Government-Owned Inventions; Availability for Licensing, 10537-10539 [2014-03957]
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VIII. Other Information
IHS Area Offices and Service Units
that are financially able are authorized
to provide additional funding to make
awards to applicants in the LRP, but not
to exceed $35,000 a year plus tax
assistance. All additional funding must
be made in accordance with the priority
system outlined below. Health
professions given priority for selection
above the $20,000 threshold are those
identified as meeting the criteria in 25
U.S.C. 1616a(g)(2)(A) which provides
that the Secretary shall consider the
extent to which each such
determination:
(i) Affects the ability of the Secretary
to maximize the number of contracts
that can be provided under the LRP
from the amounts appropriated for such
contracts;
(ii) Provides an incentive to serve in
Indian health programs with the greatest
shortages of health professionals; and
(iii) Provides an incentive with
respect to the health professional
involved remaining in an Indian health
program with such a health professional
shortage, and continuing to provide
primary health services, after the
completion of the period of obligated
service under the LRP.
Contracts may be awarded to those
who are available for service no later
than September 30, 2014, and must be
in compliance with any limits in the
appropriation and Section 108 of the
IHCIA not to exceed the amount
authorized in the IHS appropriation (up
to $32,000,000 for FY 2014). In order to
ensure compliance with the statutes,
Area Offices or Service Units providing
additional funding under this section
are responsible for notifying the LRP of
such payments before funding is offered
to the LRP participant.
Should an IHS Area Office contribute
to the LRP, those funds will be used for
only those sites located in that Area.
Those sites will retain their relative
ranking from the national site-ranking
list. For example, the Albuquerque Area
Office identifies supplemental monies
for dentists. Only the dental positions
within the Albuquerque Area will be
funded with the supplemental monies
consistent with the national ranking and
site index within that Area.
Should an IHS Service Unit
contribute to the LRP, those funds will
be used for only those sites located in
that Service Unit. Those sites will retain
their relative ranking from the national
site-ranking list. For example,
Whiteriver Service Unit identifies
supplemental monies for nurses. The
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Whiteriver Service Unit consists of two
facilities, namely the Whiteriver PHS
Indian Hospital and the Cibecue Indian
Health Center. The national ranking will
be used for the Whiteriver PHS Indian
Hospital (Score = 79) and the Cibecue
Indian Health Center (Score = 95). With
a score of 95, the Cibecue Indian Health
Center would receive priority over the
Whiteriver PHS Indian Hospital.
Dated: February 14, 2014.
Yvette Roubideaux,
Acting Director, Indian Health Service.
[FR Doc. 2014–04075 Filed 2–24–14; 8:45 am]
BILLING CODE 4165–16–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.
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. 209 and 37 CFR Part 404 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.
SUMMARY:
Methods for Amelioration and
Treatment of Pathogen-Associated
Inflammatory Response
Description of Technology: This CDC
invention provides methods for
preventing or treating inflammatory
response-linked, infection induced
pathologies, which are mediated by
endogenous substance P. Substance P is
a naturally-occurring and major proinflammatory neuromediator or
neuromodulator, and elevated levels of
substance P have been implicated in
numerous inflammation-associated
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10537
diseases. More specifically, this
technology entails administration of
anti-substance P antibodies or antisubstance P antibody fragments to a
subject in need, thereby inhibiting the
activity of endogenous substance P.
Small molecule anti-inflammatory
agents currently employed to treat
inflammation frequently cause adverse
side effects, such as gastrointestinal
discomfort and decreased blood clotting
efficiency. Use of steroid-based antiinflammatory drugs may result in
reduced adrenal gland function and
generalized immune system inhibition.
This technology specifically targets and
alleviates substance P-induced hyperinflammatory diseases, potentially
avoiding the complications associated
with other anti-inflammatory
compounds. Blocking the activity of
endogenous substance P potentially can
be employed to prevent or treat a wide
variety of diseases or syndromes caused
in whole or part by an inflammatory
response mediated by substance P.
These include, but are not limited to,
virus-mediated bronchiolitis including
that mediated by respiratory syncytial
virus, bacterial colitis, inflammation
associated with chlamydial diseases,
lung injury associated with
staphylococcal enterotoxin B,
inflammation due to cytomegalovirus or
hepatitis B virus, sepsis, allergic
diseases such as asthma, autoimmune
diseases such as rheumatoid arthritis,
pancreatitis, inflammatory bowel
disease, inflammation associated with
multiple sclerosis, and rejection of
allografts and other transplanted tissues
or organs.
