Government-Owned Inventions; Availability for Licensing, 31948-31950 [2013-12531]
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31948
Federal Register / Vol. 78, No. 102 / Tuesday, May 28, 2013 / Notices
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regarding this information collection are
best assured of having their full effect if
received within 60 days of the date of
this publication.
Proposed Collection: The National
Institute of Mental Health Data Access
Request and Use Certification
(previously National Database for
Autism Research Data Access Request),
0925–0667, Revision, Expiration Date:
01/31/2016; NIMH, NIH.
Need and Use of Information
Collection: NIMH recently received
OMB approval for use of the National
Database for Autism Research (NDAR)
Data Use Certification (DUC) Form.
NIMH is interested in renaming this
form the ‘‘NIMH Data Access Request
and Use Certification (DUC) Form’’ and
using it to meet the unique data access
needs of all NIMH data repositories. The
NIMH DUC form is necessary for
‘‘Recipient’’ Principal Investigators and
their organization or corporations with
approved assurance from the DHHS
Office of Human Research Protections to
access data or images from NIMH
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the database. There are currently three
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be required to receive copies of the
patent applications.
Assay for Quantifying Fragile X Mental
Retardation-1 Gene Product
[FR Doc. 2013–12601 Filed 5–24–13; 8:45 am]
BILLING CODE 4140–01–P
DEPARTMENT OF HEALTH AND
HUMAN SERVICES
National Institutes of Health
Government-Owned Inventions;
Availability for Licensing
AGENCY:
National Institutes of Health,
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.
mstockstill on DSK4VPTVN1PROD with NOTICES
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
VerDate Mar<15>2010
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Description of Technology: The
invention is directed to a fluorescence
based assay to quantify the protein
product of the Fragile X Mental
Retardation-1 (FMR1) gene in a
biological sample.
Fragile X syndrome (FXS) is an Xlinked genetic disease that is
responsible for intellectual disability
and is also the most common single
gene cause of autism. FXS is typically
caused by loss of expression of the
FMR1 gene, which codes for an RNAbinding protein called FMRP. FXS
patients exhibit a wide spectrum of
symptoms with varying degrees of
cognitive and psychosocial impairment.
The severity of these symptoms
correlates well with the levels of FMRP
present in the FXS patient. Because the
FMR1 gene is silenced in varying
degrees, the levels of FMRP in any
particular FXS patient could vary
greatly.
Scientists at NIDDK and NCATS have
developed a sensitive, time resolved
fluorescence based assay to quantify
FMRP levels in a biological sample.
Unlike other assays, the invention assay
utilizes two highly-specific antibodies
that bind to different sites of FMRP so
as to enable precise and reliable
quantification. Currently, there is no
approved drug to treat FXS. The
invention assay can be used as a high
throughput screen to identify and
evaluate candidate drugs. In addition,
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the invention assay can be used to
assess and/or predict the severity of a
patient’s condition based on the amount
of FMRP present.
Potential Commercial Applications:
• Diagnosis assay
• High throughput screen of drug
libraries
• Optimization assay to further develop
potential drug candidates
Competitive Advantages:
• Fast, accurate, and reliable assay to
quantify FMRP in easy-to-use
fluorescence based format
• Adaptable for high throughput use
Development Stage:
• Prototype
• Pilot
• In vitro data available
Inventors: Wei Zheng (NCATS), Karen
P. Usdin (NIDDK), Manju Swaroop
(NCATS), Daman Kumari (NIDDK)
Intellectual Property: HHS Reference
No. E–083–2013/0—US Application No.
61/793,577 filed 15 March 2013
Licensing Contact: Lauren NguyenAntczak, Ph.D., J.D.; 301–435–4074;
lauren.nguyen-antczak@nih.gov.
Collaborative Research Opportunity:
The National Center for Advancing
Translational Sciences (NCATS) is
seeking statements of capability or
interest from parties interested in
collaborative research to further
develop, evaluate or commercialize
Assay for Quantifying Fragile X Mental
Retardation-1 Gene Product. For
collaboration opportunities, please
contact the NCATS Technology
Development Coordinator at
NCATSPartnerships@mail.nih.gov.
