Government-Owned Inventions; Availability for Licensing, 67985-67987 [2010-27912]
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Federal Register / Vol. 75, No. 213 / Thursday, November 4, 2010 / Notices
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jlentini on DSKJ8SOYB1PROD with NOTICES
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[FR Doc. 2010–27824 Filed 11–3–10; 8:45 am]
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67985
MRS spectrum data. The method may
also include providing raw MRS
spectrum data, recalibrating the raw
MRS spectrum data, and scaling the
recalibrated MRS spectrum data by
using a plurality of weighting constants
to generate a preprocessed MRS
spectrum data.
Applications
DEPARTMENT OF HEALTH AND
HUMAN SERVICES
National Institutes of Health
Government-Owned Inventions;
Availability for Licensing
National Institutes of Health,
Public Health Service, HHS.
ACTION: Notice.
AGENCY:
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.
SUMMARY:
System for Magnetic Resonance
Spectroscopy of Brain Tissue for
Pattern-Based Diagnostics
Description of Invention: Available for
licensing and commercial development
is a system for preprocessing magnetic
resonance spectroscopy (MRS) data of
brain tissue for pattern-based
diagnostics. The MRS preprocessing
system includes an MRS preprocessing
module that executes an operation that
normalizes MRS spectrum data,
recalibrates and scales the normalized
MRS spectrum data, and then
renormalizes the scaled MRS spectrum
data. The resulting preprocessed MRS
data is used to assist in identifying
abnormalities in tissues shown in MRS
scans. Raw MRS spectrum data and
scaling the raw MRS spectrum data is
achieved by a plurality of weighting
constants to generate a preprocessed
PO 00000
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• MRI Imaging.
• Brain Imaging.
• Neurology.
Inventors: Jon G. Wilkes (FDA/NCTR),
Dan A. Buzatu (FDA/NCTR), Pierre
Alusta (FDA/NCTR), Bruce A. Pearce
(FDA/NCTR), Richard Beger (FDA/
NCTR), Inessa Im (FDA/NCTR).
Patent Status: U.S. Provisional
Application No. 61/261,170 filed 13
Nov 2009 (HHS Reference No. E–298–
2009/0–US–01).
Licensing Status: Available for
licensing.
Licensing Contact: Michael A.
Shmilovich, Esq.; 301–435–5019;
shmilovm@mail.nih.gov.
Collaborative Research Opportunity:
The FDA National Center for
Toxicological Research is seeking
statements of capability or interest from
parties interested in collaborative
research to further develop, evaluate, or
commercialize FDA’s magnetic
resonance spectroscopy technology in
various imaging and diagnostic
applications. Please contact Alice Y.
Welch, PhD at 301–796–8449 or
alice.welch@fda.hhs.gov for more
information.
Cancer-Linked Sequences Encoding the
A2BP1/FOX1 Gene
Description of Invention:
Mesothelioma is a rare type of cancer in
which malignant cells are found in the
lining of the chest or abdomen.
Symptoms are frequently misdiagnosed
and an accurate diagnosis generally
does not occur until advanced stages,
and patients live on average nine to
thirteen months after an accurate
diagnosis. To date, there are no effective
systemic treatments.
Researchers at the National Cancer
Institute, NIH, have identified a
recurrent alteration in the DNA
sequence for ataxin-2 binding protein
(A2BP1/FOX1) in human mesothelioma
and colorectal cancers that is present in
at least twenty percent (20%) of cancer
cell lines and primary tumor samples.
The sequence is not present in normal
tissue, proving that it has arisen as an
acquired somatic mutation in cancer.
Furthermore, additional data suggests a
possible role for the alteration in
neurological diseases such as autism,
E:\FR\FM\04NON1.SGM
04NON1
67986
Federal Register / Vol. 75, No. 213 / Thursday, November 4, 2010 / Notices
inherited mental retardation, and
seizures.
This discovery offers a new approach
for the diagnosis and early detection of
cancer.
Applications: Development of assays
for detection, diagnosis, or prognosis of
diseases associated with chromosomal
disruptions of the ataxin-2 binding
protein 1 (A2BP1 or FOX1) gene, such
as cancer and neurological disorders.
