarkers of frontotemporal lobar degeneration’’. Acta Neuropathologica vol 139, 4(2020):63–77. Metrick II, Michael et al. ‘‘A single ultrasensitive assay for detection and discrimination of tau aggregates of Alzheimer and Pick diseases’’. Acta Neuropathologica Communications vol. 8, 1 (2020):22. Licensing Contact: To license this technology, please contact Jeffrey Thruston at 301–594–5179 or jeffrey.thruston@nih.gov, and reference E–015–2017–0. khammond on DSKJM1Z7X2PROD with NOTICES Dated: February 25, 2020. Wade W. Green, Acting Deputy Director, Technology Transfer and Intellectual Property Office, National Institute of Allergy and Infectious Diseases. [FR Doc. 2020–04535 Filed 3–4–20; 8:45 am] BILLING CODE 4140–01–P VerDate Sep<11>2014 16:20 Mar 04, 2020 Jkt 250001 DEPARTMENT OF HEALTH AND HUMAN SERVICES National Institutes of Health Government-Owned Inventions; Availability for Licensing AGENCY: National Institutes of Health, HHS. ACTION: Notice. The invention listed below is owned by an agency of the U.S. Government and is available for licensing to achieve expeditious commercialization of results of federally-funded research and development. Foreign patent applications are filed on selected inventions to extend market coverage for companies and may also be available for licensing. FOR FURTHER INFORMATION CONTACT: Jeffrey Thruston at 301–594–5179 or jeffrey.thruston@nih.gov. Licensing information may be obtained by communicating with the Technology Transfer and Intellectual Property Office, National Institute of Allergy and Infectious Diseases, 5601 Fishers Lane, Rockville, MD 20852; tel. 301–496– 2644. A signed Confidential Disclosure Agreement will be required to receive copies of unpublished information related to the invention. SUPPLEMENTARY INFORMATION: Technology description follows: SUMMARY: Alpha-Synuclein RT-QuIC: An Ultrasensitive Assay for the Detection of Alpha-Synuclein Seeding Activity Associated With Synucleinopathies Description of Technology: Synucleinopathies are a category of neurodegenerative diseases defined by the abnormal aggregation and accumulation of misfolded alphasynuclein protein molecules within the brain. These aggregates are of particular concern to humans as they are a primary cause of Parkinson’s disease, dementia with Lewy bodies, and other neurological disorders. This technology enables rapid, economical and ultrasensitive detection of diseaseassociated forms of alpha-synuclein as biomarkers or indicators of synucleinopathy in a biological sample. Specifically, alpha-synuclein aggregates (contained in a biological sample) seed the polymerization of vast PO 00000 Frm 00050 Fmt 4703 Sfmt 4703 12935 stoichiometric excesses of recombinant, normally folded alpha-synuclein into amyloid fibrils that are then detectable by an amyloid-sensitive fluorescent dye. This reaction can thereby amplify the seeds in a biospecimen by many orders of magnitude. For example, in its current embodiment, this assay has been used to detect alpha-synuclein seeds in cerebral spinal fluid from living patients with Parkinson’s disease and Lewybody dementia, giving high diagnostic sensitivity and specificity with unprecedented speed. This technology is available for licensing for commercial development in accordance with 35 U.S.C. 209 and 37 CFR part 404. Potential Commercial Applications: • Pre-mortem diagnosis of synucleinopathies, including Parkinson’s disease and Lewy-body dementia • A monitor of the disease progression of dementia and synucleinopathies • Clinical trial/drug development companion diagnostic Competitive Advantages: • Uses a consistent, concentrated source of truncated alpha-synuclein protein substrate • Capable of disease detection prior to onset of symptoms • Rapid and economical Development Stage: • Research Use Inventors: Byron Caughey (NIAID), Bradley Groveman (NIAID), Christina Orru (NIAID), Lynne Raymond (NIAID) Publications: Groveman, Bradley R et al. ‘‘Rapid and ultra-sensitive quantitation of disease-associated asynuclein seeds in brain and cerebrospinal fluid by aSyn RT-QuIC.’’ Acta Neuropathologica Communications vol. 6(1):7, 9 Feb. 2018. Licensing Contact: To license this technology, please contact Jeffrey Thruston at 301–594–5179 or jeffrey.thruston@nih.gov, and reference E–233–2017–0. Dated: February 25, 2020. Wade W. Green, Acting Deputy Director, Technology Transfer and Intellectual Property Office, National Institute of Allergy and Infectious Diseases. [FR Doc. 2020–04534 Filed 3–4–20; 8:45 am] BILLING CODE 4140–01–P E:\FR\FM\05MRN1.SGM 05MRN1

Agencies

[Federal Register Volume 85, Number 44 (Thursday, March 5, 2020)]
[Notices]
[Pages 12934-12935]
From the Federal Register Online via the Government Publishing Office [www.gpo.gov]
[FR Doc No: 2020-04535]


-----------------------------------------------------------------------

DEPARTMENT OF HEALTH AND HUMAN SERVICES

National Institutes of Health


Government-Owned Inventions; Availability for Licensing

AGENCY: National Institutes of Health, HHS.