E:\FR\FM\28MYN1.SGM
28MYN1
Federal Register / Vol. 78, No. 102 / Tuesday, May 28, 2013 / Notices
A Novel HIV–1 Entry Inhibitor
mstockstill on DSK4VPTVN1PROD with NOTICES
Description of Technology: The
subject invention describes a novel
polypeptide comprising a single human
CD4 domain (mD1.22) which is highly
soluble and stable with significantly
higher neutralizing activity and lower
non-specific binding to human blood
cell lines. More specifically, mD1.22 is
highly promising for several
applications due to its biophysical
properties: (1) For conjugating with
cytotoxic molecules for eradication of
HIV-infected cells; (2) for generating
multi-specific multi-valent HIV
inhibitors with high neutralization
potency and breadth, and relatively
small molecular size; (3) for generating
nanobio-sensors for rapid HIV detection;
and (4) for studying the biological
functions of CD4 in immune responses
and HIV entry.
Potential Commercial Applications:
• HIV therapeutics
• Prophylactics
• Detection reagents
• Research reagent
Competitive Advantages:
• Does not show measurable interaction
with MHCII.
• Can be solubly expressed in E. coli
with high yields leading to decreased
production costs.
Development Stage:
• Early-stage
• In vitro data available
Inventors: Dimiter Dimitrov, Weizao
Chen, Prabakaran Ponraj (NCI)
Publications:
1. Chen W, et al. Engineered single human
CD4 domains as potent HIV–1 inhibitors
and components of vaccine
immunogens. J Virol. 2011;85(18):9395–
405. [PMID 21715496]
2. 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;88(1):107–
15. [PMID 20709110]
3. Chen W, et al. Human domain antibodies
to conserved sterically restricted regions
on gpl20 as exceptionally potent crossreactive HIV–1 neutralizers. Proc Natl
Acad Sci USA. 2008;105(44):17121–6.
[PMID 18957538]
4. Lagenaur LA, et al. sCD4–17b bifunctional
proteins: extremely broad and potent
neutralization of HIV–1 Env
pseudotyped viruses from genetically
diverse primary isolates. Retrovirology
2010 Feb 16;7:11. [PMID 20158904]
5. Saha P, et al. Design and characterization
of stabilized derivatives of human
CD4D12 and CD4D1. Biochemistry 2011
Sep 20;50(37):7891–900. [PMID
21827143]
Intellectual Property: HHS Reference
No. E–033–2013/0—US Provisional
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17:46 May 24, 2013
Jkt 229001
Patent Application No. 61/791,885 filed
15 Mar 2013
Related Technologies: HHS Reference
No. E–103–2010/1—
• PCT Application No. PCT/US2011/
3743961 filed on 20 May 2011
• National stage filing in EP (EP
Application No. 11722270.3) and in
USA (US Application No. 13/699,535)
on 21 Nov. 2012
Licensing Contact: Sally H. Hu, Ph.D.,
M.B.A.; 301–435–5606;
hus@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 A Novel HIV-1 Entry
Inhibitor. For collaboration
opportunities, please contact John D.
Hewes, Ph.D. at hewesj@mail.nih.gov.
Novel Fusion Proteins for HIV Vaccine
31949
3. Xiang SH, et al. Mutagenic stabilization
and/or disruption of a CD4-bound state
reveals distinct conformations of the
human immunodeficiency virus type 1
gp120 envelope glycoprotein. J Virol.
2002 Oct;76(19):9888–99. [PMID
12208966]
Intellectual Property: HHS Reference
No. E–256–2012/0—Research Tool.
Patent protection is not being pursued
for this technology.
Licensing Contact: Sally H. Hu, Ph.D.,
M.B.A.; 301–435–5605;
hus@mail.nih.gov.