Development Status: Pre-clinical.
Inventors: Frederic J. Kaye (NCI).
Relevant Publication: Beroukhim R et
al. The landscape of somatic copynumber alteration across human
cancers. Nature 2010 Feb 18;
463(7283):899–905. [PubMed:
20164920]
jlentini on DSKJ8SOYB1PROD with NOTICES
Patent Status
• U.S. Provisional Application No.
61/121,997 filed 12 Dec 2008 (HHS
Reference No. E–180–2008/0–US–01).
• International Patent Application
No. PCT/US09/67502 filed 10 Dec 2009,
which published as WO 2010/068757
on 17 Jun 2010 (HHS Reference No. E–
180–2008/0–PCT–02).
Licensing Status: Available for
licensing.
Licensing Contact: Patrick P. McCue,
PhD; 301–435–5560;
mccuepat@mail.nih.gov.
Insertion of Foreign Genes in Rubella
Virus and Their Stable Expression in a
Live, Attenuated Viral Vaccine
Description of Invention: Rubella
virus (RUB) is the only member of the
Rubivirus genus of the family
Togaviridae. The RUB genomic RNA is
a single-stranded, 9762-nt, positivesense RNA that contains two long open
reading frames (ORFs): A 5′-proximal
ORF which encodes nonstructural
proteins (NSP) that function primarily
in viral RNA replication, including the
RdRp, and a 3′-proximal ORF which
encodes the virion structural proteins
(SP), the capsid protein (C), and two
envelope glycoproteins, E1 and E2. The
genomic RNA serves as a template for
synthesis of a complementary minusstrand RNA which is the template for
synthesis of both the genomic RNA and
the subgenomic (SG) RNA, from which
the structural proteins are translated.
All earlier efforts at expressing foreign
genes in rubella virus failed due to
stability of the insert. The inventors
have found a way to insert foreign genes
into rubella virus such that the foreign
genes can be expressed stably over
many passages of the virus. More
specifically, based on an earlier
observation that rubella virus can
tolerate a small deletion in the
nonstructural genes and still replicate
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Jkt 223001
normally, the inventors’ have used this
deletion to make room for insertion of
a foreign gene. Thus, the inventors have
conceptualized and reduced to practice
a new way to use the already-approved
rubella vaccine as a viral vector to
express the additional protein antigens
of a second (or multiple other) viruses.
This is highly advantageous because it
allows for production of a live virus
vaccine when attenuation is not
possible for highly virulent viruses such
as HIV.
Furthermore, another advantage of
this vaccine is that virus titers in cell
culture reach one thousand (1000)
human doses per milliliter (ml) of
culture supernatant. This is highly
desirable for production of multiple
millions of doses for the developing
world. In the developed world, this
vaccine could be substituted for the
current vaccine at almost no cost and
used to immunize against rubella plus
the inserted antigen(s). Without
vaccination, the average age of
becoming seropositive for rubella is
approximately nine (9) years old. This
new vaccine could be given to one to
two year olds with a booster at nine
years old. Additionally, this vaccine is
already approved, so the safe and
immunogenic doses are already known.
Applications
• Vaccines for the prevention of
rubella and other indications.
• Use of rubella vector for expression
of foreign genes.
Advantages
• Novel vaccine candidate
• Rapid production time
Development Status: Preclinical
studies have been conducted by the
inventors.
Inventors: Ira Berkower and Angelo
Spadaccini (FDA).
Patent Status
• U.S. Provisional Application No.
61/252,568 filed 16 Oct 2009 (HHS
Reference No. E–156–2008/0–US–01).
• International Patent Application
No. PCT/US2010/052948 filed 15 Oct
2010 (HHS Reference No. E–156–2008/
0–PCT–02).
Relevant Publication: Spadaccini A,
Vimik K, Ni Y, Prutzman K, Berkower
I. Stable expression of a foreign protein
by a replication-competent rubella viral
vector. Vaccine. 2010 Feb 3;28(5):1181–
1187. [PubMed: 19945412].
