[Federal Register Volume 78, Number 166 (Tuesday, August 27, 2013)]
[Notices]
[Pages 52934-52936]
From the Federal Register Online via the Government Publishing Office [www.gpo.gov]
[FR Doc No: 2013-20888]
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DEPARTMENT OF HEALTH AND HUMAN SERVICES
National Institutes of Health
Government-Owned Inventions; Availability for Licensing
AGENCY: National Institutes of Health, HHS.
ACTION: Notice.
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SUMMARY: The inventions listed below are owned by an agency of the U.S.
Government and are available for
[[Page 52935]]
licensing in the U.S. in accordance with 35 U.S.C. 209 and 37 CFR Part
404 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: Licensing information and copies of
the U.S. patent applications listed below may be obtained by writing to
the indicated licensing contact at the Office of Technology Transfer,
National Institutes of Health, 6011 Executive Boulevard, Suite 325,
Rockville, Maryland 20852-3804; telephone: 301-496-7057; fax: 301-402-
0220. A signed Confidential Disclosure Agreement will be required to
receive copies of the patent applications.
Monoclonal Antibodies That Recognize the Human Type I Interferon
Receptor and Block Interferon Signaling
Description of Technology: Type I interferons play a critical role
in both innate and adaptive immunity through the stimulation of the
IFNAR1 which initiates interferon signaling in response to viral and
bacterial infections. However, abnormal interferon signaling is
associated with human diseases, such as lupus. The present invention
discloses six hybridomas that produce mouse monoclonal antibodies
specific for the extracellular domain of human IFNAR1. Two of the
monoclonal antibodies are able to bind IFNAR1 and reduce interferon
signaling. As such, they can be utilized as a research tool for
studying the expression of IFNAR1 and the inhibition of IFNAR1 function
in humans or possibly as therapeutic reagents for human diseases.
Potential Commercial Applications:
Research reagents for studying the expression and
signaling of IFNAR1.
A potential therapeutic reagent.
Competitive Advantages:
Specific for the extracellular domain of human IFNAR1. Can
therefore specifically recognize receptor expressed on the cell
surface.
Bind IFNAR1 and reduce interferon signaling
Development Stage:
Pilot
In vitro data available
Inventors: Sonja M. Best, Kirk Lubick, Shelly J. Robertson (NIAID)
Publications:
1. Goldman LA, et al. Characterization of antihuman IFNAR-1
monoclonal antibodies: epitope localization and functional analysis. J
Interferon Cytokine Res. 1999 Jan;19(1):15-26. [PMID 10048764]
2. Benoit P, et al. A monoclonal antibody to recombinant human IFN-
alpha receptor inhibits biologic activity of several species of human
IFN-alpha, IFN-beta, and IFN-omega. Detection of heterogeneity of the
cellular type I IFN receptor. J Immunol. 1993 Feb 1;150(3):707-16.
[PMID 8423335]
Intellectual Property: HHS Reference No. E-527-2013/0--Research
Material. Patent protection is not being pursued for this technology.
Licensing Contact: Susan Ano, Ph.D.; 301-435-5515;
[email protected].
Collaborative Research Opportunity: The National Institute of
Allergy and Infectious Diseases (NIAID) is seeking statements of
capability or interest from parties interested in collaborative
research to further develop, evaluate or commercialize human type I
interferon receptor antibodies. For collaboration opportunities, please
contact Alicia Evangelista at [email protected] or 301-594-
1673.
Anthrax Fusion Toxins With Improved Ability To Penetrate Cells
Description of Technology: Available for licensing are novel
conjugated or fusion proteins comprised of anthrax toxin lethal factor
cytolethal distending toxin subunit B. Several human tumor cell lines
have been found to be highly sensitive to these toxins with LD50 values
in the pM range. In vivo studies in mice have revealed that these
toxins selectively treat tumors and have very low systemic toxicity.
Potential Commercial Applications:
Pharmaceutical compositions to selectively treat cancer
Applications to treat or prevent growth of undesirable
cells
Competitive Advantages:
Selective with low systemic toxicity
Potent (pM LD50 values)
Development Stage:
Early-stage
In vitro data available
In vivo data available (animal)
Inventors: Christopher Bachran and Stephen Leppla (NIAID)
Intellectual Property: HHS Reference No. E-120-2013/0--US
Application No. 61/837,428 filed June 20, 2013
Licensing Contact: Patrick McCue, Ph.D.; 301-435-5560;
[email protected].
Method and Platform for Selectively Labeling RNA
Description of Technology: The invention pertains to a three step
initiation, elongation and termination method and platform for
synthesizing selectively labeled RNA molecules by first polymerizing a
first liquid phase RNA molecule from a solid phased DNA template fixed
onto a solid phase. The method includes the steps of incubating the
solid and liquid phases at appropriate elongation temperatures and then
terminating elongation by a separation stage where the phases are
incubated at near 0 degrees Celsius where it selectively terminates RNA
elongation. The steps can be repeated by the number bases (rNTPs) in
the final RNA molecule wherein in each iterative stage a new rNTP can
be added that is selectively labeled. The DNA may have a density of 30-
80% on the solid substrate, and the solid substrate may be a bead. The
bead may comprise a gel, glass, or a synthetic polymer. The bead may
have a diameter of 5-100 mm. The concentration of DNA may be 30 mm-1
nm. The concentration of rNTP may be 1-100 times the DNA concentration.
The RNA polymerase may be a T7 RNA polymerase. The label may be \13\C/
\5\N, \2\H, Cy3, Cy5, a fluorophore, a heavy atom, or a chemical
modification.