Collaborative Research Opportunity:
The National Cancer Institute (NCI) is
seeking statements of capability or
interest from parties interested in
collaborative research to further
develop, evaluate or commercialize
Novel Fusion Proteins for HIV Vaccine.
For collaboration opportunities, please
contact John D. Hewes, Ph.D. at
hewesj@mail.nih.gov.
Description of Technology: The
subject invention describes novel fusion
proteins (CD4i antibody-HIV-1 envelop
glycoprotein (gp120)) which can be used
as (1) potential vaccine immunogens
that could be more efficient than gp120
alone; (2) candidate therapeutics; and
(3) research reagents for exploration of
HIV–1 gp120 conformational flexibility,
elucidation of mechanisms of virus
entry, and evasion of immune
responses.
Potential Commercial Applications:
• Develop HIV vaccine
• Research reagent
• Research tools to study the
conformations flexibility of gp120, the
mechanisms of virus entry, and
evasion of immune responses
Competitive Advantages:
• The potential vaccine immunogens
that could be more efficient than
gp120 alone
• Higher affinity with CD4 and
antibodies directed against CD4binding site than gp120 alone
Development Stage:
• Early-stage
• In vitro data available
Inventors: Dimiter Dimitrov and
Weizao Chen (NCI)
Publications:
A Novel Human Antibody for
Deploying CH2 Based Therapeutics
Description of Technology: The
subject invention describes a novel
human antibody (anti-CH2 Fab m01m1)
which could be used safely in vitro and
in vivo for the detection of CH2 (Fc and
IgG as well). More specifically, anti-CH2
Fab m01m1 recognizes a conformational
epitope on CH2 so it can be used to
monitor the conformational changes
when CH2 is modified and mutated, as
well as to select proper folded isolated
CH2 domains. Thus, anti-CH2 Fab
m01m1 is a powerful research reagent
for developing the CH2-based novel
therapeutics (nanoantibodies, nAbs) and
for identifying several binders against
various antigens from CH2-based
libraries.
Potential Commercial Applications:
• Research reagent
• Facilitate the development of CH2based novel therapeutics
• Can be used as a library for
therapeutic candidates
Competitive Advantages: Novel
antibody.
1. Dey B, et al. Characterization of human
immunodeficiency virus type 1
monomeric and trimeric gp120
glycoproteins stabilized in the CD4bound state: antigenicity, biophysics,
and immunogenicity. J Virol. 2007
Jun;81(11):5579–93. [PMID 17360741]
2. Dey B, et al. Structure-based stabilization
of HIV-1 gp120 enhances humoral
immune responses to the induced coreceptor binding site. PLoS Pathog. 2009
May;5(5):el000445. [PMID 19478876]
1. Prabakaran P, et al. Structure of an isolated
unglycosylated antibody C(H)2 domain.
Acta Crystallogr D Biol Crystallogr. 2008
Oct; 64(Pt 10):1062–7. [PMID 18931413]
2. Dimitrov DS. Engineered CH2 domains
(nanoantibodies). MAbs. 2009 Jan–
Feb;1(1):26–8. [PMID 20046570]
3. Gong R, et al. Engineered human antibody
constant domains with increased
stability. J Biol Chem. 2009 May
22;284(21):14203–10. [PMID 19307178]
4. Xiao X, et al. A large library based on a
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Development Stage:
• Early-stage
• In vitro data available
Publications:
E:\FR\FM\28MYN1.SGM
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31950
Federal Register / Vol. 78, No. 102 / Tuesday, May 28, 2013 / Notices
novel (CH2) scaffold: identification of
HIV-1 inhibitors. Biochem Biophys Res
Commun. 2009 Sep 18;387(2):387–92.
[PMID 19615335]
5. Wozniak-Knopp G, et al. Stabilisation of
the Fc fragment of human IgG1 by
engineered intradomain disulfide bonds.
PLoS One. 2012;7(1):e30083 [PMID
22272277]
Inventors: Dimiter Dimitrov (NCI) and
Rui Gong (formerly NCI).