Licensing Status: Available for
licensing.
Licensing Contact: Peter A. Soukas,
J.D.; 301–435–4646;
soukasp@mail.nih.gov.
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Inhibition of Cell Motility, Angiogenesis
and Metastasis
Description of Invention: The present
invention relates to potent, highly
selective antagonists of Grb2 Src
homology-2 (SH2) domain binding.
Grb2, through its SH2 domain, mediates
growth factor driven cell motility in
vitro and angiogenesis in vivo. These
synthetic, small molecule antagonists
have been shown to block cell motility
stimulated by hepatocyte growth factor
(HGF), fibroblast growth factor (FGF),
epidermal growth factor (EGF), and
vascular endothelial cell growth factor
(VEGF). They also potently inhibit HGFand VEGF-stimulated morphogenesis
and angiogenesis, respectively, in
several model systems. HGF stimulates
mitogenesis, motogenesis and
morphogenesis in a wide range of
cellular targets during development and
adulthood, and its signaling pathway is
frequently over-activated in human
cancers, including colon, gastric, breast,
lung, thyroid and renal carcinomas,
melanoma, several sarcomas as well as
glioblastoma. The ability of HGF to
initiate a program of cell dissociation
and increased cell motility coupled with
increased protease production promotes
aggressive cellular invasion and is
frequently linked to tumor metastasis.
Metastasis, the primary cause of death
in most forms of cancer, is a multistep
process whereby cells from the primary
tumor spread systemically and colonize
distant new sites. Blocking critical steps
in this process could potentially inhibit
tumor metastasis and dramatically
improve cancer survival rates. The
small, synthetic Grb2 SH2 domain
antagonists described in this invention
have been shown to inhibit the induced
and spontaneous metastasis of
melanoma- and prostate cancer-derived
tumor cells in mice. These results
establish a critical role for Grb2 SH2
domain-mediated interactions in the
metastatic process and support the
potential efficacy of this class of
compound in reducing the metastatic
spread of primary solid tumors in
humans.
Applications and Modality: Inhibition
of cell motility-dependent processes,
including angiogenesis and metastasis,
in several types of cancer such as
prostate, colon, gastric, breast, lung,
thyroid and renal carcinomas,
melanoma and various sarcomas.
Development Status: In vivo and in
vitro studies have been conducted on
this technology.
Market
• Cancer is the second leading cause
of death in the U.S.
E:\FR\FM\04NON1.SGM
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Federal Register / Vol. 75, No. 213 / Thursday, November 4, 2010 / Notices
jlentini on DSKJ8SOYB1PROD with NOTICES
• The worldwide incidence of new
cancer patients is forecast to increase
from 4.2 million cases in the major
cancer markets in 2005 to 4.6 million in
2010.
• It is estimated that the worldwide
cancer marker will be worth 85.3 billion
in 2010.
Inventors: Donald P. Bottaro et al.
(NCI).
Relevant Publications
1. Atabey N, Gao Y, Yao Z-J,
Breckenridge D, Soon L, Soriano JV,
Burke TR Jr, Bottaro DP. Potent
blockade of Hepatocyte Growth
Factor-stimulated cell motility,
matrix invasion and branching
morphogenesis by antagonists of
Grb2 Src homology 2 domain
interactions. J Biol Chem. 2001 Apr
27;276(17):14308–14314. [PubMed:
11278639].
2. Shi Z-D, Wei C-Q, Wang X, Lee K, Liu
H, Zhang M, Vasselli J, Bottaro DP,
Linehan WM, Yang D, Burke TR Jr.
Macrocyclization in the design of
tetra-tetrapeptide mimetics that
display potent inhibition of Grb2
SH2 domain binding in whole cell
systems. In: Peptide Revolution:
Genomics, Proteomics
Therapeutics. Chorev, M and
Sawyer, TK, Eds. American Peptide
Society, pp 515–517, 2003.
3. Soriano JV, Lui N, Gao Y, Yao Z-J,
Ishibashi T, Underhill C, Burke TR
Jr, Bottaro DP. Inhibition of
angiogenesis by growth factor
receptor bound protein 2-Src
homology 2 domain bound
antagonists. Mol Cancer Ther. 2004
Oct;3(10):1289–1299. [PubMed:
15486196].