ACTION: Notice.

-----------------------------------------------------------------------

SUMMARY: The invention listed below is owned by an agency of the U.S. 
Government and is available for licensing to achieve expeditious 
commercialization of results of federally-funded research and 
development. Foreign patent applications are filed on selected 
inventions to extend market coverage for companies and may also be 
available for licensing.

FOR FURTHER INFORMATION CONTACT: Jeffrey Thruston at 301-594-5179 or 
[email protected]. Licensing information may be obtained by 
communicating with the Technology Transfer and Intellectual Property 
Office, National Institute of Allergy and Infectious Diseases, 5601 
Fishers Lane, Rockville, MD 20852; tel. 301-496-2644. A signed 
Confidential Disclosure Agreement will be required to receive copies of 
unpublished information related to the invention.

SUPPLEMENTARY INFORMATION: Technology description follows:

Tau RT-QuIC: Ultrasensitive Assays for the Detection of Tau Seeding 
Activity Associated With Tauopathies

    Description of Technology:
    Tauopathies are a category of neurodegenerative diseases defined by 
the abnormal accumulation of misfolded tau protein aggregates (often in 
the form of amyloid filaments) within the brain. Tau proteins exist in 
six isoforms, three of which contain three microtubule binding regions 
(3R), and the remainder contain four microtubule binding regions (4R). 
Tauopathies are characterized, in part, based on the ratio of 3R/4R 
misfolded tau proteins that make up the aggregates. This technology 
enables rapid, ultrasensitive and economical differentiation of self-
propagating tau aggregates associated with tauopathies in crude 
biospecimens. The assays use recombinant, truncated 3R, 4R, or 3R+4R 
tau protein substrates as indicators of tau aggregates. Specifically, 
misfolded tau aggregates (contained in a biological sample) seed the 
polymerization of either 3R, 4R, or 3R+4R tau substrates, and the 
polymers (amyloid fibrils) are detected as an amplified indicator of 
even extremely low concentrations of tau aggregates within the 
biological sample and aid in identification of the tauopathy. In its 
current embodiment, this assay has been used to detect tau seeds in 
brain tissue from patients with Alzheimer's disease, Pick disease, 
chronic traumatic encephalopathy, corticobasal degeneration, 
progressive supranuclear palsy, certain frontotemporal dementias, and 
other tauopathies. For several of these diseases, tau RT-QuIC assays 
have also detected tau seeding activity in patients' cerebrospinal 
fluid.
    This technology is available for licensing for commercial 
development in accordance with 35 U.S.C. 209 and 37 CFR part 404.
    Potential Commercial Applications:
 Diagnosis of tauopathies, including: Alzheimer's disease, Pick 
disease,

[[Page 12935]]

corticobasal degeneration, chronic traumatic encephalopathy, 
progressive supranuclear palsy, and frontotemporal dementias with tau 
deposition.
 Measurement of levels of pathological tau aggregates in 
biospecimens.
 Analysis of tauopathy-associated disease progression
 Clinical trial/drug development companion diagnostic
    Competitive Advantages:
 Uses a consistent, concentrated source of truncated tau 
protein
 Rapid and economical
 Highly sensitive and specific
    Development Stage:
 Research Use.
    Inventors: Byron Caughey (NIAID), Eri Saijo (NIAID), Allison Kraus 
(NIAID), Michael Metrick II (NIAID).
    Publications:

Saijo, Eri et al. ``Ultrasensitive and selective detection of 3-
repeat tau seeding activity in Pick disease brain and cerebrospinal 
fluid''. Acta Neuropathologica vol. 133 (2017):751-765.
Kraus, Allison et al. ``Seeding selectivity and ultrasensitive 
detection of tau aggregate conformers of Alzheimer disease''. Acta 
Neuropathologica vol. 137, 4 (2019): 585-598.
Metrick II Michael et al., ``Million-fold sensitivity enhancement in 
proteopathic seed amplification assays for biospecimens by 
Hofmeister ion comparisons''. Proc Natl Acad Sci USA vol. 116, 46 
(2019):23029-23039.
Saijo, Eri et al. ``4-repeat tau seeds and templating subtypes as 
brain and CSF biomarkers of frontotemporal lobar degeneration''. 
Acta Neuropathologica vol 139, 4(2020):63-77.
Metrick II, Michael et al. ``A single ultrasensitive assay for 
detection and discrimination of tau aggregates of Alzheimer and Pick 
diseases''. Acta Neuropathologica Communications vol. 8, 1 
(2020):22.

    Licensing Contact: To license this technology, please contact 
Jeffrey Thruston at 301-594-5179 or [email protected], and 
reference E-015-2017-0.

    Dated: February 25, 2020.
Wade W. Green,
Acting Deputy Director, Technology Transfer and Intellectual Property 
Office, National Institute of Allergy and Infectious Diseases.
[FR Doc. 2020-04535 Filed 3-4-20; 8:45 am]
BILLING CODE 4140-01-P
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