Intellectual Property: HHS Reference
No. E–245–2012/0—Research Tool.
Patent protection is not being pursued
for this technology.
Licensing Contact: Sally H. Hu, Ph.D.,
M.B.A.; 301–435–5606;
hus@mail.nih.gov
Collaborative Research Opportunity:
The National Cancer Institute (NCI) is
seeking statements of capability or
interest from parties interested in
collaborative research to further
develop, evaluate or commercialize A
Novel Human Antibody for Deploying
CH2 Based Therapeutics. For
collaboration opportunities, please
contact John D. Hewes, Ph.D. at
hewesj@mail.nih.gov.
mstockstill on DSK4VPTVN1PROD with NOTICES
Methods for Producing Stem Cell-like
Memory T cells for Use in T cell-based
Immunotherapies
Description of Technology: T cells
currently employed for T cell-based
immunotherapies are often senescent,
terminally differentiated cells with poor
proliferate and survival capacity.
Recently, however, NIH scientists
identified and characterized a new
human memory T cell population with
stem cell-like properties. Since these T
cells have limited quantities in vivo, the
scientists have developed methods by
which high numbers of these cells can
be generated ex vivo for use in T cellbased immunotherapies. Specifically,
this technology describes a method for
generating the stem cell-like memory T
cells by stimulating naive T cells in the
presence of inhibitors of GSK-3beta. It
also describes a method for obtaining
the stem cell-like memory T cells by
sorting T cell lymphocytes using flow
cytometry. These stem cell-like memory
T cells display enhanced proliferation
and survival upon transfer, have the
multipotent capacity to generate all
memory and effector T cell subsets and
show increased anti-tumor activity in a
humanized mouse tumor model.
Consequently, the coupling of T cell
receptor or chimeric receptor gene
transfer with this method will enable
the generation of a large number of
memory stem cells with the desired
specificity to effectively treat patients
with cancer and chronic infectious
diseases.
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Potential Commercial Applications:
• Ex vivo generation of stem cell-like
memory T cells for T cell-based
immunotherapy
• Treatment for patients with cancer
and chronic infectious diseases
Competitive Advantages:
• Enhanced proliferation and survival
upon transfer
• Multipotent capacity to generate all
memory and effector T cell subsets
• Increased anti-tumor actovity
Development Stage:
• Pre-clinical
• In vitro data available
• In vivo data available (animal)
Inventors: Luca Gattinoni (NCI),
Enrico Lugli (NIAID), Mario Roederer
(NIAID), Nicholas Restifo (NCI)
Publications:
1. Gattinoni L, et al. A human T cell memory
subset with stem cell-like properties. Nat
Med. 2011 Sep 18;17(10):1290–7. [PMID
21926977]
2. Gattinoni L, et al. Wnt signaling arrests
effector T cell differentiation and
generates CD8+ memory stem cells. Nat
Med. 2009 Jul;15(7):808–13. [PMID
19525962]
3. Lugli E, et al. Identification, isolation and
in vitro expansion of human and
nonhuman primate T stem cell memory
cells. Nat Protoc. 2013 Jan;8(1):33–42.
[PMID 23222456]
Intellectual Property: HHS Reference
No. E–174–2012/0—PCT Application
No. PCT/US12/053947 filed 06 Sep
2012
Licensing Contact: Whitney Hastings;
301–451–7337; hastingw@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 the use of T memory
stem cells for T cell-based
immunotherapies. For collaboration
opportunities, please contact Luca
Gattinoni at gattinol@mail.nih.gov or
301–451–6914, or Nicholas Restifo at
restifo@nih.gov or 301–496–4904.
Dated: May 21, 2013.
Richard U. Rodriguez,
Director, Division of Technology Development
and Transfer, Office of Technology Transfer,
National Institutes of Health.
[FR Doc. 2013–12531 Filed 5–24–13; 8:45 am]
BILLING CODE 4140–01–P
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DEPARTMENT OF HEALTH AND
HUMAN SERVICES
National Institutes of Health
National Institute of Diabetes and
Digestive and Kidney Diseases; Notice
of Closed Meetings
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 meetings.
