[Federal Register Volume 72, Number 161 (Tuesday, August 21, 2007)]
[Notices]
[Pages 46642-46646]
From the Federal Register Online via the Government Publishing Office [www.gpo.gov]
[FR Doc No: E7-16401]


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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

[[Page 46643]]

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.

Methods of Glycosylation and Bioconjugation

    Description of Technology: Eukaryotic cells express several classes 
of oligosaccharides attached to proteins or lipids. Animal glycans can 
be N-linked via beta-GlcNAc to Asn (N-glycans), O-linked via -GalNAc to 
Ser/Thr (O-glycans), or can connect the carboxyl end of a protein to a 
phosphatidylinositol unit (GPI-anchors) via a common core glycan 
structure. Beta (1,4)-galactosyltransferase I catalyzes the transfer of 
galactose from the donor, UDP-galactose, to an acceptor, N-
acetylglucosamine, to form a galactose-beta (1,4)-N-acetylglucosamine 
bond, and allows galactose to be linked to an N-acetylglucosamine that 
may itself be linked to a variety of other molecules. Examples of these 
molecules include other sugars and proteins. The reaction can be used 
to make many types of molecules having great biological significance. 
For example, galactose-beta (1,4)-N-acetylglucosamine linkages are 
important for many recognition events that control how cells interact 
with each other in the body, and how cells interact with pathogens. In 
addition, numerous other linkages of this type are also very important 
for cellular recognition and binding events as well as cellular 
interactions with pathogens, such as viruses. Therefore, methods to 
synthesize these types of bonds have many applications in research and 
medicine to develop pharmaceutical agents and improved vaccines that 
can be used to treat disease.
    The invention provides in vitro folding method for a polypeptidyl-
alpha-N-acetylgalactosaminyltransferase (pp-GalNAc-T) that transfers 
GalNAc to Ser/Thr residue on a protein. The application claims that 
this in vitro-folded recombinant ppGalNAc-T enzyme transfers modified 
sugar with a chemical handle to a specific site in the designed C-
terminal polypeptide tag fused to a protein. The invention provides 
methods for engineering a glycoprotein from a biological substrate, and 
methods for glycosylating a biological substrate for use in 
glycoconjugation. Also included in the invention are diagnostic and 
therapeutic uses.
    Application: Enzymes and methods are provided that can be used to 
promote the chemical linkage of biologically important molecules that 
have previously been difficult to link.
    Developmental Status: Enzymes have been synthesized and 
characterization studies have been performed.
    Inventors: Pradman Qasba and Boopathy Ramakrishnan (NCI/SAIC).
    Patent Status: U.S. Provisional Application No. 60/930,294 filed 14 
May 2007 (HHS Reference No. E-204-2007/0-US-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 
is seeking statements of capability or interest from parties interested 
in collaborative research to further develop, evaluate, or 
commercialize this technology. Please contact John D. Hewes, Ph.D. at 
301-435-3121 or [email protected] for more information.

Improved Bacterial Host for Production of Anthrax Toxin Proteins and 
Vaccines: Bacillus anthracis BH450

    Description of Invention: Anthrax toxin has previously been made 
from various avirulent strains of Bacillus anthracis. The inventors 
have genetically engineered a new strain of B. anthracis with improved 
properties. The strain, designated BH450, is totally deficient in the 
ability to make spores and to produce a major extracellular protease 
designated Peptidase M4. The genetic lesions introduced are defined, 
true deletions, so there is no possibility of reversion. Inability to 
make spores assures that laboratories growing the strain will not 
become contaminated with the very stable anthrax spores. Inability to 
make peptidase M4 increases the stability of proteins such as anthrax 
toxin that are secreted to the culture medium.
    Applications and Modality: B. anthracis vaccine/prophylactic and 
therapeutic studies.
    Market: Research tool useful for biodefense/therapeutic studies.
    Development Status: The technology is a research tool.
    Inventors: Andrei Pomerantsev, Dana Hsu, Ramakrishnan Sitaraman, 
Craig Galloway, Violetta Kivovich, Stephen Leppla (NIAID).
    Publication: AP Pomerantsev et al. Genome engineering in Bacillus 
anthracis using Cre recombinase. Infect Immun. 2006 Jan;74(1):682-693.
    Patent Status: HHS Reference No. E-127-2007/0--Research Tool.
    Licensing Status: This technology is not patented. The strain will 
be transferred through a Biological Materials License.
    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 Bacterial Diseases, is 
seeking statements of capability or interest from parties interested in 
collaborative research to further develop, evaluate, or commercialize 
Bacillus anthracis BH450 strain. Please contact Dr. Andrei P. 
Pomerantsev at phone 301-451-9817 and/or e-mail 
[email protected] for more information.