Potential Commercial Applications: Differentially labeled
diagnostics
Competitive Advantages: Multiple use detection method
Development Stage:
Prototype
In vitro data available
Inventors: Yun-Xing Wang (NCI), Liu Yu (NCI), Ping Yu (NCI), Rui
Sousa (Univ. Texas Health Science Ctr)
Publications:
1. Guajardo R, Sousa R. A model for the mechanism of polymerase
translocation. J Mol Biol. 1997 Jan 10;265(1):8-19. [PMID 8995520]
2. Guo Q, et al. (2005). Major conformational changes during T7RNAP
transcription initiation coincide with, and are required for, promoter
release. J Mol Biol. 2005 Oct 21;353(2):256-70. [PMID 16169559]
3. Mukherjee S, et al. Structural transitions mediating
transcription initiation by T7 RNA polymerase. Cell. 2002 Jul
12;110(1):81-91. [PMID 12150999]
4. Mentesana PE, et al. Characterization of halted T7 RNA
polymerase elongation complexes reveals multiple factors that
contribute to stability. J Mol Biol. 2000 Oct 6;302(5):1049-62. [PMID
11183774]
Intellectual Property: HHS Reference No. E-119-2013/0--US
Provisional Patent Application No. 61/843,864 filed July 8, 2013
Licensing Contact: Michael Shmilovich, Esq., CLP; 301-435-5019;
[email protected].
[[Page 52936]]
Blood-Based Assay for the Diagnosis and Monitoring of Hyposialylation
Disorders
Description of Technology: Sialic acid, a monosaccharide widely
distributed in glycoproteins and glycolipids, plays an important role
in biological processes such as cellular adhesion, cellular
communication and signal transduction. Reduced levels of sialic acid in
tissues (also known as hyposialylation) affect the function of muscle,
kidney, and other organ systems, and are found in a number of
disorders, such as hereditary inclusion body myopathy (HIBM, also known
as GNE myopathy), renal hyposialylation disorders, and congenital
disorders of glycosylation.
The inventors have developed a sensitive, reliable assay for the
diagnosis of hyposialylation disorders that detects a novel
glycoprotein biomarker in a patient blood sample. This assay has been
validated using samples from patients with GNE myopathy and other
hyposialylation disorders. A distinct advantage of this assay is that
it is minimally invasive, unlike many currently-available methods for
diagnosing hyposialylation disorders, which typically require a tissue
biopsy. In particular, this biomarker represents the first non-invasive
method for diagnosis of renal hyposialylation.
Potential Commercial Applications:
Diagnostic assay to detect hyposialylation
Monitoring tool to track patient response to sialylation-
increasing therapy
Competitive Advantages: A blood-based assay based on this
technology would be less invasive, time-consuming, and costly than a
tissue biopsy, which is the current diagnostic standard for
hyposialylation disorders, particularly kidney disorders.
Development Stage:
Early-stage
In vitro data available
Inventors: Marjan Huizing (NHGRI), William Gahl (NHGRI), Nuria
Carrillo-Carrasco (NCATS)
Intellectual Property: HHS Reference No. E-056-2013/0--U.S.
Application No. 61/785,094 filed 14 Mar 2013
Related Technologies:
HHS Reference No. E-217-2007/0--N-Acetyl Mannosamine as a
Therapeutic Agent
HHS Reference No. E-270-2011/0--Encapsulated N-
Acetylmannosamine or N-Acetylneuraminic Acid to Increase Sialylation
Licensing Contact: Tara Kirby, Ph.D.; 301-435-4426;
[email protected].
Vaccine Adjuvant for Inducing Th17 Focused Response
Description of Technology: Adjuvant selection can be critical to a
vaccine's effectiveness. Ideally, an adjuvant will target and activate
specific immune pathways to increase the magnitude of a response to the
vaccine. A limited range of adjuvants are presently available for human
clinical use; these primarily affect T helper cells 1 and 2 (Th1 and
Th2). Currently, no adjuvants are approved for human use which
primarily affect IL-17-producing T helper cells (Th17) cells. Th17
focused adjuvants may prove critical for developing operative vaccines
against pathogens where Th17 activity is essential for protection. This
technology relates to novel adjuvants activating either caspase-
associated recruitment domain protein 9 (CARD9) or caspase 1 pathways,
or a combination of the two; and methods for using these adjuvants for
stimulating an immune response. These adjuvants induce Th17 focused
stimulation, which may prove essential to development of effective
vaccines against a range of pathogens including bacteria and fungi.
Potential Commercial Applications: Vaccine
Competitive Advantages: Th17 skewing adjuvant
Development Stage: Early-stage
Inventors: Alan Sher (NIAID), Kevin Shenderov (NIAID), Vincenzo
Cerundolo (University of Oxford, U.K.), Gurdyal Besra (University of
Birmingham, U.K.)
Publication: Shenderov K, et al. Cord factor and peptidoglycan
recapitulate the Th17-promoting adjuvant activity of mycobacteria
through mincle/CARD9 signaling and the inflammasome. J Immunol. 2013
Jun 1;190(11):5722-30. [PMID 23630357]
Intellectual Property: HHS Reference No. E-089-2012/0--U.S.
Provisional Patent Application No. 61/709,713 filed October 4, 2012
Licensing Contact: Edward (Tedd) Fenn, J.D.; 424-500-2005;
[email protected].
Collaborative Research Opportunity: The National Institute of
Allergy and Infectious Diseases is seeking statements of capability or
interest from parties interested in collaborative research to further
develop, evaluate or commercialize this technology. For collaboration
opportunities, please contact Richard Kitei at 301-496-2644.
Dated: August 22, 2013.
Richard U. Rodriguez,
Director, Division of Technology Development and Transfer, Office of
Technology Transfer, National Institutes of Health.
[FR Doc. 2013-20888 Filed 8-26-13; 8:45 am]
BILLING CODE 4140-01-P