[Federal Register Volume 72, Number 200 (Wednesday, October 17, 2007)]
[Notices]
[Pages 58860-58861]
From the Federal Register Online via the Government Publishing Office [www.gpo.gov]
[FR Doc No: E7-20515]


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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.

Alpha 1-3 N-Acetylgalactosaminyltransferases With Altered Donor and 
Acceptor Specificities, Compositions, and Methods of Use

    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 1-3galactosyltransferase (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.
    Application: Development of pharmaceutical agents and improved 
vaccines.
    Developmental Status: Enzymes have been synthesized and preclinical 
studies have been performed.
    Inventors: Pradman Qasba, Boopathy Ramakrishnan, Elizabeth 
Boeggman, Marta Pasek (NCI).
    Patent Status: PCT Patent Application filed 22 Aug 2007 (HHS 
Reference No. E-279-2007/0-PCT-01).
    Licensing Status: Available for exclusive or non-exclusive 
licensing.
    Licensing Contact: Peter A. Soukas, J.D.; 301/435-4646; 
[email protected].
    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, Ph.D. at 301-435-
3121 or [email protected] for more information.

Beta 1,4-Galactosyltransferases With Altered Donor and Acceptor 
Specificities, Compositions and Methods of Use

    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.
    Developmental Status: Enzymes have been synthesized and preclinical 
studies have been performed.

[[Page 58861]]

    Inventors: Pradman Qasba, Boopathy Ramakrishnan, Elizabeth Boeggman 
(NCI).
    Patent Status: PCT Patent Application filed 22 Aug 2007 (HHS 
Reference No. E-280-2007/0-PCT-01).
    Licensing Status: Available for exclusive or non-exclusive 
licensing.
    Licensing Contact: Peter A. Soukas, J.D.; 301/435-4646; 
[email protected]
    Collaborative Research Opportunity: The CCR Nanobiology Program of 
the National Cancer Institute 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, Ph.D., Technology Transfer Specialist, NCI, at 
(301) 435-3121 or [email protected].

Targeting Poly-Gamma-Glutamic Acid to Treat Staphylococcus Epidermidis 
and Related Infections

    Description of Invention: Over the past decade, Staphylococcus 
epidermidis has become the most prevalent pathogen involved in 
nosocomial infections. Usually an innocuous commensal microorganism on 
human skin, this member of the coagulase-negative group of 
staphylococci can cause severe infection after penetration of the 
epidermal protective barriers of the human body. In the U.S. alone, S. 
epidermidis infections on in-dwelling medical devices, which represent 
the main type of infection with S. epidermidis, cost the public health 
system approximately $1 billion per year. Importantly, S. epidermidis 
is frequently resistant to common antibiotics.
    Immunogenic compositions and methods for eliciting an immune 
response against S. epidermidis and other related staphylococci are 
claimed. The immunogenic compositions can include immunogenic 
conjugates of poly-[gamma]-glutamic acid (such as [gamma]DLPGA) 
polypeptides of S. epidermidis, or related staphylococci that express a 
[gamma]PGA polypeptide. The [gamma]PGA conjugates elicit an effective 
immune response against S. epidermidis, or other staphylococci, in 
subjects to which the conjugates are administered. A method of treating 
an infection caused by a Staphylococcus organism that expresses cap 
genes is also disclosed. The method can include selecting a subject who 
is at risk of or has been diagnosed with the infection by the 
Staphylococcus organism which expresses [gamma]PGA from the cap genes. 
Further, the expression of a [gamma]PGA polypeptide by the organism can 
then be altered.
    Application: Prophylactics against S. epidermidis.
    Developmental Status: Preclinical studies have been performed.
    Inventors: Michael Otto, Stanislava Kocianova, Cuong Vuong, Jovanka 
Voyich, Yufeng Yao, Frank DeLeo (NIAID)
    Publication: S Kocianova et al. Key role of poly-gamma-DL-glutamic 
acid in immune evasion and virulence of Staphylococcus epidermidis. J 
Clin Invest. 2005 Mar;115(3):688-694.
    Patent Status: PCT Patent Application No. PCT/US2006/026900 filed 
10 Jul 2006 (HHS Reference No. E-263-2005/0-PCT-02).
    Licensing Status: Available for exclusive or non-exclusive 
licensing.
    Licensing Contact: Peter A. Soukas, J.D.; 301/435-4646; 
[email protected]
    Collaborative Research Opportunity: The National Institute of 
Allergy and Infectious Diseases, Laboratory of Human Bacterial 
Pathogenesis, is seeking statements of capability or interest from 
parties interested in collaborative research to further develop, 
evaluate, or commercialize the use of poly-[gamma]-glutamic acid of 
staphylococci. Please contact Dr. Michael Otto at [email protected] 
for more information.

    Dated: October 10, 2007.
Steven M. Ferguson,
Director, Division of Technology Development and Transfer, Office of 
Technology Transfer, National Institutes of Health.
[FR Doc. E7-20515 Filed 10-16-07; 8:45 am]
BILLING CODE 4140-01-P