Compositions and Methods for Increasing Recombinant Protein Yields 
Through the Modification of Cellular Properties

    Description of Technology: This technology relates to compositions 
and methods for improving the growth characteristics of cells 
engineered to produce biologically active products such as antibodies 
or glycosylated proteins. Featured is a method that uses gene 
candidates (e.g., cdkl3, siat7e, or lama4), or their expressed or 
inhibited products in cell lines, such as Human Embryonic Kidney 
(including HEK-293), HeLa, or Chinese Hamster Ovary (CHO). The gene 
expression modulates growth characteristics, such as adhesion 
properties, of the cell lines thereby increasing recombinant protein 
yields and reducing product production costs.
    Applications: This technology may be used to improve production of 
therapeutic and/or diagnostic compounds, including therapeutic proteins 
or monoclonal antibodies from mammalian cells. Optimization of 
mammalian cells for use as expression systems in the production of 
biologically active products is very difficult. For certain 
applications, anchorage-independent cell lines may be preferred, 
whereas for other applications, a cell line that adheres to a surface, 
e.g. is anchorage-dependent, may be preferable. This technology 
provides a method for identifying a gene whose expression modulates 
such cellular adhesion characteristics. This method thus leads to an 
increase in the

[[Page 46644]]

expression or yield of polypeptides, including therapeutic biologicals, 
such as antibodies, cytokines, growth factors, enzymes, 
immunomodulators, thrombolytics, glycosylated proteins, secreted 
proteins, and DNA sequences encoding such polypeptides and a reduction 
in the associated costs of such biological products.
    Advantages: This technology offers the ability to improve yields 
and reduce the cost associated with the production of recombinant 
protein products through the selection of cell lines having: altered 
growth characteristics; altered adhesion characteristics; altered rate 
of proliferation; improvement in cell density growth; improvement in 
recombinant protein expression level.
    Market: Biopharmaceuticals, including recombinant therapeutic 
proteins and monoclonal antibody-based products used for in vivo 
medical purposes and nucleic acid based medicinal products now 
represent approximately one in every four new pharmaceuticals on the 
market. The market size has been estimated at $33 billion in 2004 and 
is projected to reach $70 billion by the end of the decade. The list of 
approved biopharmaceuticals includes recombinant hormones and growth 
factors, mAB-based products and therapeutic enzymes as well as 
recombinant vaccines and nucleic acid based products.
    Mammalian cells are widely used expression systems for the 
production of biopharmaceuticals. Human embryo kidney (including HEK-
293) and Chinese hamster ovary (CHO) are host cell of choice. The genes 
identified in this technology (e.g., cdkl3, sia7e, or lama4) can be 
used to modify these important cell based systems.
    This technology is ready for use in drug/vaccine discovery, 
production and development. The technology provides methods for 
identification of specific gene targets useful for altering the 
production properties of either existing cell lines to improve yields 
or with new cell lines for the production of therapeutic and or 
diagnostic compounds from mammalian cells.
    Companies that are actively seeking production platforms based on 
mammalian cell lines that offer high efficiency, high throughput 
systems for protein production or analysis at lower cost and ease of 
scale-up would be potential licensors of this technology.
    Development Status: Late Stage--Ready for Production.
    Inventors: Joseph Shiloach (NIDDK), Pratik Jaluria (NIDDK).
    Related Publication: P. Jaluria et al. Application of microarrays 
to identify and characterize genes involved in attachment dependence in 
HeLa cells. Metab Eng. 2006 Dec 13, Epub ahead of print, doi:10.1016/
j.ymben.2006.12.001.
    Patent Status: U.S. Provisional Application No. 60/840,381 filed 24 
Aug 2006 (HHS Reference No. E-149-2006/0-US-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 Institute of 
Diabetes and Digestive and Kidney Diseases, Biotechnology Core 
Laboratory, is seeking parties interested in collaborative research 
projects directed toward the use of this technology with cells for drug 
and vaccine production and development, including growth optimization, 
production and product recovery processes. For more information, please 
contact Dr. Joseph Shiloach, [email protected], or Rochelle 
S. Blaustein at [email protected].

