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Government-Owned Inventions; Availability for Licensing

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AGENCY:

National Institutes of Health, Public Health Service, DHHS.

ACTION:

Notice.

SUMMARY:

The inventions listed below are owned by agencies 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 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.

Development of a Novel High Throughput Assay To Measure Cell Infection With Vaccinia Strains Expressing Reporter Genes

Hana Golding (FDA).

U.S. Provisional Patent Application 60/429,767 filed 27 Nov 2002.

Licensing Contact: Peter Soukas; 301/435-4646; soukasp@od.nih.gov.

Critical to developing a vaccine against viral infections is an assay to measure the neutralizing antibody present in blood of vaccine recipients. The currently available tests are labor intensive and require 5-6 days to complete. The inventors have designed a high throughput vaccinia neutralization assay, which offers several advantages over the assays that are currently used. It is completed in as little as 24 hours, it is sensitive, highly reproducible, requires only 50 μl of plasma and uses automated readout. This assay is based on the use of recombinant vaccinia virus (vSC56) expressing a bacterial gene coding for the enzyme b-galactosidase (b-Gal) under the control of a synthetic early/late promotor. Another recombinant virus expressing an inducible reporter gene (EGFP) is also being tested in neutralization assay. These assays may be of value in the clinical trials of new smallpox vaccines, for evaluations of new vaccinia immunoglobulin (VIG) and anti-viral agents under development. The technology itself may be adapted for construction of neutralization assays for other viruses and intracellular pathogens.

Method of Separating Recombinant Immunotoxin

Hua Jiang et al. (NCI).

DHHS Reference No. E-209-2002/0-US-01 filed 07 Nov 2002.Start Printed Page 12915

Licensing Contact: Jonathan Dixon; 301/435-5559; dixonj@od.nih.gov.

Over the past several years, dsFv-immunotoxins have generated significant interest in the research and commercial communities, as they have been shown to me more useful in certain therapeutic applications over intact antibody-immunotoxins and Fv-immunotoxins. dsFv-immunotoxins are created when a single-chain variable domain-toxin conjugate is associated with the complementary single-chain variable domain via one or more disulfide bonds to form a “disulfide-stabilized” Fv (dsFv)-immunotoxin.

Separation of dsFv-immunotoxin from its single-chain variable domain subunits (and any other contaminants) has thus far been achieved through a low yielding and relatively expensive process. The present invention discloses a new method of purifying dsFv-immunotoxins that has shown a three-fold increase in yield while at the same time keeping costs at a commercially reasonable level. As the demand for dsFv-immunotoxins increases, this method will give companies the ability to purify sufficient quantities to support their clinical trials and make their way to the commercial marketplace.

Optimization of Cardiac Contraction by Novel Human Kinase Mediated Differential Phosphorylation of Myosin

Dr. Neal D. Epstein (NHLBI).

DHHS Reference Nos. E-261-00/0 filed 12 Sep 2000 and E-261-00/2 filed 12 Sep 2001.

Licensing Contact: Fatima Sayyid; 301/435-4521; sayyidf@od.nih.gov.

This invention relates to the development of drugs that provide novel therapeutic interventions to increase the efficiency of failing hearts. It describes the cloning of the active cardiac kinase which modified the cardiac stretch-activation response and myofiber tension via phosphorylation of the beta myosin light chain molecules. These molecules are differentially phosphorylated by this kinase as a function of location to produce the spatial variation in myofiber mechanics that optimize cardiac torsion. The data in this invention indicate that targeting this cardiac light chain kinase could yield novel therapeutics to increase the efficiency of hearts failing from a variety of causes. This approach represents an alternative to present day therapeutics such as calcium blocking agents or digoxin, and thus may have the added benefit of providing therapeutics that are synergistic with present treatments.

This invention is described, in part, in Davis et al., Cell 2001 Nov 30; 107(5):631-41.

Methods of Screening for Risk of Cancer Using Human Lactoferrin DNA Probe or Primer

Christina Teng and Timothy Panella (NIEHS).

U.S. Patent 5,948,613 issued 07 Sep 1999.

Licensing Contact: Marlene Shinn-Astor; 301/435-4426; shinnm@od.nih.gov.

While normal breast ductal epithelium and neutrophilic granulocytes contain lactoferrin, their malignant counterparts frequently do not. The NIH announces primers or probes corresponding to the human lactoferrin gene, its promoter region, and its protein product, obtained from human breast tissue. The lactoferrin primer or probes can be used to screen for malignancy arising from tissues that normally secrete lactferrin, or as a test to check the recovery of a patient from a malignancy.

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Dated: March 5, 2003.

Steven M. Ferguson,

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

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[FR Doc. 03-6366 Filed 3-17-03; 8:45 am]

BILLING CODE 4140-01-P