The meetings 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
Diabetes and Digestive and Kidney Diseases
Special Emphasis Panel; Time-Sensitive
Obesity Prevention.
Date: June 24, 2013.
Time: 11:00 a.m. to 12:30 p.m.
Agenda: To review and evaluate grant
applications.
Place: National Institutes of Health, Two
Democracy Plaza, 6707 Democracy
Boulevard, Bethesda, MD 20892, (Telephone
Conference Call).
Contact Person: Michele L. Barnard, PhD,
Scientific Review Officer, Review Branch,
DEA, NIDDK, National Institutes of Health,
Room 753, 6707 Democracy Boulevard,
Bethesda, MD 20892–2542, (301) 594–8898,
barnardm@extra.niddk.nih.gov.
Name of Committee: National Institute of
Diabetes and Digestive and Kidney Diseases
Special Emphasis Panel; Close Loop
Technologies.
Date: July 2, 2013.
Time: 11:00 a.m. to 3:00 p.m.
Agenda: To review and evaluate grant
applications.
Place: National Institutes of Health, Two
Democracy Plaza, 6707 Democracy
Boulevard, Bethesda, MD 20892, (Telephone
Conference Call).
Contact Person: Elena Sanovich, PhD,
Scientific Review Officer, Review Branch,
DEA, NIDDK, National Institutes of Health,
Room 750, 6707 Democracy Boulevard,
Bethesda, MD 20892–2542, 301–594–8886,
sanoviche@mail.nih.gov.
Name of Committee: National Institute of
Diabetes and Digestive and Kidney Diseases
Special Emphasis Panel; Advancing Clinical
Research in Primary Glomerular Diseases
(UM1).
Date: July 8, 2013.
Time: 2:00 p.m. to 6:00 p.m.
Agenda: To review and evaluate grant
applications.
Place: National Institutes of Health, Two
Democracy Plaza, 6707 Democracy
E:\FR\FM\28MYN1.SGM
28MYN1
]]>Agencies
[Federal Register Volume 78, Number 102 (Tuesday, May 28, 2013)]
[Notices]
[Pages 31948-31950]
From the Federal Register Online via the Government Printing Office [www.gpo.gov]
[FR Doc No: 2013-12531]
-----------------------------------------------------------------------
DEPARTMENT OF HEALTH AND HUMAN SERVICES
National Institutes of Health
Government-Owned Inventions; Availability for Licensing
AGENCY: National Institutes of Health, 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.
Assay for Quantifying Fragile X Mental Retardation-1 Gene Product
Description of Technology: The invention is directed to a
fluorescence based assay to quantify the protein product of the Fragile
X Mental Retardation-1 (FMR1) gene in a biological sample.
Fragile X syndrome (FXS) is an X-linked genetic disease that is
responsible for intellectual disability and is also the most common
single gene cause of autism. FXS is typically caused by loss of
expression of the FMR1 gene, which codes for an RNA-binding protein
called FMRP. FXS patients exhibit a wide spectrum of symptoms with
varying degrees of cognitive and psychosocial impairment. The severity
of these symptoms correlates well with the levels of FMRP present in
the FXS patient. Because the FMR1 gene is silenced in varying degrees,
the levels of FMRP in any particular FXS patient could vary greatly.
Scientists at NIDDK and NCATS have developed a sensitive, time
resolved fluorescence based assay to quantify FMRP levels in a
biological sample. Unlike other assays, the invention assay utilizes
two highly-specific antibodies that bind to different sites of FMRP so
as to enable precise and reliable quantification. Currently, there is
no approved drug to treat FXS. The invention assay can be used as a
high throughput screen to identify and evaluate candidate drugs. In
addition, the invention assay can be used to assess and/or predict the
severity of a patient's condition based on the amount of FMRP present.
