Government-Owned Inventions; Availability for Licensing, 60442-60444 [2012-24251]
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60442
Federal Register / Vol. 77, No. 192 / Wednesday, October 3, 2012 / Notices
for public review in the Division of
Dockets Management (see ADDRESSES)
between 9 a.m. and 4 p.m., Monday
through Friday.
DEPARTMENT OF HEALTH AND
HUMAN SERVICES
Dated: September 26, 2012.
Leslie Kux,
Assistant Commissioner for Policy.
[Docket No. FDA–2012–N–0981]
applications (ANADAs) at the sponsors’
request because the products are no
longer manufactured or marketed.
Food and Drug Administration
Withdrawal of approval is
effective October 15, 2012.
DATES:
Withdrawal of Approval of New Animal
Drug Applications; Butorphanol;
Doxapram; Triamcinolone; Tylosin
[FR Doc. 2012–24213 Filed 10–2–12; 8:45 am]
BILLING CODE 4160–01–P
AGENCY:
Food and Drug Administration,
HHS.
ACTION:
Notice.
FOR FURTHER INFORMATION CONTACT:
David Alterman, Center for Veterinary
Medicine (HFV–212), Food and Drug
Administration, 7519 Standish Pl.,
Rockville, MD 20855, 240–453–6843,
email: david.alterman@fda.hhs.gov.
The
following sponsors have requested that
FDA withdraw approval of the NADA
and ANADAs listed in table 1 of this
document because the products are no
longer manufactured or marketed.
SUPPLEMENTARY INFORMATION:
The Food and Drug
Administration (FDA) is withdrawing
approval of a new animal drug
application (NADA) and three
abbreviated new animal drug
SUMMARY:
TABLE 1—NADA AND ANADAS FOR WHICH WITHDRAWAL OF APPROVAL HAS BEEN REQUESTED
NADA/ANADA No.
Trade name (drug)
Applicant
100–556 ...............................
Vigorena Feeds Hy-Ty Premix (tylosin phosphate) ........
200–435 ...............................
RESPIRAM (doxapram hydrochloride) Injection .............
200–446 ...............................
BUTORPHINE (butorphanol tartrate) Injection ...............
200–459 ...............................
VETAZINE (triamcinolone) Cream ..................................
Springfield Milling Corp., Vigorena Feeds, Springfield,
MN 56087.
Modern Veterinary Therapeutics, LLC, 18001 Old Cutler Rd., Suite 317, Miami, FL 33157.
Modern Veterinary Therapeutics, LLC, 18001 Old Cutler Rd., Suite 317, Miami, FL 33157.
Modern Veterinary Therapeutics, LLC, 18001 Old Cutler Rd., Suite 317, Miami, FL 33157.
Therefore, under authority delegated
to the Commissioner of Food and Drugs
and redelegated to the Center for
Veterinary Medicine, and in accordance
with § 514.116 Notice of withdrawal of
approval of application (21 CFR
514.116), notice is given that approval
of NADA 100–556 and ANADAs 200–
435, 200–446, and 200–459, and all
supplements and amendments thereto,
is hereby withdrawn, effective October
15, 2012.
Elsewhere in this issue of the Federal
Register, FDA is amending the animal
drug regulations to reflect the voluntary
withdrawal of approval of these
applications.
Dated: September 27, 2012.
Bernadette Dunham,
Director, Center for Veterinary Medicine.
[FR Doc. 2012–24330 Filed 10–2–12; 8:45 am]
BILLING CODE 4160–01–P
DEPARTMENT OF HEALTH AND
HUMAN SERVICES
erowe on DSK2VPTVN1PROD with
National Institutes of Health
Government-Owned Inventions;
Availability for Licensing
National Institutes of Health,
Public Health Service, HHS.
ACTION: Notice.
AGENCY:
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18:36 Oct 02, 2012
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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.
SUMMARY:
FOR FURTHER INFORMATION CONTACT:
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.
