[Federal Register Volume 66, Number 14 (Monday, January 22, 2001)]
[Notices]
[Pages 6637-6638]
From the Federal Register Online via the Government Publishing Office [www.gpo.gov]
[FR Doc No: 01-1643]


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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, DHHS.

ACTION: Notice.

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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.

ADDRESS: 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.

Ribonuclease H1--A Protein Expressed in Escherichia coli From a 
Cloned Human RNase H1 cDNA

Robert J. Crouch, Susana Cerritelli, Sergey Gaidamakov, and Hirofumi 
Yamada (NICHD)
DHHS Reference No. E-047-01/0
    Licensing Contact: Sally Hu; 301/496-7056 ext. 265; e-mail: 
<a href="/cdn-cgi/l/email-protection#fb938e88bb949fd5959293d59c948d"><span class="__cf_email__" data-cfemail="f29a8781b29d96dc9c9b9adc959d84">[email protected]</span></a>.
    Available for licensing through a Materials License Agreement (no 
patent or patent application) are samples of purified human RNase H1 
protein, expressed in E. coli from human RNase H1 cDNA. This protein is 
important for cellular functions such as DNA synthesis and repair. This 
protein also is related by sequence, structure and enzymatic mechanism 
to the RNase H of retroviruses such as HIV. Since the cellular and 
viral proteins have similar properties, it would be useful to screen 
for potential drugs that have little or only modest effects on the 
cellular protein while inhibiting the HIV enzyme. Thus, the 
availability of both the retroviral and human RNases H1 makes drug 
screening and anti-sense therapy possible to perform.

Methods for the Identification of Textual and Physical Structured 
Query Fragments for the Analysis of Textual and Biopolymer 
Information

Robert J. Boissy (NIEHS)
DHHS Reference No. E-270-99/0 filed 15 Nov 2000
    Licensing Contact: Dale Berkley; 301/496-7735 ext. 223; e-mail: 
<a href="/cdn-cgi/l/email-protection#751710071e19100c11351a115b1b1c1d5b121a03"><span class="__cf_email__" data-cfemail="e18384938a8d849885a18e85cf8f8889cf868e97">[email protected]</span></a>.
    The invention comprises algorithms implemented in software for 
``structured combinatorial queries'' that may be used for analyses of 
relatedness and information content in any textual information, and 
especially in biological sequences. The invention also includes 
experimental methods for isolating and comparing DNA fragments 
(``Structured Query Fragments'' or SQFs) obtained using site-specific 
cleavage effectors acting on substrate DNA that is asymmetrically end-
immobilized on a solid support. A small, structured array of such 
cleavage effectors may be used in a combinatorial fashion to generate 
progressively expanding sets of asymmetrically end-immobilized, double-
stranded DNA. This ultimately yields extremely large numbers of SQFs, 
which typically have lengths in the range of 100-700 nucleotides (and 
are termed ranged SQFs). Thus, each SQF is defined by a method (a 
specific combinatorial pathway required to isolate it) and one or more 
properties (typically its length). These attributes yield sufficient 
information to identify and assign ranged SQFs to specific locations in 
known sequences automatically using the software disclosed in the 
invention. The invention shows how millions of individual ranged SQFs 
distributed throughout the human genome may be unambiguously identified 
at nucleotide resolution using a fragment analysis instrument. 
Accordingly, the invention provides a computational method that is 
flexible and efficient at comparing large amounts of textual 
information (typically biological sequence data), and a unique 
laboratory strategy that emulates the computational method and provides 
a highly scalable approach for physical analyses of polynucleotides. 
This laboratory strategy allows for the analysis and isolation of large 
numbers

[[Page 6638]]

of specific SQFs of interest, without the use of cloning techniques or 
polynucleotide amplification protocols that require locus-specific 
primers.

Probe Using Diffuse-Reflectance Spectroscopy

Amir H. Gandjbakhche (NICHD), David W. Hattery (NICHD), James L. 
Mulshine (NCI), Paul D. Smith (ORS), Ernie Hawk (NCI), Victor 
Chernomordik (NICHD)
DHHS Reference No. E-309-00/0 filed 06 Oct 2000
    Licensing Contact: Dale Berkley; 301/496-7735 ext. 223; e-mail: 
<a href="/cdn-cgi/l/email-protection#f89a9d8a93949d819cb8979cd6969190d69f978e"><span class="__cf_email__" data-cfemail="d6b4b3a4bdbab3afb296b9b2f8b8bfbef8b1b9a0">[email protected]</span></a>.
    The invention uses an oblique angle reflectance spectroscopy method 
to non-invasively quantify the thickness of the oral epithelium as a 
means for quantifying inflammation at sites in the oral cavity. In this 
technique, a toothbrush-sized probe is used to direct photon sources at 
two or more oblique angles and measure the scattered spectra to 
determine the thickness of the epithelial layer. Analysis of the 
spectra provides the location of the stroma/epithelium interface. The 
invention has applications in the assessment of drugs used in the 
treatment of Leukoplakia, which is characterized by a thickening of the 
oral epithelium as the underlying stroma remains unchanged. The 
invention provides a non-invasive technique for determining the 
efficacy of drugs used to treat the lesion, and promises to replace the 
need for uncomfortable punch biopsies.

Modified HCV Peptide Vaccine

Jay A. Berzofsky (NCI), Pablo Sarobe (NCI), CD Pendleton (NCI), Stephen 
M. Feinstone (FDA)
DHHS Reference Nos. E-192-98/0 filed 21 Aug 1998 and E-192-98/1 filed 
17 Aug 1999
    Licensing Contact: Carol Salata; 301/496-7735 ext. 232; e-mail: 
<a href="/cdn-cgi/l/email-protection#ea998b868b9e8b89aa858ec4848382c48d859c"><span class="__cf_email__" data-cfemail="9eedfff2ffeafffddef1fab0f0f7f6b0f9f1e8">[email protected]</span></a>.
    Hepatitis C virus (HCV) is a single stranded RNA virus responsible 
for the majority of non-A non-B hepatitis. Hepatitis C virus (HCV) has 
a worldwide distribution and is a major cause of liver cirrhosis and 
hepatocellular carcinoma in the U.S., Europe, and Japan. For this 
reason, development of a vaccine against hepatitis C is of great 
importance.
    The present invention provides immunogenic peptides of HCV core 
protein which elicit an enhanced immune response, methods for making 
these peptides, and methods for using these peptides for a variety of 
therapeutic, diagnostic, and prognostic applications, including a 
vaccine. More specifically, the present invention provides an isolated 
peptide, an isolated HCV core polypeptide, a fragment of an HCV core 
polypeptide and nucleic acids which encode the peptides and 
polypeptides of this invention. The invention provides a modified HCV 
core peptide that is more immunogenic than the corresponding natural 
core peptide for eliciting human cytotoxic T lymphocytes.

    Dated: January 8, 2001.
Jack Spiegel,
Director, Division of Technology Development and Transfer, Office of 
Technology Transfer, National Institutes of Health.
[FR Doc. 01-1643 Filed 1-19-01; 8:45 am]
BILLING CODE 4140-01-P


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