[Federal Register Volume 75, Number 79 (Monday, April 26, 2010)]
[Notices]
[Pages 21636-21638]
From the Federal Register Online via the Government Publishing Office [www.gpo.gov]
[FR Doc No: 2010-9642]
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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, Public Health Service, 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 licensing in the U.S. in accordance
with
[[Page 21637]]
35 U.S.C. 207 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.
ADDRESSES: 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.
Thermostable Y-Family Polymerases From Fungi for Use in Forensic DNA
Services and Analysis of Damaged or Ancient DNA
Description of Invention: Y-family polymerases are able to bypass
lesions in DNA that would otherwise block replication by high fidelity
DNA polymerases and are key to the effective study of ancient DNA and
for use in forensic medicine. These enzymes are ubiquitous and are
found in all kingdoms of life: Bacteria, archaea and eukaryotes. The
number of proteins related to the Y-family polymerases is well over 200
orthologs and despite being closely related at the phylogenetic level,
the few polymerases now characterized, each show a unique set of
properties including processivity, fidelity, and the ability to bypass
certain types of DNA. Y-family polymerases from thermostable organisms
are of particular interest because the enzymes isolated from such
species tend to be more stable, easy to work with and may have more
utility in assays at higher temperatures, such as Polymerase Chain
Reaction (PCR). For example, the thermostable archeal Sulfolobus
solfataricus DinB-like polymerase Dpo4 can bypass lesions by generally
inserting the correct complementary nucleotide opposite a variety of
damaged bases and can, under appropriate conditions substitute for Taq
polymerase in PCR applications [Nucleic Acids Res. 2001 Nov
15;29(22):4607-4616; HHS Ref. No. E-232-2001/0]. Additionally,
functional and structural organization of this family of polymerases
permits domain swapping designed to optimize specific properties of use
in novel applications [J Biol Chem. 2004 Jul 30;279(31):32932-32940].
Dr. Woodgate's group at the National Institute of Child Health and
Development have expanded their earlier work (HHS Ref. Nos. E-166-2004/
0,/1, &/2) and have now cloned and expressed full length Y-family
polymerases Thermoascus auranticus Pol eta, Thermomyces lanuginosus Pol
eta, Thermomyces lanuginosus Pol iota, Thermomyces lanuginosus Pol
kappa, Thermomyces lanuginosus REV1, Sporotrichum thermophile Pol eta,
Sporotrichum thermophile Pol iota, Sporotrichum thermophile Pol kappa,
and Sporotrichum thermophile REV1. These full length enzymes may be a
good substitute for Taq polymerase in applications utilizing
fluorescent nucleoside triphosphate derivatives. These lesion-bypassing
polymerases could also be included along with a conventional
thermostable polymerase in a PCR protocol designed to amplify old or
damaged DNA samples which could greatly increase recoverability,
accuracy and length of products. Other applications could include
labelling or tagging DNA, real-time PCR, detection of SNPs, mismatches
or DNA lesions, mutagenic PCR, directed-evolution methods and expanding
the ``DNA alphabet'' utilizing non-natural nucleotides.
Available for licensing are several full length novel Y-family
polymerases. These enzymes and methods should be of interest to
forensic DNA service companies as well as to research reagent companies
pursuing novel thermophilic enzymes for use in ancient and damaged DNA
analysis and for novel applications with modified nucleotides.
Inventors: Roger Woodgate and John P. McDonald (NICHD).
Patent Status: U.S. Provisional Application No. 61/289,901 filed 23
Dec 2009 (HHS Reference No. E-254-2009/0-US-01).
Related Patents and Technologies:
HHS Reference No. E-166-2004/2--
U.S. Patent Application No. 11/596,783 filed 17 Nov 2006.
Australian Patent Application No. 2005245966 filed 20 May
2005.
Canadian Patent Application No. 2567563 filed 20 May 2005.
South African Patent Application No. 2006/10533 filed 20
May 2005.
Licensing Status: Available for licensing.
Licensing Contact: Suryanarayana (Sury) Vepa, Ph.D., J.D.; 301-435-
5020; [email protected].
Collaborative Research Opportunity: The National Institute of Child
Health and Human Development, Laboratory of Genomic Integrity, is
seeking statements of capability or interest from parties interested in
collaborative research to further develop, evaluate, or commercialize
the aforementioned thermostable fungal Y-family DNA polymerases. Please
contact Joseph Conrad, Ph.D. at 301-435-3107 or [email protected]
for more information.