4. Shi Z-D, Karki RG, Worthy KM,
Bindu LK, Dharmawardana PG,
Nicklaus MC, Bottaro DP, Fisher RJ,
Burke TR Jr. Utilization of a
nitrobenzoxadiazole (NBD)
fluorophore in the design of a Grb2
SH2 domain-binding peptide
mimetic. Bioorg Med Chem Lett.
2005 Mar 1;15(5):1385–1388.
[PubMed: 15713392].
5. Kang S-U, Shi, Z-D, Worthy KM,
Bindu LK, Dharmawardana PG,
Choyke SJ, Bottaro DP, Fisher RJ,
Burke TR Jr. Examination of
phosphoryl-mimicking
functionalities within a macrocyclic
Grb2 SH2 domain-binding platform.
J Med Chem. 2005 Jun
16;48(12):3945–3948. [PubMed:
15943469].
6. Shi Z-D, Peruzzi B, Dharmawardana
PG, Leech T, Appella E, Worthy
KM, Bindu LK, Fisher RJ, Bottaro
DP, Burke TR Jr. Synthesis and use
of C-terminally biotinylated
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16:47 Nov 03, 2010
Jkt 223001
peptidomimetics with high Grb2
SH2 domain-binding affinity. In:
Understanding Biology Using
Peptides, Blondelle SE (Ed),
American Peptide Society, pp 208–
209, 2005.
7. Dharmawardana PG, Peruzzi B,
Giubellino A, Burke TR Jr, Bottaro
DP. Molecular targeting of growth
factor receptor-bound 2 (Grb-2) as
an anti-cancer strategy. Anti-Cancer
Drugs 2006 Jan;17(1):13–20.
[PubMed: 16317285].
8. Liu F, Worthy KM, Bindu L,
Giubellino A, Bottaro DP, Fisher RJ,
Burke TR Jr. Utilization of achiral
alkenyl amines for the preparation
of high affinity Grb2 SH2 domainbinding macrocycles by ring-closing
metathesis. Org Biomol Chem. 2007
Jan 21;5(2):367–372. [PubMed:
17205182].
9. Giubellino A, Gao Y, Lee S, Lee MJ, Vasselli JR, Medepalli S, Trepel
JB, Burke TR Jr, Bottaro DP.
Inhibition of tumor metastasis by a
growth factor receptor bound
protein Src domain-binding
antagonist. Cancer Res. (Priority
Report) 2007 Jul 1;67(13):6012–
6016. [PubMed: 17616655].
Patent Status: U.S. Patent Application
No. 11/525,672 filed 22 Sep 2006 (HHS
Reference No. E–265–1999/2–US–01).
Licensing Status: Available for
licensing.
Licensing Contact: Jennifer Wong;
301–435–4633; wongje@mail.nih.gov.
Collaborative Research Opportunity:
The Urologic Oncology Branch of the
National Cancer Institute is seeking
statements of capability or interest from
parties interested in collaborative
research to further develop, evaluate, or
commercialize Grb2 SH2 domain
antagonists as anti-cancer drugs. Please
contact John D. Hewes, Ph.D. at 301–
435–3121 or hewesj@mail.nih.gov for
more information.
Dated: October 29, 2010.
Richard U. Rodriguez,
Director, Division of Technology Development
and Transfer, Office of Technology Transfer,
National Institutes of Health.
[FR Doc. 2010–27912 Filed 11–3–10; 8:45 am]
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67987
DEPARTMENT OF HEALTH AND
HUMAN SERVICES
Food and Drug Administration
[Docket No. FDA–2009–D–0132]
Guidance for Industry: Cellular
Therapy for Cardiac Disease;
Availability
AGENCY:
Food and Drug Administration,
HHS.
ACTION:
Notice.