A Novel Immortalized Human Adrenal
Cell Line With Inactive Protein Kinase
A for Studies on cAMP Signaling and
Endocrine Tumorigenesis
Description of Technology: The first
known immortalized cell line with a
naturally-occurring inactivating
mutation in PRKAR1A, the regulatory
subunit type 1A (R1alpha) of protein
PO 00000
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Fmt 4703
Sfmt 4703
kinase A (PKA), which is associated
with tumor formation.
PKA isozyme balance is critical for
the control of cAMP signaling and
related cell cycle and proliferation
changes. Aberrant cAMP signaling has
been linked to adrenocortical and other,
mostly endocrine, tumors. Inactivating
mutations in the PRKAR1A gene are a
known cause of Carney Complex—an
autosomal dominant multiple neoplasia
syndrome associated with skin, heart,
and other myxomas and a variety of
endocrine tumors.
Potential Commercial Applications:
• Studies on multiple tumor
formation associated with Carney
Complex.
• Characterization of cAMP-mediated
mechanisms of endocrine tumor
formation.
• Studies of a large variety of cAMPmediated processes in normal
physiology and disease.
Competitive Advantages: First known
immortalized cell line with a naturallyoccurring inactivating mutation in the
PRKAR1A gene.
Development Stage: In vitro data
available.
Inventor: Constantine A. Stratakis
(NICHD).
Publication: Nesterova M, et al. An
immortalized human cell line bearing a
PRKAR1A-inactivating mutation: effects
of overexpression of the wild-type
E:\FR\FM\03OCN1.SGM
03OCN1
Federal Register / Vol. 77, No. 192 / Wednesday, October 3, 2012 / Notices
Allele and other protein kinase A
subunits. J Clin Endocrinol Metab. 2008
Feb;93(2):565–71. [PMID 18056771].
Intellectual Property: HHS Reference
No. E–267–2012/0—Research Material.
Patent protection is not being pursued
for this technology.
Licensing Contact: Patrick McCue,
Ph.D.; 301–435–5560;
mccuepat@mail.nih.gov.
Collaborative Research Opportunity:
The Eunice Kennedy Shriver National
Institute of Child Health and Human
Development is seeking statements of
capability or interest from parties
interested in collaborative research to
further develop, evaluate or
commercialize this technology. For
collaboration opportunities, please
contact Joseph Conrad III, Ph.D. at
jmconrad@mail.nih.gov.
erowe on DSK2VPTVN1PROD with
Modulation of Regulatory T-Cell and BCell Lymphocytes for the Treatment of
Autoimmune and Other Disease
Indications
Description of Technology: A method
of modulating the immune response by
affecting the activity of the regulatory
lymphocytes through targeting of the
Hepatitis A Virus receptor 1 (HAVCR1)
receptor. This methodology can be
developed for the treatment of
autoimmune diseases, allergies,
prevention of transplant rejection, and
incorporated into therapeutic strategies
for cancer.
Regulatory lymphocytes, such as
regulatory T-cells (Tregs) and B-cells
(Bregs), play a significant role in
suppressing and controlling immune
responses to antigens, including
allergens and self-antigens that induce
autoimmune diseases. The Tregs and
Bregs also control the immune
responses to microbial pathogens
thereby limiting excessive damage to
tissue. HAVCR1 is expressed on these
regulatory lymphocytes and functions as
a master regulator of these cells.
Potential Commercial Applications:
• Treatment of Autoimmune
Diseases.
• Treatment of Allergies.
• Prevention of Rejection of Allogenic
Transplants.
• Cancer Therapy.
• Immunotherapies.
• Stimulate Response to Vaccines
(adjuvant).
Competitive Advantages: Can be used
to target multiple disease states.
Development Stage:
• Early-stage.
• Pre-clinical.
• In vitro data available.
Inventors: Gerardo Kaplan, Mohanraj
Manangeeswaran, Jerome Jacques,
Krishnamurthy Konduru (all of FDA).
VerDate Mar<15>2010
15:03 Oct 02, 2012
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Publication: Manangeeswaran M, et
al. Binding of hepatitis A virus to its
cellular receptor 1 inhibits T-regulatory
cell functions in humans.