Potential Commercial Applications:
• Treatment of pathogen induced
inflammation, especially bronchiolitis
• Prevention or lessening of adverse
effects associated with other antiinflammatory agents
• Amelioration of pain
Competitive Advantages:
• Useful for management of
numerous inflammatory-related viral
and/or bacterial infections
• May reduce or circumvent adverse
side effects associated with other smallmolecule and/or steroid-based antiinflammatory treatments
Development Stage:
• In vitro data available
• In vivo data available (animal)
Inventors:
Ralph A. Tripp, Larry J. Anderson, Deborah
D. Moore (all of CDC)
Publication:
Tripp RA, et al. Respiratory syncytial virus
infection and G and/or SH protein
expression contribute to substance P,
which mediates inflammation and
enhanced pulmonary disease in BALB/c
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Federal Register / Vol. 79, No. 37 / Tuesday, February 25, 2014 / Notices
second variable loop (V2) of HIV–1
gp120 stabilizes V2–V3 interaction and
modulates neutralization sensitivity.
Proc Natl Acad Sci USA. E-pub before
print, 2014 Feb 03. [doi:10.1073/
pnas.1314718111]
mice. J Virol. 2000 Feb;74(4):1614–22.
[PMID 10644330]
emcdonald on DSK67QTVN1PROD with NOTICES
Intellectual Property: HHS Reference
No. E–236–2013/0—
• PCT Application No. PCT/US2000/
001032 filed 14 Jan 2000
• US Patent No. 7,101,547 issued 05
Sep 2006
• Various international patent
applications pending or issued
Licensing Contact: Whitney Blair, J.D.,
M.P.H.; 301–435–4937; whitney.blair@
nih.gov
Recombinant Sulfated HIV Envelope
Protein and Methods for Making
Protein
Description of Technology: This
technology comprises sulfated
recombinant gp120 proteins and
peptides. Also included are methods for
producing sulfated recombinant gp120
proteins. The focus of this technology is
on sulfation of two tyrosines in the V2
loop of the HIV major envelope
glycoprotein, gp120, which increase the
stability of gp120 and promote the
synthesis of gp120 protein in its native
‘‘closed’’ conformation. Gp120 in its
native form is highly sulfated; however,
recombinant gp120 produced for
vaccines or structural analyses typically
display low levels of V2 tyrosine
sulfation. Sulfation of the V2 loop
results in increased binding to trimerrecognizing anti-HIV antibodies specific
to the V2 loop region of gp120 (PG9,
PG16, CH01, PGT145) and decreased
binding of CD4. The sulfation of
recombinant gp120 is accomplished by
over expression of a tyrosyl
sulfotransferase in the producing cell
line. Preliminary experiments indicate
the recombinant sulfated gp120 proteins
can be used to elicit the formation of
HIV neutralizing antibodies in
immunized animals.
Potential Commercial Applications:
• Design of HIV vaccines
• Production of HIV vaccines
• Induction of Neutralizing
Antibodies
• HIV vaccine booster protein
Competitive Advantages:
• Consistent sulfation/production of
gp120
• Gp120 vaccine component with
improved stability and immunogenicity
• Recombinant gp120 vaccine
component in native conformation
Development Stage:
• Early-stage
• In vitro data available
• In vivo data available (animal)
• Prototype
Inventors: Paolo Lusso and Raffaello
Cimbro (NIAID)
Publication:
Cimbro R, et al. Tyrosine sulfation in the
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Intellectual Property: HHS Reference
No. E–067–2012/0—PCT Application
No. PCT/US2013/074801, claiming
priority to U.S. Provisional Application
No. 61/736,350 filed 12 Dec 2012
Related Technology: Unpublished
modifications to recombinant GP120.
Licensing Contact: Cristina
Thalhammer-Reyero, Ph.D., M.B.A.;
301–435–4507; thalhamc@mail.nih.gov
Collaborative Research Opportunity:
The National Institute of Allergy and
Infectious Diseases is seeking statements
of capability or interest from parties
interested in collaborative research to
further develop, evaluate or
commercialize this technology as a HIV
vaccine component or a therapeutic for
treating HIV. For collaboration
opportunities, please contact Bill
Ronnenberg at wronnenberg@
niaid.nih.gov or 301–451–3522.
Novel Host Target for Treatment of
Hepatitis C Virus Infection
Description of Technology: The
subject technology is a newly
discovered Interferon-lambda 4 (IFNL4)
protein found through analysis of
genomic data derived from primary
human hepatocytes, molecular cloning
and functional annotation. The IFNL4
protein is related to but distinct from
other known IFNs and its expression is
inducible in conditions that mimic viral
infection. Preliminary studies indicate
that this protein may play a role in
impaired natural and treatment induced
clearance of HCV. These findings
suggest that the protein can potentially
be a new target for treating HCV
infection.
Potential Commercial Applications:
• Novel target for treatment of HCV
infection.
• Diagnostics can be developed for
detection of IFNL4 mRNA or protein.
• Existing biological reagents for
detection of IFNL4—expression assays,
antibodies and protein.
Competitive Advantages: IFNL4 is
created by a genetic variant IFNL4deltaG, which is present only in a subset
of individuals, suggesting that IFNL4 is
not an essential protein and its
functional inactivation may be welltolerated.
Development Stage:
• Early-stage
• Pre-clinical
• In vitro data available
Inventors: Liudmila Prokunina (NCI),
Thomas R. O’Brien (NCI), Brian P.