Methods for Conjugation of Oligosaccharides or Polysaccharides to 
Protein Carriers Through Oxime Linkages Via 3-Deoxy-D-Manno-Octulsonic 
Acid

    Description of Technology: This technology comprises new methods 
for the conjugation of O-specific polysaccharides/oligosaccharides (O-
SP/OS) derived from bacterial lipooligosaccharides/ lipopolysaccharides 
(LOS/LPS), after their cleavage from Lipid A, to carrier proteins, to 
serve as potential vaccines. Conjugation is performed between the 
carbonyl group on the terminal reducing end of the saccharide and the 
aminooxy group of a bifunctional linker bound further to the protein.
    The inventors have carried out the reaction under mild conditions 
and in a short time resulting in binding 3-deoxy-D-manno-octulosonic 
acid (KDO) on the saccharide to the protein. These conjugates preserve 
the external non-reducing end of the saccharide, are recognized by 
antisera, and induce immune responses in mice to both conjugate 
components (i.e., the OS and the associated carrier protein).
    Application: Cost effective and efficient manufacturing of 
conjugate vaccines.
    Inventors: Joanna Kubler-Kielb (NICHD), Vince Pozsgay (NICHD), Gil 
Ben-Menachem (NICHD), Rachel Schneerson (NICHD), et al.
    Patent Status: U.S. Provisional Application No. 60/832,448 filed 21 
Jul 2006 (HHS Reference No. E-183-2005/0-US-01); PCT Patent Application 
filed 21 Jul 2007 (HHS Reference No. E-183-2005/0-PCT-02).
    Licensing Status: Available for exclusive or non-exclusive 
licensing.
    Licensing Contact: Peter A. Soukas, J.D.; 301/435-4646; 
[email protected].

In Vitro Model for Hepatitis C Virion Production

    Description of Technology: This invention provides an in vitro 
hepatitis C virus (HCV) replication system that is capable of producing 
viral particles in a culture medium. Hepatitis C is a major public 
health problem, the development of therapeutics for which has been 
hampered by a lack of a robust model system to study the complete viral 
life cycle. This invention provides a new model system for the complete 
replication cycle of hepatitis C virus and virion production, assembly 
and release. The model is useful for screening antiviral agents against 
HCV.
    A full length HCV construct, CG1b of genotype 1b which is known to 
be infectious, was placed between two ribozymes designed to generate 
the exact 5' and 3' ends of HCV when cleaved. Using this system, HCV 
proteins and positive and negative RNA strands have been shown to 
reproduce intracellularly, and viral particles that resemble authentic 
HCV virions are produced and secreted into the culture medium.
    The patent application includes claims directed toward the 
following: A construct comprising specific nucleic acid sequences 
including HCV genotype 1b, genotype 1a, genotype 2a or potentially 
other genotypes; a method for identifying a cell line that is 
permissive for infection with HCV; a method for propagating HCV in 
vitro; a method for screening agents capable of modulating HCV 
replication or activity; a method for testing the level of HCV 
replication or activity; a HCV vaccine comprising HCV virus particles.
    Applications: The model offers a novel method for investigating the 
entire HCV life cycle including replication and pathogenesis and is 
useful for high-throughput antiviral screening. This technique may also 
be useful for making infectious particles that are useful in the 
production of HCV vaccines.
    Advantages: This system provides a new, stable and efficient cell 
culture model to further study the life cycle and biology of HCV, and 
to test potential therapeutic targets for hepatitis C. This model has 
also been used to generate in cell culture HCV strains infectious for 
chimpanzees, the only experimental animal susceptible to infection with 
the

[[Page 46645]]