Potential Commercial Applications:
Diagnosis assay
High throughput screen of drug libraries
Optimization assay to further develop potential drug
candidates
Competitive Advantages:
Fast, accurate, and reliable assay to quantify FMRP in easy-
to-use fluorescence based format
Adaptable for high throughput use
Development Stage:
Prototype
Pilot
In vitro data available
Inventors: Wei Zheng (NCATS), Karen P. Usdin (NIDDK), Manju Swaroop
(NCATS), Daman Kumari (NIDDK)
Intellectual Property: HHS Reference No. E-083-2013/0--US
Application No. 61/793,577 filed 15 March 2013
Licensing Contact: Lauren Nguyen-Antczak, Ph.D., J.D.; 301-435-
4074; lauren.nguyen-antczak@nih.gov.
Collaborative Research Opportunity: The National Center for
Advancing Translational Sciences (NCATS) is seeking statements of
capability or interest from parties interested in collaborative
research to further develop, evaluate or commercialize Assay for
Quantifying Fragile X Mental Retardation-1 Gene Product. For
collaboration opportunities, please contact the NCATS Technology
Development Coordinator at NCATSPartnerships@mail.nih.gov.
[[Page 31949]]
A Novel HIV-1 Entry Inhibitor
Description of Technology: The subject invention describes a novel
polypeptide comprising a single human CD4 domain (mD1.22) which is
highly soluble and stable with significantly higher neutralizing
activity and lower non-specific binding to human blood cell lines. More
specifically, mD1.22 is highly promising for several applications due
to its biophysical properties: (1) For conjugating with cytotoxic
molecules for eradication of HIV-infected cells; (2) for generating
multi-specific multi-valent HIV inhibitors with high neutralization
potency and breadth, and relatively small molecular size; (3) for
generating nanobio-sensors for rapid HIV detection; and (4) for
studying the biological functions of CD4 in immune responses and HIV
entry.
Potential Commercial Applications:
HIV therapeutics
Prophylactics
Detection reagents
Research reagent
Competitive Advantages:
Does not show measurable interaction with MHCII.
Can be solubly expressed in E. coli with high yields leading
to decreased production costs.
Development Stage:
Early-stage
In vitro data available
Inventors: Dimiter Dimitrov, Weizao Chen, Prabakaran Ponraj (NCI)
Publications:
1. Chen W, et al. Engineered single human CD4 domains as potent HIV-
1 inhibitors and components of vaccine immunogens. J Virol.
2011;85(18):9395-405. [PMID 21715496]
2. 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;88(1):107-
15. [PMID 20709110]
3. Chen W, et al. Human domain antibodies to conserved sterically
restricted regions on gpl20 as exceptionally potent cross-reactive
HIV-1 neutralizers. Proc Natl Acad Sci USA. 2008;105(44):17121-6.
[PMID 18957538]
4. Lagenaur LA, et al. sCD4-17b bifunctional proteins: extremely
broad and potent neutralization of HIV-1 Env pseudotyped viruses
from genetically diverse primary isolates. Retrovirology 2010 Feb
16;7:11. [PMID 20158904]
5. Saha P, et al. Design and characterization of stabilized
derivatives of human CD4D12 and CD4D1. Biochemistry 2011 Sep
20;50(37):7891-900. [PMID 21827143]
Intellectual Property: HHS Reference No. E-033-2013/0--US
Provisional Patent Application No. 61/791,885 filed 15 Mar 2013
Related Technologies: HHS Reference No. E-103-2010/1--
PCT Application No. PCT/US2011/3743961 filed on 20 May 2011
National stage filing in EP (EP Application No. 11722270.3)
and in USA (US Application No. 13/699,535) on 21 Nov. 2012
Licensing Contact: Sally H. Hu, Ph.D., M.B.A.; 301-435-5606;
hus@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
A Novel HIV-1 Entry Inhibitor. For collaboration opportunities, please
contact John D. Hewes, Ph.D. at hewesj@mail.nih.gov.