Gastroenterology. 2012 Jun;142(7):1516–
25.e3. [PMID 22430395].
Intellectual Property: HHS Reference
No. E–095–2012/0—U.S. Provisional
Application No. 61/611,437 filed 15 Mar
2012.
Related Technology: HHS Reference
No. E–150–1994/0—U.S. Patent
5,622,861 issued 22 Apr 1997 (Hepatitis
A Virus Receptor).
Licensing Contact: Kevin W. Chang,
Ph.D.; 301–435–5018; changke@mail.
nih.gov.
Collaborative Research Opportunity:
The Center for Biologics Evaluation and
Research, Laboratory of Emerging
Pathogens, is seeking statements of
capability or interest from parties
interested in collaborative research to
further develop, evaluate or
commercialize targeting of HAVCR1 to
control Treg and Breg function in
human diseases. For collaboration
opportunities, please contact Gerardo
Kaplan at gerardo.kaplan@fda.hhs.gov.
A Method To Expand a Population of
Regulatory T Cells Optimal for the
Treatment of Autoimmune Diseases
Description of Technology: The
transfusion of regulatory T cells (Tregs)
has been used in the clinic to
successfully prevent graft vs. host
disease and is currently being evaluated
in the treatment of other autoimmune
diseases, such as organ graft rejection,
type 1 diabetes and multiple sclerosis.
Prior to transfusion, adoptive regulatory
T cell transfer requires the expansion of
regulatory T cells in culture; this results
in a mixed population of regulatory T
cells that limits the effectiveness of the
transferred cells.
Scientists at the NIH have developed
a method that promotes the expansion
of regulatory T cells that are longer
lived, more stable, and more
suppressive of the autoimmune
response. By supplementing T cell
cultures with DNA oligonucleotides, the
inventors were able to enrich the
regulatory T cell population that
enhanced the suppression of the
autoimmune response. This method has
the potential to more effectively
generate regulatory T cells for the
treatment of autoimmune diseases.
Potential Commercial Applications:
Treatment of autoimmune diseases,
such as Graft vs. Host Disease, Organ
Graft Rejection Type 1 Diabetes,
Multiple Sclerosis.
Competitive Advantages:
PO 00000
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60443
• More effective therapy when
compared to traditional T cell
expansion methods.
• Expansion method is inexpensive
and similar to current methods.
Development Stage: In vitro data
available.
Inventors: Yong Chan Kim and Ethan
M. Shevach (NIAID).
Publication: Kim Y, et al.
Oligodeoxynucleotides stabilize Heliosexpressing Foxp3+ human T regulatory
cells during in vitro expansion. Blood.
2012 Mar 22;119(12):2810–8. [PMID
22294730].
Intellectual Property: HHS Reference
No. E–279–2011/0—U.S. Provisional
Application No. 61/576,837 filed 16 Dec
2011.
Licensing Contact: John Stansberry,
Ph.D.; 301–435–5236; stansbej@mail.
nih.gov.
Peptides for Treatment of Tumor
Necrosis Factor Alpha Mediated
Inflammatory Disease
Description of Technology: Tumor
Necrosis Factor alpha (TNF-alpha) is a
multifunctional cytokine that mediates
inflammation, immune regulation, and
cellular proliferation. This cytokine is
converted to its active form by TNFalpha converting enzyme (TACE).
Pathological increases in TNF-alpha
activity have been associated with a
wide variety of inflammatory diseases,
including inflammatory bowel disease,
rheumatoid arthritis, and cancer.
Inhibiting the conversion of TNF-alpha
to its active form by inhibiting TACE
represents a potential treatment for
these diseases.
The current technology provides
peptides, derived from an N-terminal
fragment of the TACE protein, that
inhibit TACE activity. Also described
are methods of using these peptides to
lower levels of active TNF-alpha. These
peptides could be used as a treatment
for TNF-alpha-mediated inflammatory
diseases.
Potential Commercial Applications:
Treatment of TNF-alpha mediated
inflammatory diseases.
Competitive Advantages: Inhibition of
TACE activity represents a novel
mechanism to treat inflammatory
disease.