hepatitis C virus, a critical step in the development of new vaccines 
for Hepatitis C.
    Market: Hepatitis C virus (HCV) chronically infects approximately 
200 million people worldwide and increases the risk of developing 
cirrhosis and hepatocellular carcinoma. This technology would be useful 
for studying the HCV life cycle, screening for therapeutic agents 
against multiple HCV strains, including Genotype 1a, 1b and 2a, and the 
development of HCV vaccines. HCV genotypes 1 and 2 are the major 
genotypes with worldwide distribution; they are known to be associated 
with different clinical profiles and therapeutic responses. Hence, the 
model may be used to screen for varying levels of effectiveness of 
therapeutics against the major HCV genotypes.
    Development Status: This technology is available for use in 
diagnostics, drug/vaccine discovery, production and development. 
Current work is directed toward studies into the HCV life cycle and 
replication and the pathogenesis of HCV screening for antiviral agents 
against multiple HCV strains. This model has been used to generate in 
cell culture HCV strains infectious for chimpanzees, the only 
experimental animal susceptible to infection with the hepatitis C 
virus, a critical step in the development of new vaccines for Hepatitis 
C. Future work may be directed toward the use of this system for 
development of vaccine candidates against HCV.
    Inventors: T. Jake Liang and Theo Heller (NIDDK).
    Related Publications:
    1. Z. Hu et al. Altered proteolysis and global gene expression in 
hepatitis B virus X transgenic mouse liver. J Virol. 2006 
Feb;80(3):1405-1413.
    2. T. Heller et al. An in vitro model of hepatitis C virion 
production. Proc Natl Acad Sci USA. 2005 Feb 15;102(7):2579-2583.
    Patent Status: PCT Application No. PCT/US2005/035487 filed 30 Sep 
2005 (HHS Reference No. E-324-2004/3-PCT-01), based on: U.S. 
Provisional Application No. 60/615,301 filed 30 Sep 2004 (HHS Reference 
No. E-324-2004/0-US-01), now abandoned; U.S. Provisional Application 
No. 60/642,210 filed 06 Jan 2005 (HHS Reference No. E-324-2004/1-US-
01), now abandoned; U.S. Provisional Application No. 60/720,692 filed 
26 Sep 2005 (HHS Reference No. E-324-2004/2-US-01), now abandoned.
    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 
Diabetes and Digestive and Kidney Diseases, Liver Diseases Branch, is 
seeking parties interested in collaborative research directed toward 
molecular strategies for vaccine and antiviral development, and animal 
models of viral hepatitis C. Please contact Dr. T. Jake Liang at 301-
496-1721, [email protected] or Rochelle S. Blaustein at 
[email protected] for more information.

Monoclonal Antibodies Against Orthopoxviruses

    Description of Invention: Concerns that variola (smallpox) virus 
might be used as a biological weapon have led to the recommendation of 
widespread vaccination with vaccinia virus. While vaccination is 
generally safe and effective for prevention of smallpox, it is well 
documented that various adverse reactions in individuals have been 
caused by vaccination with existing licensed vaccines. Vaccinia immune 
globulin (VIG) prepared from vaccinated humans has historically been 
used to treat adverse reactions arising from vaccinia immunization. 
However, VIG lots may have different potencies and carry the potential 
to transmit other viral agents.
    Chimpanzee Fabs against the B5 and A33 outer extracellular membrane 
proteins of vaccinia virus were isolated and converted into complete 
mAbs with human gamma1 heavy chain constant regions. The two mAbs 
displayed high binding affinities to B5 and A33. The mAbs inhibited the 
spread of vaccinia virus as well as variola virus (the causative agent 
of smallpox) in vitro, protected mice from subsequent intranasal 
challenge with virulent vaccinia virus, protected mice when 
administered 2 days after challenge, and provided significantly greater 
protection than that afforded by VIG.
    Application: Prophylactics or therapeutics against orthopoxviruses.
    Developmental Status: Preclinical studies have been performed.
    Inventors: Zhaochun Chen, Robert Purcell, Suzanne Emerson, Patricia 
Earl, Bernard Moss (NIAID).
    Publications:
    1. Z. Chen et al. Chimpanzee/human mAbs to vaccinia virus B5 
protein neutralize vaccinia and smallpox viruses and protect mice 
against vaccinia virus. Proc Natl Acad Sci USA. 2006 Feb 7;103(6):1882-
1887. Epub 2006 Jan 25.
    2. Z. Chen et al. Characterization of chimpanzee/human monoclonal 
antibodies to the vaccinia A33 glycoprotein and its variola virus 
homolog in vitro and in a vaccinia mouse protection model. J Virol. 
2007 Jun 20; Epub ahead of print, doi 10.1128/JVI.00906-07.
    Patent Status: PCT Patent Application No. PCT/US2006/048832 filed 
22 Dec 2006 (HHS Reference No. E-145-2004/3-PCT-01); PCT Patent 
Application No. PCT/US2006/048833 filed 22 Dec 2006 (HHS Reference No. 
E-145-2004/4-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 Institute of 
Allergy and Infectious Diseases, Laboratory of Infectious Diseases, is 
seeking statements of capability or interest from parties interested in 
collaborative research to further develop, evaluate, or commercialize 
Chimpanzee/human neutralizing monoclonal antibodies against 
orthopoxviruses. Please contact Dr. Robert Purcell at 301-496 5090 for 
more information.