Novel Fusion Proteins for HIV Vaccine
Description of Technology: The subject invention describes novel
fusion proteins (CD4i antibody-HIV-1 envelop glycoprotein (gp120))
which can be used as (1) potential vaccine immunogens that could be
more efficient than gp120 alone; (2) candidate therapeutics; and (3)
research reagents for exploration of HIV-1 gp120 conformational
flexibility, elucidation of mechanisms of virus entry, and evasion of
immune responses.
Potential Commercial Applications:
Develop HIV vaccine
Research reagent
Research tools to study the conformations flexibility of
gp120, the mechanisms of virus entry, and evasion of immune responses
Competitive Advantages:
The potential vaccine immunogens that could be more efficient
than gp120 alone
Higher affinity with CD4 and antibodies directed against CD4-
binding site than gp120 alone
Development Stage:
Early-stage
In vitro data available
Inventors: Dimiter Dimitrov and Weizao Chen (NCI)
Publications:
1. Dey B, et al. Characterization of human immunodeficiency virus
type 1 monomeric and trimeric gp120 glycoproteins stabilized in the
CD4-bound state: antigenicity, biophysics, and immunogenicity. J
Virol. 2007 Jun;81(11):5579-93. [PMID 17360741]
2. Dey B, et al. Structure-based stabilization of HIV-1 gp120
enhances humoral immune responses to the induced co-receptor binding
site. PLoS Pathog. 2009 May;5(5):el000445. [PMID 19478876]
3. Xiang SH, et al. Mutagenic stabilization and/or disruption of a
CD4-bound state reveals distinct conformations of the human
immunodeficiency virus type 1 gp120 envelope glycoprotein. J Virol.
2002 Oct;76(19):9888-99. [PMID 12208966]
Intellectual Property: HHS Reference No. E-256-2012/0--Research
Tool. Patent protection is not being pursued for this technology.
Licensing Contact: Sally H. Hu, Ph.D., M.B.A.; 301-435-5605;
hus@mail.nih.gov.
Collaborative Research Opportunity: The National Cancer Institute
(NCI) is seeking statements of capability or interest from parties
interested in collaborative research to further develop, evaluate or
commercialize Novel Fusion Proteins for HIV Vaccine. For collaboration
opportunities, please contact John D. Hewes, Ph.D. at
hewesj@mail.nih.gov.
A Novel Human Antibody for Deploying CH2 Based Therapeutics
Description of Technology: The subject invention describes a novel
human antibody (anti-CH2 Fab m01m1) which could be used safely in vitro
and in vivo for the detection of CH2 (Fc and IgG as well). More
specifically, anti-CH2 Fab m01m1 recognizes a conformational epitope on
CH2 so it can be used to monitor the conformational changes when CH2 is
modified and mutated, as well as to select proper folded isolated CH2
domains. Thus, anti-CH2 Fab m01m1 is a powerful research reagent for
developing the CH2-based novel therapeutics (nanoantibodies, nAbs) and
for identifying several binders against various antigens from CH2-based
libraries.
Potential Commercial Applications:
Research reagent
Facilitate the development of CH2-based novel therapeutics
Can be used as a library for therapeutic candidates
Competitive Advantages: Novel antibody.
Development Stage:
Early-stage
In vitro data available
Publications:
1. Prabakaran P, et al. Structure of an isolated unglycosylated
antibody C(H)2 domain. Acta Crystallogr D Biol Crystallogr. 2008
Oct; 64(Pt 10):1062-7. [PMID 18931413]
2. Dimitrov DS. Engineered CH2 domains (nanoantibodies). MAbs. 2009
Jan-Feb;1(1):26-8. [PMID 20046570]
3. Gong R, et al. Engineered human antibody constant domains with
increased stability. J Biol Chem. 2009 May 22;284(21):14203-10.
[PMID 19307178]
4. Xiao X, et al. A large library based on a
[[Page 31950]]
novel (CH2) scaffold: identification of HIV-1 inhibitors. Biochem
Biophys Res Commun. 2009 Sep 18;387(2):387-92. [PMID 19615335]
5. Wozniak-Knopp G, et al. Stabilisation of the Fc fragment of human
IgG1 by engineered intradomain disulfide bonds. PLoS One.