The Food and Drug
Administration (FDA) is announcing the
availability of a document entitled
‘‘Guidance for Industry: Cellular
Therapy for Cardiac Disease’’ dated
October 2010. The guidance document
provides sponsors who are developing
cellular therapies for the treatment of
cardiac disease with recommendations
on the design of preclinical and clinical
studies and on the chemistry,
manufacturing and controls (CMC)
information that should be included in
an investigational new drug application
(IND) for cellular therapy for cardiac
disease. The guidance announced in
this notice finalizes the draft guidance
entitled ‘‘Guidance for Industry: Somatic
Cell Therapy for Cardiac Disease’’ dated
March 2009.
DATES: Submit either electronic or
written comments on agency guidances
at any time.
ADDRESSES: Submit written requests for
single copies of the guidance to the
Office of Communication, Outreach and
Development (HFM–40), Center for
Biologics Evaluation and Research
(CBER), Food and Drug Administration,
1401 Rockville Pike, suite 200N,
Rockville, MD 20852–1448; or to the
Division of Small Manufacturers,
International, and Consumer Assistance,
Center for Devices and Radiological
Health, Food and Drug Administration,
10903 New Hampshire Ave., Bldg. 66,
rm. 4613, Silver Spring, MD 20993–
0002. Send one self-addressed adhesive
label to assist the office in processing
your requests. The guidance may also be
obtained by mail by calling CBER at
1–800–835–4709 or 301–827–1800. See
the SUPPLEMENTARY INFORMATION section
for electronic access to the guidance
document.
Submit electronic comments on the
guidance to https://www.regulations.gov.
Submit written comments to the
Division of Dockets Management (HFA–
305), Food and Drug Administration,
5630 Fishers Lane, rm. 1061, Rockville,
MD 20852.
FOR FURTHER INFORMATION CONTACT:
Benjamin A. Chacko, Center for
SUMMARY:
E:\FR\FM\04NON1.SGM
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Agencies
[Federal Register Volume 75, Number 213 (Thursday, November 4, 2010)]
[Notices]
[Pages 67985-67987]
From the Federal Register Online via the Government Printing Office [www.gpo.gov]
[FR Doc No: 2010-27912]
-----------------------------------------------------------------------
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.
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.
System for Magnetic Resonance Spectroscopy of Brain Tissue for Pattern-
Based Diagnostics
Description of Invention: Available for licensing and commercial
development is a system for preprocessing magnetic resonance
spectroscopy (MRS) data of brain tissue for pattern-based diagnostics.
The MRS preprocessing system includes an MRS preprocessing module that
executes an operation that normalizes MRS spectrum data, recalibrates
and scales the normalized MRS spectrum data, and then renormalizes the
scaled MRS spectrum data. The resulting preprocessed MRS data is used
to assist in identifying abnormalities in tissues shown in MRS scans.
Raw MRS spectrum data and scaling the raw MRS spectrum data is achieved
by a plurality of weighting constants to generate a preprocessed MRS
spectrum data. The method may also include providing raw MRS spectrum
data, recalibrating the raw MRS spectrum data, and scaling the
recalibrated MRS spectrum data by using a plurality of weighting
constants to generate a preprocessed MRS spectrum data.
Applications
MRI Imaging.
Brain Imaging.
Neurology.
Inventors: Jon G. Wilkes (FDA/NCTR), Dan A. Buzatu (FDA/NCTR),
Pierre Alusta (FDA/NCTR), Bruce A. Pearce (FDA/NCTR), Richard Beger
(FDA/NCTR), Inessa Im (FDA/NCTR).
Patent Status: U.S. Provisional Application No. 61/261,170 filed 13
Nov 2009 (HHS Reference No. E-298-2009/0-US-01).
Licensing Status: Available for licensing.
Licensing Contact: Michael A. Shmilovich, Esq.; 301-435-5019;
shmilovm@mail.nih.gov.
Collaborative Research Opportunity: The FDA National Center for
Toxicological Research is seeking statements of capability or interest
from parties interested in collaborative research to further develop,
evaluate, or commercialize FDA's magnetic resonance spectroscopy
technology in various imaging and diagnostic applications. Please
contact Alice Y. Welch, PhD at 301-796-8449 or alice.welch@fda.hhs.gov
for more information.