A Method With Increased Yield for Production of Polysaccharide-Protein 
Conjugate Vaccines Using Hydrazide Chemistry

    Description of Technology: Current methods for synthesis and 
manufacturing of polysaccharide-protein conjugate vaccines employ 
conjugation reactions with low efficiency (about twenty percent). This 
means that up to eighty percent of the added activated polysaccharide 
(PS) is lost. In addition, inclusion of a chromatographic process for 
purification of the conjugates from unconjugated PS is required.
    The present invention utilizes the characteristic chemical property 
of hydrazide groups on one reactant to react with aldehyde groups or 
cyanate esters on the other reactant with an improved conjugate yield 
of at least sixty percent. With this conjugation efficiency the 
leftover unconjugated protein and polysaccharide would not need to be 
removed and thus the purification process of the conjugate product can 
be limited to diafiltration to remove the by-products of small 
molecules. The new conjugation reaction can be carried out within one 
or two days with reactant concentrations between 1 and 25 mg/mL at PS/
protein ratios from 1:2 to 3:1, at temperatures between 4 and 40 
degrees Centigrade, and in a pH range of 5.5 to 7.4, optimal conditions 
varying from PS to PS.

[[Page 46646]]

    Application: Cost effective and efficient manufacturing of 
conjugate vaccines.
    Inventors: Che-Hung Robert Lee and Carl E. Frasch (CBER/FDA).
    Patent Status: U.S. Patent Application No. 10/566,899 filed 01 Feb 
2006, claiming priority to 06 Aug 2003 (HHS Reference No. E-301-2003/0-
US-10); U.S. Patent Application No. 10/566,898 filed 01 Feb 2006, 
claiming priority to 06 Aug 2003 (HHS Reference No. E-301-2003/1-US-
02); International rights available.
    Licensing Status: Available for non-exclusive licensing.
    Licensing Contact: Peter A. Soukas, J.D.; 301/435-4646; 
[email protected].

Neutralizing Monoclonal Antibodies to Respiratory Syncytial Virus

    Description of Technology: Respiratory syncytial virus (RSV) is the 
most common cause of bronchiolitis and pneumonia among infants and 
children under 1 year of age. Illness begins most frequently with 
fever, runny nose, cough, and sometimes wheezing. During their first 
RSV infection, between 25% and 40% of infants and young children have 
signs or symptoms of bronchiolitis or pneumonia, and 0.5% to 2% require 
hospitalization. Most children recover from illness in 8 to 15 days. 
The majority of children hospitalized for RSV infection are under 6 
months of age. RSV also causes repeated infections throughout life, 
usually associated with moderate-to-severe cold-like symptoms; however, 
severe lower respiratory tract disease may occur at any age, especially 
among the elderly or among those with compromised cardiac, pulmonary, 
or immune systems.
    This invention is a human monoclonal antibody fragment (Fab) 
discovered utilizing phage display technology. The neutralizing 
monoclonal antibody was isolated and its binding site was identified. 
Fab F2-5 is a broadly reactive fusion (F) protein-specific recombinant 
Fab generated by antigen selection from a random combinatorial library 
displayed on the surface of filamentous phage. In an in vitro plaque-
reduction test, the Fab RSVF2-5 neutralized the infectivity of a 
variety of field isolates representing viruses of both RSV subgroups A 
and B. The Fab recognized an antigenic determinant that differed from 
the only other human anti-F monoclonal antibody (RSV Fab 19) described 
thus far. A single dose of 4.0 mg of Fab RSVF2-5/kg of body weight 
administered by inhalation was sufficient to achieve a 2000-fold 
reduction in pulmonary virus titer in RSV-infected mice. The antigen-
binding domain of Fab RSVF2-5 offers promise as part of a prophylactic 
regimen for RSV infection in humans.
    Application: Respiratory Syncytial Virus prophylaxis/therapeutic.
    Development Stage: The antibodies have been synthesized and 
preclinical studies have been performed.
    Inventors: Brian Murphy (NIAID), Robert Chanock (NIAID), James 
Crowe (NIAID), et al.
    Publication: JE Crowe et al. Isolation of a second recombinant 
human respiratory syncytial virus monoclonal antibody fragment (Fab 
RSVF2-5) that exhibits therapeutic efficacy in vivo. J Infect Dis. 1998 
Apr;177(4):1073-1076.
    Patent Status: HHS Reference No. E-001-1996/0--U.S. and Foreign 
Rights Available.
    Licensing Status: Available for exclusive or non-exclusive 
licensing.
    Licensing Contact: Peter A. Soukas, JD; 301/435-4646; 
[email protected].

