[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