Cancer-Linked Sequences Encoding the A2BP1/FOX1 Gene
Description of Invention: Mesothelioma is a rare type of cancer in
which malignant cells are found in the lining of the chest or abdomen.
Symptoms are frequently misdiagnosed and an accurate diagnosis
generally does not occur until advanced stages, and patients live on
average nine to thirteen months after an accurate diagnosis. To date,
there are no effective systemic treatments.
Researchers at the National Cancer Institute, NIH, have identified
a recurrent alteration in the DNA sequence for ataxin-2 binding protein
(A2BP1/FOX1) in human mesothelioma and colorectal cancers that is
present in at least twenty percent (20%) of cancer cell lines and
primary tumor samples. The sequence is not present in normal tissue,
proving that it has arisen as an acquired somatic mutation in cancer.
Furthermore, additional data suggests a possible role for the
alteration in neurological diseases such as autism,
[[Page 67986]]
inherited mental retardation, and seizures.
This discovery offers a new approach for the diagnosis and early
detection of cancer.
Applications: Development of assays for detection, diagnosis, or
prognosis of diseases associated with chromosomal disruptions of the
ataxin-2 binding protein 1 (A2BP1 or FOX1) gene, such as cancer and
neurological disorders.
Development Status: Pre-clinical.
Inventors: Frederic J. Kaye (NCI).
Relevant Publication: Beroukhim R et al. The landscape of somatic
copy-number alteration across human cancers. Nature 2010 Feb 18;
463(7283):899-905. [PubMed: 20164920]
Patent Status
U.S. Provisional Application No. 61/121,997 filed 12 Dec
2008 (HHS Reference No. E-180-2008/0-US-01).
International Patent Application No. PCT/US09/67502 filed
10 Dec 2009, which published as WO 2010/068757 on 17 Jun 2010 (HHS
Reference No. E-180-2008/0-PCT-02).
Licensing Status: Available for licensing.
Licensing Contact: Patrick P. McCue, PhD; 301-435-5560;
mccuepat@mail.nih.gov.
Insertion of Foreign Genes in Rubella Virus and Their Stable Expression
in a Live, Attenuated Viral Vaccine
Description of Invention: Rubella virus (RUB) is the only member of
the Rubivirus genus of the family Togaviridae. The RUB genomic RNA is a
single-stranded, 9762-nt, positive-sense RNA that contains two long
open reading frames (ORFs): A 5'-proximal ORF which encodes
nonstructural proteins (NSP) that function primarily in viral RNA
replication, including the RdRp, and a 3'-proximal ORF which encodes
the virion structural proteins (SP), the capsid protein (C), and two
envelope glycoproteins, E1 and E2. The genomic RNA serves as a template
for synthesis of a complementary minus-strand RNA which is the template
for synthesis of both the genomic RNA and the subgenomic (SG) RNA, from
which the structural proteins are translated.
All earlier efforts at expressing foreign genes in rubella virus
failed due to stability of the insert. The inventors have found a way
to insert foreign genes into rubella virus such that the foreign genes
can be expressed stably over many passages of the virus. More
specifically, based on an earlier observation that rubella virus can
tolerate a small deletion in the nonstructural genes and still
replicate normally, the inventors' have used this deletion to make room
for insertion of a foreign gene. Thus, the inventors have
conceptualized and reduced to practice a new way to use the already-
approved rubella vaccine as a viral vector to express the additional
protein antigens of a second (or multiple other) viruses. This is
highly advantageous because it allows for production of a live virus
vaccine when attenuation is not possible for highly virulent viruses
such as HIV.
Furthermore, another advantage of this vaccine is that virus titers
in cell culture reach one thousand (1000) human doses per milliliter
(ml) of culture supernatant. This is highly desirable for production of
multiple millions of doses for the developing world. In the developed
world, this vaccine could be substituted for the current vaccine at
almost no cost and used to immunize against rubella plus the inserted
antigen(s). Without vaccination, the average age of becoming
seropositive for rubella is approximately nine (9) years old. This new
vaccine could be given to one to two year olds with a booster at nine
years old. Additionally, this vaccine is already approved, so the safe
and immunogenic doses are already known.