2012;7(1):e30083 [PMID 22272277]
Inventors: Dimiter Dimitrov (NCI) and Rui Gong (formerly NCI).
Intellectual Property: HHS Reference No. E-245-2012/0--Research
Tool. Patent protection is not being pursued for this technology.
Licensing Contact: Sally H. Hu, Ph.D., M.B.A.; 301-435-5606;
hus@mail.nih.gov
Collaborative Research Opportunity: The National Cancer Institute
(NCI) is seeking statements of capability or interest from parties
interested in collaborative research to further develop, evaluate or
commercialize A Novel Human Antibody for Deploying CH2 Based
Therapeutics. For collaboration opportunities, please contact John D.
Hewes, Ph.D. at hewesj@mail.nih.gov.
Methods for Producing Stem Cell-like Memory T cells for Use in T cell-
based Immunotherapies
Description of Technology: T cells currently employed for T cell-
based immunotherapies are often senescent, terminally differentiated
cells with poor proliferate and survival capacity. Recently, however,
NIH scientists identified and characterized a new human memory T cell
population with stem cell-like properties. Since these T cells have
limited quantities in vivo, the scientists have developed methods by
which high numbers of these cells can be generated ex vivo for use in T
cell-based immunotherapies. Specifically, this technology describes a
method for generating the stem cell-like memory T cells by stimulating
naive T cells in the presence of inhibitors of GSK-3beta. It also
describes a method for obtaining the stem cell-like memory T cells by
sorting T cell lymphocytes using flow cytometry. These stem cell-like
memory T cells display enhanced proliferation and survival upon
transfer, have the multipotent capacity to generate all memory and
effector T cell subsets and show increased anti-tumor activity in a
humanized mouse tumor model. Consequently, the coupling of T cell
receptor or chimeric receptor gene transfer with this method will
enable the generation of a large number of memory stem cells with the
desired specificity to effectively treat patients with cancer and
chronic infectious diseases.
Potential Commercial Applications:
Ex vivo generation of stem cell-like memory T cells for T
cell-based immunotherapy
Treatment for patients with cancer and chronic infectious
diseases
Competitive Advantages:
Enhanced proliferation and survival upon transfer
Multipotent capacity to generate all memory and effector T
cell subsets
Increased anti-tumor actovity
Development Stage:
Pre-clinical
In vitro data available
In vivo data available (animal)
Inventors: Luca Gattinoni (NCI), Enrico Lugli (NIAID), Mario
Roederer (NIAID), Nicholas Restifo (NCI)
Publications:
1. Gattinoni L, et al. A human T cell memory subset with stem cell-
like properties. Nat Med. 2011 Sep 18;17(10):1290-7. [PMID 21926977]
2. Gattinoni L, et al. Wnt signaling arrests effector T cell
differentiation and generates CD8+ memory stem cells. Nat Med. 2009
Jul;15(7):808-13. [PMID 19525962]
3. Lugli E, et al. Identification, isolation and in vitro expansion
of human and nonhuman primate T stem cell memory cells. Nat Protoc.
2013 Jan;8(1):33-42. [PMID 23222456]
Intellectual Property: HHS Reference No. E-174-2012/0--PCT
Application No. PCT/US12/053947 filed 06 Sep 2012
Licensing Contact: Whitney Hastings; 301-451-7337;
hastingw@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
the use of T memory stem cells for T cell-based immunotherapies. For
collaboration opportunities, please contact Luca Gattinoni at
gattinol@mail.nih.gov or 301-451-6914, or Nicholas Restifo at
restifo@nih.gov or 301-496-4904.
Dated: May 21, 2013.
Richard U. Rodriguez,
Director, Division of Technology Development and Transfer, Office of
Technology Transfer, National Institutes of Health.
[FR Doc. 2013-12531 Filed 5-24-13; 8:45 am]
BILLING CODE 4140-01-P