Development Stage:
• Early-stage.
• In vitro data available.
Inventors: Stewart J. Levine et al.
(NHLBI).
Publication: Buckley CA, et al.
Amino-terminal TACE prodomain
attenuates TNFR2 cleavage
independently of the cysteine switch.
Am J Physiol Lung Cell Mol Physiol.
2005 Jun;288(6):L1132–8. [PMID
15749738].
E:\FR\FM\03OCN1.SGM
03OCN1
60444
Federal Register / Vol. 77, No. 192 / Wednesday, October 3, 2012 / Notices
erowe on DSK2VPTVN1PROD with
Intellectual Property: HHS Reference
No. E–208–2003/0—U.S. Patent No.
7,655,752 issued 02 Feb 2010.
Licensing Contact: Tara Kirby, Ph.D.;
301–435–4426; tarak@mail.nih.gov.
Human Antibodies and Fusion Proteins
With Potent and Broad HIV–1
Neutralizing Activity
Description of Technology: The
inventions listed below provide
multiple novel human anti-HIV–1
domain antibodies (m36 and its affinitymatured versions) and their fusion
proteins with two-domain or singledomain human soluble CD4 (sCD4) that
can potentially be used alone or
synergistically with other anti-HIV–1
antibodies and antiretroviral drugs as
therapeutics and/or preventatives for
infection by different HIV–1 strains.
Some of the inventions listed below
also describe some fusion proteins as
vaccine immunogens that could elicit
broadly neutralizing antibodies against
HIV-isolates from different clades. One
invention also describes the methods to
prepare and use the immunogens in the
vaccination for prevention of HIV–1
infections. More specifically, the later
invention provides a vaccine composed
of a primary immunogen and a
secondary immunogen, and a method
for making the vaccine which could be
effective in eliciting desired broadly
neutralizing antibodies. The primary
immunogen could be effective in
activating B cell receptors (BCRs) that
are on the maturational pathways of the
desired antibodies and have an
intermediate degree of somatic
mutational diversity. The secondary
immunogen contains epitopes of the
desired antibodies and could be
effective in further diversifying the
BCRs sufficiently to form mature BCRs
that have the identical or substantially
identical sequence as the desired
antibodies.
Potential Commercial Applications:
Treatment and prevention of HIV–1
infections.
Competitive Advantages:
• Elicits broadly neutralizing
antibodies against HIV–1 isolates from
different clades.
• Potentially elicits antibodies that
are not regulated by tolerance
mechanisms.
• Novel methods to design vaccines
for HIV–1 treatment and prevention.
• May also be used for designing
vaccines for cancer treatment.
• Relatively small size allows for
potential penetration into lymphoid
tissues.
Development Stage:
• In vitro data available.
• In vivo data available (animal).
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Inventors: Dimiter Dimitrov and
Weizao Chen (NCI).
Publications:
1. Chen W, et al. Human domain
antibodies to conserved sterically
restricted regions on gp120 as
exceptionally potent cross-reactive HIV–
1 neutralizers. Proc Natl Acad Sci USA.
2008 Nov 4;105(44):17121–6. [PMID
18957538].
2. Chen W, et al. Engineered single
human CD4 domains as potent HIV–1
inhibitors and components of vaccine
immunogens. J Virol. 2011
Sep;85(18):9395–405. [PMID 21715496].
3. Chen W, et al. Bifunctional fusion
proteins of the human engineered
antibody domain m36 with human
soluble CD4 are potent inhibitors of
diverse HIV–1 isolates. Antiviral Res.
2010 Oct;88(1):107–15. [PMID
20709110].
4. Chen W, Dimitrov DS. Human
monoclonal antibodies and engineered
antibody domains as HIV entry
inhibitors. Curr Opin HIV AIDS. 2009
Mar;4(2):112–7. [PMID 19339949].
Intellectual Property:
• HHS Reference No. E–043–2008/
0—U.S. Patent Application No. 12/
811,998 filed 07 Jul 2010; related
international applications.
