Source: https://www.federalregister.gov/documents/2010/04/26/2010-9642/government-owned-inventions-availability-for-licensing
Timestamp: 2017-09-21 00:25:29
Document Index: 689219506

Matched Legal Cases: ['Application No. 61', 'Application No. 11', 'Application No. 2005245966', 'Application No. 2567563', 'Application No. 2006', 'Application No. 61']

21636-21638 (3 pages)
Thermostable Y-Family Polymerases From Fungi for Use in Forensic DNA Services and Analysis of Damaged or Ancient DNA
https://www.federalregister.gov/d/2010-9642 https://www.federalregister.gov/d/2010-9642
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 Start Printed Page 2163735 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.
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.
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 jmconrad@mail.nih.gov for more information.
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.
Stimulating immunity to vaccinations, tumors or infections.
Blocking the induction of an immune response in an autoimmune disease or organ transplant rejection.
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.
Pre-clinical stage.
Animal data available.
Inventors: Alan M. Krensky and Carol Clayberger (NCI).
1. Stenger S, Hanson DA, Teitlebaum R, Dewan P, Niazi KR, Froelich CJ, Ganz T, Thoma-Uszynski S, Melián A, Bogdan C, Porcelli SA, Bloom BR, Start Printed Page 21638Krensky 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 Contact: Whitney Hastings, M.S.; 301-451-7337; hastingw@mail.nih.gov.
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 hewesj@mail.nih.gov for more information.
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 naïve human antibody phage display library against Ephrin-B2 and EphB4. These human monoclonal antibodies have high affinity and specificity for Ephrin-B2 and EphB4.
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.
High affinity and antigen specificity.
Bind both soluble ectodomains and cell surface-expressed molecules.
Patent Status: HHS Reference No. E-331-2008/0 & E-331-2008/1—Research Material. Patent protection is not being pursued for this technology.
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 hewesj@mail.nih.gov for more information.
[FR Doc. 2010-9642 Filed 4-23-10; 8:45 am]