[Federal Register: August 21, 2007 (Volume 72, Number 161)]
[Notices]
[Page 46642-46646]
From the Federal Register Online via GPO Access [wais.access.gpo.gov]
[DOCID:fr21au07-82]
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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;
soukasp@mail.nih.gov.
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 hewesj@mail.nih.gov 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;
soukasp@mail.nih.gov.
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
apomerantsev@niaid.nih.gov 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;
soukasp@mail.nih.gov.
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, josephs@intra.niddk.nih.gov, or Rochelle
S. Blaustein at Rochelle.Blaustein@nih.gov.
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;
soukasp@mail.nih.gov.
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;
soukasp@mail.nih.gov.
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,
jliang@nih.gov or Rochelle S. Blaustein at Rochelle.Blaustein@nih.gov 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;
soukasp@mail.nih.gov
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;
soukasp@mail.nih.gov.
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;
soukasp@mail.nih.gov.
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;
soukasp@mail.nih.gov.
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;
soukasp@mail.nih.gov.
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