• HHS Reference No. E–322–2008/
0—U.S. Patent Application No. 13/
123,659 filed 11 Apr 2011.
• HHS Reference No. E–103–2010/
1—PCT Application No. PCT/US2011/
037439 filed 20 May 2011, which
published as WO 2011–146891 on 31
May 2012.
Licensing Contact: Sally Hu, Ph.D.;
301–435–5606; hus@mail.nih.gov.
Collaborative Research Opportunity:
The NCI CCR Nanobiology Program is
seeking statements of capability or
interest from parties interested in
collaborative research to further
develop, evaluate or commercialize
m36, single domain sCD4, and related
fusion proteins as candidate
therapeutics against HIV–1. For
collaboration opportunities, please
contact John Hewes, Ph.D. at hewesj@
mail.nih.gov.
DEPARTMENT OF HEALTH AND
HUMAN SERVICES
Dated: September 27, 2012.
Richard U. Rodriguez,
Director, Division of Technology Development
and Transfer, Office of Technology Transfer,
National Institutes of Health.
National Institutes of Health
[FR Doc. 2012–24251 Filed 10–2–12; 8:45 am]
Frm 00072
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National Institute of General Medical
Sciences Notice of Closed Meeting
Pursuant to section 10(d) of the
Federal Advisory Committee Act, as
amended (5 U.S.C. App.), notice is
hereby given of the following meeting.
The meeting will be closed to the
public in accordance with the
provisions set forth in sections
552b(c)(4) and 552b(c)(6), Title 5 U.S.C.,
as amended. The grant applications and
the discussions could disclose
confidential trade secrets or commercial
property such as patentable material,
and personal information concerning
individuals associated with the grant
applications, the disclosure of which
would constitute a clearly unwarranted
invasion of personal privacy.
Name of Committee: National Institute of
General Medical Sciences Special Emphasis
Panel; Phase III Antibiotic Clinical Trials.
Date: November 1, 2012.
Time: 11 a.m. to 12 p.m.
Agenda: To review and evaluate grant
applications.
Place: National Institutes of Health,
Natcher Building, 45 Center Drive, Room
3An18K, Bethesda, MD 20892.
Contact Person: Brian R. Pike, Ph.D.,
Scientific Review Officer, Office of Scientific
Review, National Institute of General Medical
Sciences, National Institutes of Health, 45
Center Drive, Room 3An18, Bethesda, MD
20892, 301–594–3907, pikbr@mail.nih.gov.
(Catalogue of Federal Domestic Assistance
Program Nos. 93.375, Minority Biomedical
Research Support; 93.821, Cell Biology and
Biophysics Research; 93.859, Pharmacology,
Physiology, and Biological Chemistry
Research; 93.862, Genetics and
Developmental Biology Research; 93.88,
Minority Access to Research Careers; 93.96,
Special Minority Initiatives, National
Institutes of Health, HHS)
Dated: September 27, 2012.
Melanie J. Gray,
Program Analyst, Office of Federal Advisory
Committee Policy.
[FR Doc. 2012–24253 Filed 10–2–12; 8:45 am]
BILLING CODE 4140–01–P
DEPARTMENT OF HEALTH AND
HUMAN SERVICES
Eunice Kennedy Shriver National
Institute of Child Health & Human
Development; Notice of Closed
Meeting
Pursuant to section 10(d) of the
Federal Advisory Committee Act, as
BILLING CODE 4140–01–P
PO 00000
National Institutes of Health
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]]>Agencies
[Federal Register Volume 77, Number 192 (Wednesday, October 3, 2012)]
[Notices]
[Pages 60442-60444]
From the Federal Register Online via the Government Printing Office [www.gpo.gov]
[FR Doc No: 2012-24251]
-----------------------------------------------------------------------
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.
-----------------------------------------------------------------------
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.
FOR FURTHER INFORMATION CONTACT: 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.
A Novel Immortalized Human Adrenal Cell Line With Inactive Protein
Kinase A for Studies on cAMP Signaling and Endocrine Tumorigenesis
Description of Technology: The first known immortalized cell line
with a naturally-occurring inactivating mutation in PRKAR1A, the
regulatory subunit type 1A (R1alpha) of protein kinase A (PKA), which
is associated with tumor formation.
