[Federal Register Volume 75, Number 35 (Tuesday, February 23, 2010)]
[Notices]
[Pages 8082-8083]
From the Federal Register Online via the Government Publishing Office [www.gpo.gov]
[FR Doc No: 2010-3450]


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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 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.

Automated Computer-Aided Polyp Detection for Computed Tomography 
Colonography (Virtual Colonoscopy)

    Description of Invention: This invention describes an automated 
method for colon registration from supine and prone scans that combines 
the use of Computed Tomographic Colonography (CTC) and Computer Aided 
Detection (CAD) software. Currently, in order to detect colonic polyps, 
patients are scanned twice--once in the supine, and again in the prone 
positions. This approach improves CTC sensitivity by reducing the 
extent of non-interpretable collapsed or fluid-filled segments. In 
order to assist radiologists in interpreting CTC data or evaluating 
colonic polyp candidates detected by CAD in both scans, it is important 
to provide not only the locations of suspicious polyps, but also the 
possible matched pairs (correspondences) of polyps in these scans. To 
achieve this, the two scans need to be aligned. In this invention, the 
colon registration problem is formulated as time series matching along 
the centerline of the colon. Anatomically salient points on the colon 
are initially distinguished as they can be viewed as landmarks along 
the central path of the colon. Correlation optimized warping is then 
applied to the segments defined by the anatomical landmarks to find 
better global registration based on the local correlation of segments.
    When CTC is performed in conjunction with CAD software, screening 
may become easier on patients, less time-consuming, and more accurate. 
The effectiveness of the method was verified in experiments in which 
the polyp location was used as a measure for the registration error. 
The algorithm was tested on a CTC dataset of 12 patients with 14 
polyps. Experimental results showed that by using this method, the 
estimation error of polyp location could be reduced 60.4% (from 47.2mm 
to18.7mm on average) compared to a traditional method based on dynamic 
time warping.
    Colon cancer is the second leading cause of cancer-related deaths 
in the United States, and the method used in this invention will aid in 
effective early detection of the disease, which will have a significant 
impact on its prognosis.
    Applications: Efficient and robust detection of colon cancer.
    Development Status: Early stage.
    Inventors: Ronald M. Summers et al. (NIHCC).
    Related Publication: Huang A, Roy D, Franaszek M, Summers RM. 
Teniae coli guided navigation and registration for virtual colonoscopy. 
Visualization, 2005. VIS 05. IEEE, pp. 279-285, 23-28 Oct 2005; doi 
10.1109/VISUAL.2005.1532806.
    Patent Status: U.S. Patent Application No. 61/220,481 filed June 
25, 2009 (HHS Reference No. E-135-2009/0-US-01).
    Licensing Status: Available for licensing.

[[Page 8083]]

    Licensing Contact: Jeffrey A. James, Ph.D.; 301-435-5474; 
<a href="/cdn-cgi/l/email-protection#137976757561766a7972537e727a7f3d7d7a7b3d747c65"><span class="__cf_email__" data-cfemail="18727d7e7e6a7d617279587579717436767170367f776e">[email protected]</span></a>.

Alpha 1-3 N-Acetylgalactosaminyltransferases With Altered Donor and 
Acceptor Specificities, Compositions, and Methods of Use: Development 
of Pharmaceutical Agents and Improved Vaccines

    Description of Invention: The present invention relates to the 
field of glycobiology, specifically to glycosyltransferases. The 
present invention provides structure-based design of novel 
glycosyltransferases and their biological applications.
    The structural information of glycosyltransferases has revealed 
that the specificity of the sugar donor in these enzymes is determined 
by a few residues in the sugar-nucleotide binding pocket of the enzyme, 
which is conserved among the family members from different species. 
This conservation has made it possible to reengineer the existing 
glycosyltransferases with broader sugar donor specificities. Mutation 
of these residues generates novel glycosyltransferases that can 
transfer a sugar residue with a chemically reactive functional group to 
N-acetylglucosarnine (GlcNAc), galactose (Gal) and xylose residues of 
glycoproteins, glycolipids and proteoglycans (glycoconjugates). Thus, 
there is potential to develop mutant glycosyltransferases to produce 
glycoconjugates carrying sugar moieties with reactive groups that can 
be used in the assembly of bio-nanoparticles to develop targeted-drug 
delivery systems or contrast agents for medical uses.
    Accordingly, methods to synthesize N-acetylglucosamine linkages 
have many applications in research and medicine, including in the 
development of pharmaceutical agents and improved vaccines that can be 
used to treat disease.
    This application claims compositions and methods based on the 
structure-based design of alpha 1-3 N-Acetylgalactosaminyltransferase 
(alpha 3 GalNAc-T) mutants from alpha l-3galactosyltransferase (a3Gal-
T) that can transfer 2'-modified galactose from the corresponding UDP-
derivatives due to mutations that broaden the alpha 3Gal-T donor 
specificity and make the enzyme alpha3 GalNAc-T.
    Applications: Development of pharmaceutical agents and improved 
vaccines.
    Development Status: Enzymes have been synthesized and preclinical 
studies have been performed.
    Inventors: Pradman Qasba, Boopathy Ramakrishnan, Elizabeth 
Boeggeman, Marta Pasek (NCI).
    Patent Status: PCT Application No. PCT/US2007/018678 filed August 
22, 2007, which published as WO 2009/025646 on February 26, 2009 (HHS 
Reference No. E-279-2007/0-PCT-01).
    Licensing Status: Available for licensing.
    Licensing Contact: John Stansberry, PhD; 301-435-5236; 
<a href="/cdn-cgi/l/email-protection#196a6d78776a7b7c73597478707537777071377e766f"><span class="__cf_email__" data-cfemail="c4b7b0a5aab7a6a1ae84a9a5ada8eaaaadaceaa3abb2">[email protected]</span></a>.
    Collaborative Research Opportunity: The National Cancer Institute's 
Nanobiology Program is seeking statements of capability or interest 
from parties interested in collaborative research to further develop, 
evaluate, or commercialize structure-based design of novel 
glycosyltransferases. Please contact John D. Hewes, PhD at 301-435-3121 
or <a href="/cdn-cgi/l/email-protection#b6ded3c1d3c5dcf6dbd7dfda98d8dfde98d1d9c0"><span class="__cf_email__" data-cfemail="c7afa2b0a2b4ad87aaa6aeabe9a9aeafe9a0a8b1">[email protected]</span></a> for more information.