Applications
Vaccines for the prevention of rubella and other
indications.
Use of rubella vector for expression of foreign genes.
Advantages
Novel vaccine candidate
Rapid production time
Development Status: Preclinical studies have been conducted by the
inventors.
Inventors: Ira Berkower and Angelo Spadaccini (FDA).
Patent Status
U.S. Provisional Application No. 61/252,568 filed 16 Oct
2009 (HHS Reference No. E-156-2008/0-US-01).
International Patent Application No. PCT/US2010/052948
filed 15 Oct 2010 (HHS Reference No. E-156-2008/0-PCT-02).
Relevant Publication: Spadaccini A, Vimik K, Ni Y, Prutzman K,
Berkower I. Stable expression of a foreign protein by a replication-
competent rubella viral vector. Vaccine. 2010 Feb 3;28(5):1181-1187.
[PubMed: 19945412].
Licensing Status: Available for licensing.
Licensing Contact: Peter A. Soukas, J.D.; 301-435-4646;
soukasp@mail.nih.gov.
Inhibition of Cell Motility, Angiogenesis and Metastasis
Description of Invention: The present invention relates to potent,
highly selective antagonists of Grb2 Src homology-2 (SH2) domain
binding. Grb2, through its SH2 domain, mediates growth factor driven
cell motility in vitro and angiogenesis in vivo. These synthetic, small
molecule antagonists have been shown to block cell motility stimulated
by hepatocyte growth factor (HGF), fibroblast growth factor (FGF),
epidermal growth factor (EGF), and vascular endothelial cell growth
factor (VEGF). They also potently inhibit HGF- and VEGF-stimulated
morphogenesis and angiogenesis, respectively, in several model systems.
HGF stimulates mitogenesis, motogenesis and morphogenesis in a wide
range of cellular targets during development and adulthood, and its
signaling pathway is frequently over-activated in human cancers,
including colon, gastric, breast, lung, thyroid and renal carcinomas,
melanoma, several sarcomas as well as glioblastoma. The ability of HGF
to initiate a program of cell dissociation and increased cell motility
coupled with increased protease production promotes aggressive cellular
invasion and is frequently linked to tumor metastasis.
Metastasis, the primary cause of death in most forms of cancer, is
a multistep process whereby cells from the primary tumor spread
systemically and colonize distant new sites. Blocking critical steps in
this process could potentially inhibit tumor metastasis and
dramatically improve cancer survival rates. The small, synthetic Grb2
SH2 domain antagonists described in this invention have been shown to
inhibit the induced and spontaneous metastasis of melanoma- and
prostate cancer-derived tumor cells in mice. These results establish a
critical role for Grb2 SH2 domain-mediated interactions in the
metastatic process and support the potential efficacy of this class of
compound in reducing the metastatic spread of primary solid tumors in
humans.
Applications and Modality: Inhibition of cell motility-dependent
processes, including angiogenesis and metastasis, in several types of
cancer such as prostate, colon, gastric, breast, lung, thyroid and
renal carcinomas, melanoma and various sarcomas.
Development Status: In vivo and in vitro studies have been
conducted on this technology.
Market
Cancer is the second leading cause of death in the U.S.
[[Page 67987]]
The worldwide incidence of new cancer patients is forecast
to increase from 4.2 million cases in the major cancer markets in 2005
to 4.6 million in 2010.
It is estimated that the worldwide cancer marker will be
worth 85.3 billion in 2010.
Inventors: Donald P. Bottaro et al. (NCI).
Relevant Publications
1. Atabey N, Gao Y, Yao Z-J, Breckenridge D, Soon L, Soriano JV, Burke
TR Jr, Bottaro DP. Potent blockade of Hepatocyte Growth Factor-
stimulated cell motility, matrix invasion and branching morphogenesis
by antagonists of Grb2 Src homology 2 domain interactions. J Biol Chem.