PKA isozyme balance is critical for the control of cAMP signaling
and related cell cycle and proliferation changes. Aberrant cAMP
signaling has been linked to adrenocortical and other, mostly
endocrine, tumors. Inactivating mutations in the PRKAR1A gene are a
known cause of Carney Complex--an autosomal dominant multiple neoplasia
syndrome associated with skin, heart, and other myxomas and a variety
of endocrine tumors.
Potential Commercial Applications:
Studies on multiple tumor formation associated with Carney
Complex.
Characterization of cAMP-mediated mechanisms of endocrine
tumor formation.
Studies of a large variety of cAMP-mediated processes in
normal physiology and disease.
Competitive Advantages: First known immortalized cell line with a
naturally-occurring inactivating mutation in the PRKAR1A gene.
Development Stage: In vitro data available.
Inventor: Constantine A. Stratakis (NICHD).
Publication: Nesterova M, et al. An immortalized human cell line
bearing a PRKAR1A-inactivating mutation: effects of overexpression of
the wild-type
[[Page 60443]]
Allele and other protein kinase A subunits. J Clin Endocrinol Metab.
2008 Feb;93(2):565-71. [PMID 18056771].
Intellectual Property: HHS Reference No. E-267-2012/0--Research
Material. Patent protection is not being pursued for this technology.
Licensing Contact: Patrick McCue, Ph.D.; 301-435-5560;
mccuepat@mail.nih.gov.
Collaborative Research Opportunity: The Eunice Kennedy Shriver
National Institute of Child Health and Human Development is seeking
statements of capability or interest from parties interested in
collaborative research to further develop, evaluate or commercialize
this technology. For collaboration opportunities, please contact Joseph
Conrad III, Ph.D. at jmconrad@mail.nih.gov.
Modulation of Regulatory T-Cell and B-Cell Lymphocytes for the
Treatment of Autoimmune and Other Disease Indications
Description of Technology: A method of modulating the immune
response by affecting the activity of the regulatory lymphocytes
through targeting of the Hepatitis A Virus receptor 1 (HAVCR1)
receptor. This methodology can be developed for the treatment of
autoimmune diseases, allergies, prevention of transplant rejection, and
incorporated into therapeutic strategies for cancer.
Regulatory lymphocytes, such as regulatory T-cells (Tregs) and B-
cells (Bregs), play a significant role in suppressing and controlling
immune responses to antigens, including allergens and self-antigens
that induce autoimmune diseases. The Tregs and Bregs also control the
immune responses to microbial pathogens thereby limiting excessive
damage to tissue. HAVCR1 is expressed on these regulatory lymphocytes
and functions as a master regulator of these cells.
Potential Commercial Applications:
Treatment of Autoimmune Diseases.
Treatment of Allergies.
Prevention of Rejection of Allogenic Transplants.
Cancer Therapy.
Immunotherapies.
Stimulate Response to Vaccines (adjuvant).
Competitive Advantages: Can be used to target multiple disease
states.
Development Stage:
Early-stage.
Pre-clinical.
In vitro data available.
Inventors: Gerardo Kaplan, Mohanraj Manangeeswaran, Jerome Jacques,
Krishnamurthy Konduru (all of FDA).
Publication: Manangeeswaran M, et al. Binding of hepatitis A virus
to its cellular receptor 1 inhibits T-regulatory cell functions in
humans. Gastroenterology. 2012 Jun;142(7):1516-25.e3. [PMID 22430395].
Intellectual Property: HHS Reference No. E-095-2012/0--U.S.
Provisional Application No. 61/611,437 filed 15 Mar 2012.
Related Technology: HHS Reference No. E-150-1994/0--U.S. Patent
5,622,861 issued 22 Apr 1997 (Hepatitis A Virus Receptor).
Licensing Contact: Kevin W. Chang, Ph.D.; 301-435-5018;
changke@mail.nih.gov.