Compositions and Methods for Immunotherapy
Description of Invention: Granulysin is a cytolytic and
proinflammatory molecule expressed by activated human cytotoxic T
lymphocytes (CTLs) and natural killer (NK) cells. It has been
implicated in many of diseases including infection, cancer,
transplantation, autoimmunity, skin and reproductive maladies. Small
synthetic forms of granulysin are being developed as novel antibiotics
and studies suggest that granulysin may be a useful diagnostic
biomarker and/or therapeutic for a wide variety of diseases.
The invention relates to methods of stimulating or enhancing an
immune response using 15 kD granulysin. Investigators at the NIH have
discovered that 15 kD granulysin (but not 9 kD granulysin) activates
monocytes and induces them to differentiate into mature dendritic cells
and activates allospecific T cells. This activation and subsequent
differentiation induced by 15 kD granulysin may prove important in
inducing or regulating immune responses in a host. Consequently, this
invention could be used treat tumors and infections, particularly as an
adjuvant for vaccines and immunotherapies. Further, this technology
could be used to treat autoimmune disorders and organ transplant
rejection.
Applications:
Stimulating immunity to vaccinations, tumors or
infections.
Blocking the induction of an immune response in an
autoimmune disease or organ transplant rejection.
Advantages:
An immune response activator with broad applicability to
the treatment of several diseases, including cancer, atherosclerosis,
diabetes, autoimmune disorders, allergies, and infections.
Co-administering 15kD granulysin could increase the
efficacy of vaccines and immunotherapeutics.
Development Status:
Pre-clinical stage.
Animal data available.
Inventors: Alan M. Krensky and Carol Clayberger (NCI).
Publications:
1. Stenger S, Hanson DA, Teitlebaum R, Dewan P, Niazi KR, Froelich
CJ, Ganz T, Thoma-Uszynski S, Meli[aacute]n A, Bogdan C, Porcelli SA,
Bloom BR,
[[Page 21638]]
Krensky AM, Modlin RL. An antimicrobial activity of cytolytic T cells
mediated by granulysin. Science 1998 Oct 2;282(5386):121-125. [PubMed:
9756476]
2. Krensky AM and Clayberger C. Biology and clinical relevance of
granulysin. Tissue Antigens 2009 Mar;73(3):193-198. [PubMed: 19254247]
Patent Status: U.S. Provisional Application No. 61/250,601 filed 12
Oct 2009 (HHS Reference No. E-158-2009/0-US-01).
Licensing Status: Available for licensing.
Licensing Contact: Whitney Hastings, M.S.; 301-451-7337;
[email protected].
Collaborative Research Opportunity: The Center for Cancer Research,
Laboratory of Cellular and Molecular Biology, is seeking statements of
capability or interest from parties interested in collaborative
research to further develop, evaluate, or commercialize this
technology. Please contact John Hewes, Ph.D. at 301-435-3131 or
[email protected] for more information.
Fully-Human Monoclonal Antibodies Against Human EphrinB2 and EphB4 for
Use in the Study of Cancer Pathogenesis
Description of Invention: Ephrin receptor tyrosine kinases and
their ephrin ligands have been implicated in cancer pathogenesis.
Ephrin receptors and ligands affect tumor growth, invasiveness,
angiogenesis, and metastasis. Ephrin signaling activities in cancer are
complex and are only now beginning to be uncovered.
Researchers at the National Cancer Institute-Frederick, NIH, have
developed a set of five fully-human monoclonal antibodies against human
Ephrin-B2 and Ephrin type-B receptor 4 (``EphB4''). The antibodies were
identified by screening a na[iuml]ve human antibody phage display
library against Ephrin-B2 and EphB4. These human monoclonal antibodies
have high affinity and specificity for Ephrin-B2 and EphB4.
Applications:
Research reagents for in vitro/in vivo investigation of
Ephrin receptor and ligand interactions.
Targeting reagents for in vivo imaging.
Research reagents for protein co-crystallization.
Advantages:
High affinity and antigen specificity.
Bind both soluble ectodomains and cell surface-expressed
molecules.
Inventors: Dimiter S. Dimitrov et al. (NCI).
Patent Status: HHS Reference No. E-331-2008/0 & E-331-2008/1--
Research Material. Patent protection is not being pursued for this
technology.
Licensing Status: Available for licensing.
Licensing Contact: Patrick P. McCue, Ph.D.; 301-435-5560;
[email protected].
Collaborative Research Opportunity: The Center for Cancer Research
Nanobiology Program is seeking statements of capability or interest
from parties interested in collaborative research to further develop,
evaluate, or commercialize this technology. Please contact John Hewes,
Ph.D. at 301-435-3131 or [email protected] for more information.
Dated: April 20, 2010.
Richard U. Rodriguez,
Director, Division of Technology Development and Transfer, Office of
Technology Transfer, National Institutes of Health.
[FR Doc. 2010-9642 Filed 4-23-10; 8:45 am]
BILLING CODE 4140-01-P