Beta 1,4-Galactosyltransferases With Altered Donor and Acceptor 
Specificities, Compositions and Methods of Use: Development of 
Pharmaceuticals and Improved Vaccines

    Description of Invention: The present invention relates to the 
field of glycobiology, specifically to glycosyltransferases. The 
present invention provides structure-based design of novel 
glycosyltransferases and their biological applications.
    The structural information of glycosyltransferases has revealed 
that the specificity of the sugar donor in these enzymes is determined 
by a few residues in the sugar-nucleotide binding pocket of the enzyme, 
which is conserved among the family members from different species. 
This conservation has made it possible to reengineer the existing 
glycosyltransferases with broader sugar donor specificities. Mutation 
of these residues generates novel glycosyltransferases that can 
transfer a sugar residue with a chemically reactive functional group to 
N-acetylglucosarnine (GlcNAc), galactose (Gal) and xylose residues of 
glycoproteins, glycolipids and proteoglycans (glycoconjugates). Thus, 
there is potential to develop mutant glycosyltransferases to produce 
glycoconjugates carrying sugar moieties with reactive groups that can 
be used in the assembly of bio-nanoparticles to develop targeted-drug 
delivery systems or contrast agents for medical uses.
    Accordingly, methods to synthesize N-acetylglucosamine linkages 
have many applications in research and medicine, including in the 
development of pharmaceutical agents and improved vaccines that can be 
used to treat disease.
    The invention claims beta (1,4)-galactosyltransferase I mutants 
having altered donor and acceptor and metal ion specificities, and 
methods of use thereof. In addition, the invention claims methods for 
synthesizing oligosaccharides using the beta (1,4)-
galactosyltransferase I mutants and to using the beta (1,4)-
galactosyltransferase I mutants to conjugate agents, such as 
therapeutic agents or diagnostic agents, to acceptor molecules. More 
specifically, the invention claims a double mutant beta 1, 4 
galactosyltransferase, human beta-1, 4-Tyr289Leu-Met344His-Gal-T1, 
constructed from the individual mutants, Tyr289Leu-Gal-T1 and 
Met344His-Gal-T1, that transfers modified galactose in the presence of 
magnesium ion, in contrast to the wild-type enzyme which requires 
manganese ion.
    Application: Development of pharmaceutical agents and improved 
vaccines.
    Development Status: Enzymes have been synthesized and preclinical 
studies have been performed.
    Inventors: Pradman Qasba, Boopathy Ramakrishnan, Elizabeth 
Boeggeman (NCI).
    Patent Status: PCT Application No. PCT/US2007/018656 filed August 
22, 2007, which published as WO 2009/025645 on February 26, 2009 (HHS 
Reference No. E-280-2007/0-PCT-01).
    Licensing Status: Available for licensing.
    Licensing Contact: John Stansberry, PhD; 301-435-5236; 
<a href="/cdn-cgi/l/email-protection#582b2c39362b3a3d32183539313476363130763f372e"><span class="__cf_email__" data-cfemail="1e6d6a7f706d7c7b745e737f77723070777630797168">[email protected]</span></a>.
    Collaborative Research Opportunity: The National Cancer Institute's 
Nanobiology Program is seeking statements of capability or interest 
from parties interested in collaborative research to further develop, 
evaluate, or commercialize glycosyltransferases. Please contact John D. 
Hewes, PhD at 301-435-3121 or <a href="/cdn-cgi/l/email-protection#224a4755475148624f434b4e0c4c4b4a0c454d54"><span class="__cf_email__" data-cfemail="066e637163756c466b676f6a28686f6e28616970">[email protected]</span></a> for more information.

    Dated: February 4, 2010.
Richard U. Rodriguez,
Director, Division of Technology Development and Transfer, Office of 
Technology Transfer, National Institutes of Health.
[FR Doc. 2010-3450 Filed 2-22-10; 8:45 am]
BILLING CODE 4140-01-P


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