Collaborative Research Opportunity: The Center for Biologics
Evaluation and Research, Laboratory of Emerging Pathogens, is seeking
statements of capability or interest from parties interested in
collaborative research to further develop, evaluate or commercialize
targeting of HAVCR1 to control Treg and Breg function in human
diseases. For collaboration opportunities, please contact Gerardo
Kaplan at gerardo.kaplan@fda.hhs.gov.
A Method To Expand a Population of Regulatory T Cells Optimal for the
Treatment of Autoimmune Diseases
Description of Technology: The transfusion of regulatory T cells
(Tregs) has been used in the clinic to successfully prevent graft vs.
host disease and is currently being evaluated in the treatment of other
autoimmune diseases, such as organ graft rejection, type 1 diabetes and
multiple sclerosis. Prior to transfusion, adoptive regulatory T cell
transfer requires the expansion of regulatory T cells in culture; this
results in a mixed population of regulatory T cells that limits the
effectiveness of the transferred cells.
Scientists at the NIH have developed a method that promotes the
expansion of regulatory T cells that are longer lived, more stable, and
more suppressive of the autoimmune response. By supplementing T cell
cultures with DNA oligonucleotides, the inventors were able to enrich
the regulatory T cell population that enhanced the suppression of the
autoimmune response. This method has the potential to more effectively
generate regulatory T cells for the treatment of autoimmune diseases.
Potential Commercial Applications: Treatment of autoimmune
diseases, such as Graft vs. Host Disease, Organ Graft Rejection Type 1
Diabetes, Multiple Sclerosis.
Competitive Advantages:
More effective therapy when compared to traditional T cell
expansion methods.
Expansion method is inexpensive and similar to current
methods.
Development Stage: In vitro data available.
Inventors: Yong Chan Kim and Ethan M. Shevach (NIAID).
Publication: Kim Y, et al. Oligodeoxynucleotides stabilize Helios-
expressing Foxp3+ human T regulatory cells during in vitro expansion.
Blood. 2012 Mar 22;119(12):2810-8. [PMID 22294730].
Intellectual Property: HHS Reference No. E-279-2011/0--U.S.
Provisional Application No. 61/576,837 filed 16 Dec 2011.
Licensing Contact: John Stansberry, Ph.D.; 301-435-5236;
stansbej@mail.nih.gov.
Peptides for Treatment of Tumor Necrosis Factor Alpha Mediated
Inflammatory Disease
Description of Technology: Tumor Necrosis Factor alpha (TNF-alpha)
is a multifunctional cytokine that mediates inflammation, immune
regulation, and cellular proliferation. This cytokine is converted to
its active form by TNF-alpha converting enzyme (TACE). Pathological
increases in TNF-alpha activity have been associated with a wide
variety of inflammatory diseases, including inflammatory bowel disease,
rheumatoid arthritis, and cancer. Inhibiting the conversion of TNF-
alpha to its active form by inhibiting TACE represents a potential
treatment for these diseases.
The current technology provides peptides, derived from an N-
terminal fragment of the TACE protein, that inhibit TACE activity. Also
described are methods of using these peptides to lower levels of active
TNF-alpha. These peptides could be used as a treatment for TNF-alpha-
mediated inflammatory diseases.
Potential Commercial Applications: Treatment of TNF-alpha mediated
inflammatory diseases.
Competitive Advantages: Inhibition of TACE activity represents a
novel mechanism to treat inflammatory disease.
Development Stage:
Early-stage.
In vitro data available.
Inventors: Stewart J. Levine et al. (NHLBI).
Publication: Buckley CA, et al. Amino-terminal TACE prodomain
attenuates TNFR2 cleavage independently of the cysteine switch. Am J
Physiol Lung Cell Mol Physiol. 2005 Jun;288(6):L1132-8. [PMID
15749738].
[[Page 60444]]
Intellectual Property: HHS Reference No. E-208-2003/0--U.S. Patent
No. 7,655,752 issued 02 Feb 2010.
Licensing Contact: Tara Kirby, Ph.D.; 301-435-4426;
tarak@mail.nih.gov.
