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Government-Owned Inventions; Availability for Licensing

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National Institutes of Health, Public Health Service, DHHS.




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 35 U.S.C. 207 to achieve expeditious commercialization of results of federally-funded research and Start Printed Page 52404development. Foreign patent applications are filed on selected inventions to extend market coverage for companies and may also be available for licensing.


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.

Method for Inducing T-Cell Proliferation

Warren J. Leonard et al. (NHLBI).

U.S. Provisional Application No. 60/555,898 filed 23 Mar 2004 (HHS Reference No. E-104-2004/0-US-01); U.S. Utility Application No. 11/084,408, filed 18 Mar 2005 (HHS Reference No. E-104-2004/0-US-02).

Licensing Contact: Susan Ano; 301/435-5515;

This technology relates to the use of thymic stromal lymphopoietin (TSLP) or TSLP agonists to induce CD4+ T cell proliferation as well as the use of TSLP antagonists to treat IgE-mediated disorders such as asthma or allergies. The T cell proliferation application of this technology could be of particular relevance for patients in whom this cell population has been significantly reduced by e.g., HIV/AIDS infection or another condition resulting in immunodeficiency. The patent application describes methods of treating individuals afflicted with an immunodeficiency by administering CD4+ T cells that have been isolated and induced to proliferate using TSLP or by direct administration of TSLP or a nucleic acid encoding TSLP. The need for appropriate treatment methods for conditions such as asthma and allergies are well recognized. The patent application describes administration of a TSLP antagonist to an individual suffering from an IgE-mediated disorder to remove or lessen the symptoms. TSLPR knockout mice are also described in the patent application and available for licensing through a biological materials license agreement.

Vaccines Using Universally Inactivated Viruses, Parasites, and Tumor Cells

Yossef Raviv et al. (NCI).

U.S. Provisional Application filed 22 Mar 2004 (HHS Reference No. E-303-2003/0-US-01); PCT Application filed 22 Mar 2005 (HHS Reference No. E-303-2003/0-PCT-02).

Licensing Contact: Susan Ano; 301/435-5515;

The current technology describes the universal inactivation of viruses, parasites, and tumor cells by hydrophobic, photoactivatable compounds. These non-toxic compounds, such as 1,5-iodoanpthylazide (INA), will selectively accumulate in the innermost regions of biological membrane bilayers, where the compounds will bind to proteins and lipids upon irradiation with light, thus inactivating deeply embedded proteins while maintaining integrity and activity of the proteins on the surface. This inactivation preserves the structural and conformational integrity and therefore immunogenicity of the agent in question, which overcomes a potential problem associated with some other vaccines such as those containing killed pathogens. As representative examples, the patent application describes experimental results obtained using HIV, SIV, and Ebola viruses. The inactivation approach presented in this technology provides for a safe, non-infectious composition for vaccination against the corresponding agent, whereas some vaccines, such as those involving live-attenuated microbial agents, still have a risk of infectivity associated with them.

In addition to licensing, the technology is available for further development through collaborative research opportunities with the inventors.

High Expression Level Vectors Combining of mRNA Transport Elements for Use in Mammalian Cells

Barbara K. Felber et al. (NCI).

U.S. Provisional Application No. 60/471,988 filed 19 May 2003 (HHS Reference No. E-223-2003/0-US-01); U.S. Provisional Application No. 60/472,223, filed 20 May 2003 (HHS Reference No. E-258-2003/0-US-01); PCT Application No. PCT/US04/15776 filed 19 May 2004, which published as WO2004/113547 on 29 Dec 2004 (HHS Reference No. E-223-2003/1-PCT-01).

Licensing Contact: Susan Ano; 301/435-5515;

This technology relates to improving levels of gene expression using a combination of a constitutive RNA transport element (CTE) with a mutant form of another RNA transport element (RTE). The combination of these elements results in a synergistic effect on stability of mRNA transcripts, which in turn leads to increased expression levels. Using HIV-1 gag as reporter mRNA, one mutated RTE in combination with a CTE was found to improve expression of unstable mRNA by about 500-fold. Similarly this combination of elements lead to synergistically elevated levels of HIV-1 Env expression. The function of CTEs and RTEs is conserved in mammalian cells, so this technology is a simple and useful way of obtaining high levels of expression of otherwise poorly expressed genes and can be used in a number of applications such as but not limited to improvements of gene therapy vectors, expression vectors for mammalian cells.

In addition to licensing, the technology is available for further development through collaborative research opportunities with the inventors.

Recombinant Plasmids Containing HIV Reverse Transcriptase

Stephen H. Hughes and Paul L. Boyer (NCI).

HHS Reference Nos. E-034-1991/0, /1, /2, /3, and /4—Research Tools.

Licensing Contact: Sally Hu; 301/435-5606;

NIH offers below HIV-1 Reverse Transcriptase (RT) Expression plasmids that are available for licensing via biological material licenses (BML). In an appropriate strain of E. coli, these plasmids cause the expression of an HIV-1 RT heterodimer (p66/p51). In the expression plasmid, the RT coding region is flanked by synthetic initiation and termination codons. The amino terminus of the RT made in E. coli has two additional amino acids relative to the viral enzyme (MV); these have no obvious effect on enzymatic activity. The carboxy terminus of p66 carries a 6-histidine tag that facilitates purification. The plasmid also causes the expression of a low level of HIV-1 protease; this leads to the conversion of the approximately half of the p66 synthesized in E. coli to p51. The p66/p51 heterodimer can be easily extracted from the E. coli host and purified by metal-chelate chromatography. Expression constructs for many of the common drug-resistant versions of HIV-1 RT (a partial list is given below) and for a number of other mutants are available. Alternate RT expression plasmids that encode versions of HIV-1 RT that do not have his tags and plasmids that separately encode p51 and p66 (allowing subunit selective mutagenesis) are also available. The HIV-1 RT expression plasmids can be used to generate wild-type and drug resistant RTs that can be used in both biological and medical research. The RTs are particularly useful in the screening and development of RT Start Printed Page 52405inhibitors in vitro and can be used to test drug candidates for their effectiveness against common drug resistant mutants of HIV-1 RT. Please contact Dr. Hughes directly ( if you want additional information about RT expression plasmids that are not listed below.

VectorDescriptionReference No.
Wild-type HIV-1 RTfull length, wild typeE-034-1991/0
L100INNRTI resistantE-034-1991/1
K103NNNRTI resistantE-034-1991/1
V106ANNRTI resistantE-034-1991/1
E138KNNRTI resistantE-034-1991/1
Y181CNNRTI resistantE-034-1991/1
Y188HNNRTI resistantE-034-1991/1
P236LNNRTI resistantE-034-1991/1
RTs that carry some combinations of NNRTI mutations, e.g., K103N+Y181I, are also available.
K65RNRTI resistantE-034-1991/2
L74VNRTI resistantE-034-1991/1
M184ILamivudine (3TC) resistant
M184VLamivudine (3TC) resistantE-034-1991/1
AZT-R (5 mutations)AZT resistantE-034-1991/1
Δ67 complexMulti-NRTI resistantE-034-1991/4
Q151MMulti-NRTI resistantE-034-1991/4
Q151M ComplexMulti-NRTI resistantE-034-1991/4
SSGR/T215YMulti-NRTI resistantE-034-1991/4
SSSR/T215YMulti-NRTI resistantE-034-1991/4
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Dated: August 20, 2005.

Steven M. Ferguson,

Director, Division of Technology Development and Transfer, Office of Technology Transfer, National Institutes of Health.

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[FR Doc. 05-17517 Filed 9-1-05; 8:45 am]