Human Neutralizing Monoclonal Antibodies to Respiratory Syncytial Virus 
and Human Neutralizing Antibodies to Respiratory Syncytial Virus

    Description of Technology: This invention is a human monoclonal 
antibody fragment (Fab) discovered utilizing phage display technology. 
It is described in Crowe et al., Proc Natl Acad Sci USA. 1994 Feb 
15;91(4):1386-1390 and Barbas et al., Proc Natl Acad Sci USA. 1992 Nov 
1;89(21):10164-10168. This MAb binds an epitope on the RSV F 
glycoprotein at amino acid 266 with an affinity of approximately 10\9\ 
M-1. This MAb neutralized each of 10 subgroup A and 9 
subgroup B RSV strains with high efficiency. It was effective in 
reducing the amount of RSV in lungs of RSV-infected cotton rats 24 
hours after treatment, and successive treatments caused an even greater 
reduction in the amount of RSV detected.
    Applications: Research and drug development for treatment of 
respiratory syncytial virus.
    Inventors: Robert M. Chanock (NIAID), Brian R. Murphy (NIAID), 
James E. Crowe Jr. (NIAID), et al.
    Patent Status: U.S. Patent 5,762,905 issued 09 June 1998 (HHS 
Reference No. E-032-1993/1-US-01); U.S. Patent 6,685,942 issued 03 
February 2004 (HHS Reference No. E-032-1993/1-US-02); U.S. Patent 
Application No. 10/768,952 filed 29 January 2004 (HHS Reference No. E-
032-1993/1-US-03).
    Licensing Status: Available for non-exclusive licensing.
    Licensing Contact: Peter A. Soukas, JD; 301/435-4646; 
[email protected].

Murine Monoclonal Antibodies Effective To Treat Respiratory Syncytial 
Virus

    Description of Technology: Available for licensing through a 
Biological Materials License Agreement are the murine MAbs described in 
Beeler et al., ``Neutralization epitopes of the F glycoprotein of 
respiratory syncytial virus: effect of mutation upon fusion function,'' 
J Virol. 1989 July;63(7):2941-2950. The MAbs that are available for 
licensing are the following: 1129, 1153, 1142, 1200, 1214, 1237, 1112, 
1269, and 1243. One of these MAbs, 1129, is the basis for a humanized 
murine MAb (see U.S. Patent 5,824,307 to humanized 1129 owned by 
MedImmune, Inc.), recently approved for marketing in the United States. 
MAbs in the panel reported by Beeler et al. have been shown to be 
effective therapeutically when administered into the lungs of cotton 
rats by small-particle aerosol. Among these MAbs several exhibited a 
high affinity (approximately 10\9\ M-1) for the RSV F 
glycoprotein and are directed at epitopes encompassing amino acids 262, 
272, 275, 276 or 389. These epitopes are separate, nonoverlapping and 
distinct from the epitope recognized by the human Fab of U.S. Patent 
5,762,905 owned by The Scripps Research Institute.
    Applications: Research and drug development for treatment of 
respiratory syncytial virus.
    Inventors: Robert M. Chanock, Brian R. Murphy, Judith A. Beeler, 
and Kathleen L. van Wyke Coelingh (NIAID).
    Patent Status: HHS Reference No. B-056-1994/1--Research Tool.
    Licensing Status: Available for non-exclusive licensing under a 
Biological Materials License Agreement.
    Licensing Contact: Peter A. Soukas, JD; 301/435-4646; 
[email protected].

     Dated: August 13, 2007.
Steven M. Ferguson,
Director, Division of Technology Development and Transfer, Office of 
Technology Transfer, National Institutes of Health.
[FR Doc. E7-16401 Filed 8-20-07; 8:45 am]
BILLING CODE 4140-01-P