Human Antibodies and Fusion Proteins With Potent and Broad HIV-1
Neutralizing Activity
Description of Technology: The inventions listed below provide
multiple novel human anti-HIV-1 domain antibodies (m36 and its
affinity- matured versions) and their fusion proteins with two-domain
or single-domain human soluble CD4 (sCD4) that can potentially be used
alone or synergistically with other anti-HIV-1 antibodies and
antiretroviral drugs as therapeutics and/or preventatives for infection
by different HIV-1 strains.
Some of the inventions listed below also describe some fusion
proteins as vaccine immunogens that could elicit broadly neutralizing
antibodies against HIV-isolates from different clades. One invention
also describes the methods to prepare and use the immunogens in the
vaccination for prevention of HIV-1 infections. More specifically, the
later invention provides a vaccine composed of a primary immunogen and
a secondary immunogen, and a method for making the vaccine which could
be effective in eliciting desired broadly neutralizing antibodies. The
primary immunogen could be effective in activating B cell receptors
(BCRs) that are on the maturational pathways of the desired antibodies
and have an intermediate degree of somatic mutational diversity. The
secondary immunogen contains epitopes of the desired antibodies and
could be effective in further diversifying the BCRs sufficiently to
form mature BCRs that have the identical or substantially identical
sequence as the desired antibodies.
Potential Commercial Applications: Treatment and prevention of HIV-
1 infections.
Competitive Advantages:
Elicits broadly neutralizing antibodies against HIV-1
isolates from different clades.
Potentially elicits antibodies that are not regulated by
tolerance mechanisms.
Novel methods to design vaccines for HIV-1 treatment and
prevention.
May also be used for designing vaccines for cancer
treatment.
Relatively small size allows for potential penetration
into lymphoid tissues.
Development Stage:
In vitro data available.
In vivo data available (animal).
Inventors: Dimiter Dimitrov and Weizao Chen (NCI).
Publications:
1. Chen W, et al. Human domain antibodies to conserved sterically
restricted regions on gp120 as exceptionally potent cross-reactive HIV-
1 neutralizers. Proc Natl Acad Sci USA. 2008 Nov 4;105(44):17121-6.
[PMID 18957538].
2. Chen W, et al. Engineered single human CD4 domains as potent
HIV-1 inhibitors and components of vaccine immunogens. J Virol. 2011
Sep;85(18):9395-405. [PMID 21715496].
3. Chen W, et al. Bifunctional fusion proteins of the human
engineered antibody domain m36 with human soluble CD4 are potent
inhibitors of diverse HIV-1 isolates. Antiviral Res. 2010
Oct;88(1):107-15. [PMID 20709110].
4. Chen W, Dimitrov DS. Human monoclonal antibodies and engineered
antibody domains as HIV entry inhibitors. Curr Opin HIV AIDS. 2009
Mar;4(2):112-7. [PMID 19339949].
Intellectual Property:
HHS Reference No. E-043-2008/0--U.S. Patent Application
No. 12/811,998 filed 07 Jul 2010; related international applications.
HHS Reference No. E-322-2008/0--U.S. Patent Application
No. 13/123,659 filed 11 Apr 2011.
HHS Reference No. E-103-2010/1--PCT Application No. PCT/
US2011/037439 filed 20 May 2011, which published as WO 2011-146891 on
31 May 2012.
Licensing Contact: Sally Hu, Ph.D.; 301-435-5606; hus@mail.nih.gov.
Collaborative Research Opportunity: The NCI CCR Nanobiology Program
is seeking statements of capability or interest from parties interested
in collaborative research to further develop, evaluate or commercialize
m36, single domain sCD4, and related fusion proteins as candidate
therapeutics against HIV-1. For collaboration opportunities, please
contact John Hewes, Ph.D. at hewesj@mail.nih.gov.
Dated: September 27, 2012.
Richard U. Rodriguez,
Director, Division of Technology Development and Transfer, Office of
Technology Transfer, National Institutes of Health.
[FR Doc. 2012-24251 Filed 10-2-12; 8:45 am]
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