2001 Apr 27;276(17):14308-14314. [PubMed: 11278639].
2. Shi Z-D, Wei C-Q, Wang X, Lee K, Liu H, Zhang M, Vasselli J, Bottaro
DP, Linehan WM, Yang D, Burke TR Jr. Macrocyclization in the design of
tetra-tetrapeptide mimetics that display potent inhibition of Grb2 SH2
domain binding in whole cell systems. In: Peptide Revolution: Genomics,
Proteomics Therapeutics. Chorev, M and Sawyer, TK, Eds. American
Peptide Society, pp 515-517, 2003.
3. Soriano JV, Lui N, Gao Y, Yao Z-J, Ishibashi T, Underhill C, Burke
TR Jr, Bottaro DP. Inhibition of angiogenesis by growth factor receptor
bound protein 2-Src homology 2 domain bound antagonists. Mol Cancer
Ther. 2004 Oct;3(10):1289-1299. [PubMed: 15486196].
4. Shi Z-D, Karki RG, Worthy KM, Bindu LK, Dharmawardana PG, Nicklaus
MC, Bottaro DP, Fisher RJ, Burke TR Jr. Utilization of a
nitrobenzoxadiazole (NBD) fluorophore in the design of a Grb2 SH2
domain-binding peptide mimetic. Bioorg Med Chem Lett. 2005 Mar
1;15(5):1385-1388. [PubMed: 15713392].
5. Kang S-U, Shi, Z-D, Worthy KM, Bindu LK, Dharmawardana PG, Choyke
SJ, Bottaro DP, Fisher RJ, Burke TR Jr. Examination of phosphoryl-
mimicking functionalities within a macrocyclic Grb2 SH2 domain-binding
platform. J Med Chem. 2005 Jun 16;48(12):3945-3948. [PubMed: 15943469].
6. Shi Z-D, Peruzzi B, Dharmawardana PG, Leech T, Appella E, Worthy KM,
Bindu LK, Fisher RJ, Bottaro DP, Burke TR Jr. Synthesis and use of C-
terminally biotinylated peptidomimetics with high Grb2 SH2 domain-
binding affinity. In: Understanding Biology Using Peptides, Blondelle
SE (Ed), American Peptide Society, pp 208-209, 2005.
7. Dharmawardana PG, Peruzzi B, Giubellino A, Burke TR Jr, Bottaro DP.
Molecular targeting of growth factor receptor-bound 2 (Grb-2) as an
anti-cancer strategy. Anti-Cancer Drugs 2006 Jan;17(1):13-20. [PubMed:
16317285].
8. Liu F, Worthy KM, Bindu L, Giubellino A, Bottaro DP, Fisher RJ,
Burke TR Jr. Utilization of achiral alkenyl amines for the preparation
of high affinity Grb2 SH2 domain-binding macrocycles by ring-closing
metathesis. Org Biomol Chem. 2007 Jan 21;5(2):367-372. [PubMed:
17205182].
9. Giubellino A, Gao Y, Lee S, Lee M-J, Vasselli JR, Medepalli S,
Trepel JB, Burke TR Jr, Bottaro DP. Inhibition of tumor metastasis by a
growth factor receptor bound protein Src domain-binding antagonist.
Cancer Res. (Priority Report) 2007 Jul 1;67(13):6012-6016. [PubMed:
17616655].
Patent Status: U.S. Patent Application No. 11/525,672 filed 22 Sep
2006 (HHS Reference No. E-265-1999/2-US-01).
Licensing Status: Available for licensing.
Licensing Contact: Jennifer Wong; 301-435-4633;
wongje@mail.nih.gov.
Collaborative Research Opportunity: The Urologic Oncology Branch of
the National Cancer Institute is seeking statements of capability or
interest from parties interested in collaborative research to further
develop, evaluate, or commercialize Grb2 SH2 domain antagonists as
anti-cancer drugs. Please contact John D. Hewes, Ph.D. at 301-435-3121
or hewesj@mail.nih.gov for more information.
Dated: October 29, 2010.
Richard U. Rodriguez,
Director, Division of Technology Development and Transfer, Office of
Technology Transfer, National Institutes of Health.
[FR Doc. 2010-27912 Filed 11-3-10; 8:45 am]
BILLING CODE 4140-01-P