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Muchmore (NCI), Raymond P. Donnelly
(FDA)
Publication:
Prokunina-Olsson L, et al. A variant
upstream of IFNL3 (IL28B) creating
novel interferon gene IFNL4 is associated
with impaired clearance of hepatitis C
virus. Nat Genet. 2013 Feb;45(2):164–71.
[PMID 23291588]
Intellectual Property: HHS Reference
No. E–217–2011/1—
• U.S. Provisional Patent Application
No. 61/616,664 filed 28 Mar 2012
• International PCT Application No.
PCT/US13/31624 filed 14 Mar 2013,
which published as WO 2013/148272
on 03 Oct 2013
Related Technology: HHS Reference
No. E–217–2011/0—
• U.S. Provisional Patent Application
No. 61/543,620 filed 05 Oct 2011
• International PCT Application No.
PCT/US2012/59048 filed 05 Oct 2012,
which published as WO 2013/052862
on 11 Apr 2013
Licensing Contact: Kevin W. Chang,
Ph.D.; 301–435–5018; changke@
mail.nih.gov
Collaborative Research Opportunity:
The NCI Division of Cancer
Epidemiology & Genetics, Laboratory of
Translational Genomics, is seeking
statements of capability or interest from
parties interested in collaborative
research to further develop, evaluate or
commercialize development of tools for
detection of IFNL4 mRNA and protein
and modulation of its function. For
collaboration opportunities, please
contact John Hewes, Ph.D. at hewesj@
mail.nih.gov.
Knockout Mouse Models for Study of
Cholesterol Biosynthesis and Metabolic
Diseases
Description of Technology: The
farnesoid X receptor (FXR), also known
as the bile acid receptor (BAR), is
expressed in high levels in the liver and
intestine, and controls the synthesis and
transport of bile acids, which are
degradation products of cholesterol. As
such, FXR is a potential drug target for
a number of metabolic disorders, such
as dyslipidemia, diabetes and
atherosclerosis.
Available for licensing are mouse
models with a total deletion of the FXR
gene (FXR-null mouse), as well as mice
with tissue-specific deletions of the FXR
gene in the liver or in the intestine.
These mice may be useful for the study
of cholesterol and bile acid synthesis
and their role in metabolic disease, as
well as for the development of drugs
targeting FXR.
Potential Commercial Applications:
• Development of FXR/BAR-based
drugs for the treatment of cholesterol
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Federal Register / Vol. 79, No. 37 / Tuesday, February 25, 2014 / Notices
disorders and metabolic diseases
including dyslipidemia, diabetes and
atherosclerosis.
• Study of the role of FXR in
cholesterol biosynthesis and metabolic
disease.
Development Stage: Early-stage
Inventor: Frank J. Gonzalez (NCI)
Publications:
1. Sinal C, et al. Targeted disruption of the
nuclear receptor FXR/BAR impairs bile
acid and lipid homeostasis. Cell. 2000
Sep 15;102(6):731–44. [PMID 11030617]
2. Kim I, et al. Differential regulation of bile
acid homeostasis by the farnesoid X
receptor in liver and intestine. J Lipid
Res. 2007 Dec;48(12):2664–72. [PMID
17720959]
Intellectual Property: Research
Tools—Patent protection is not being
pursued for this technology:
• HHS Reference No. E–323–2001/
0—a mouse line lacking the nuclear
receptor FXR/BAR
• HHS Reference No. E–323–2001/
1—a mouse line lacking FXR/BAR
expression in the liver
• HHS Reference No. E–323–2001/
2—a mouse line lacking FXR/BAR
expression in the intestine
Licensing Contact: Tara L. Kirby,
Ph.D.; 301–435–4426; tarak@
mail.nih.gov
Musculoskeletal Rehabilitation Sciences
Overflow.
Date: February 28, 2014.
Time: 3:00 p.m. to 4:00 p.m.
Agenda: To review and evaluate grant
applications.
Place: Hilton Alexandria Old Town, 1767
King Street, Alexandria, VA 22314.
Contact Person: Jo Pelham, BA, Scientific
Review Officer, Center for Scientific Review,
National Institutes of Health, 6701 Rockledge
Drive, Room 4102, MSC 7814, Bethesda, MD
20892, (301) 435–1786, pelhamj@csr.nih.gov.
This notice is being published less than 15
days prior to the meeting due to the timing
limitations imposed by the review and
funding cycle.
(Catalogue of Federal Domestic Assistance
Program Nos. 93.306, Comparative Medicine;
93.333, Clinical Research, 93.306, 93.333,
93.337, 93.393–93.396, 93.837–93.844,
93.846–93.878, 93.892, 93.893, National
Institutes of Health, HHS)
Dated: February 19, 2014.
Michelle Trout,
Program Analyst, Office of Federal Advisory
Committee Policy.
[FR Doc. 2014–03941 Filed 2–24–14; 8:45 am]
BILLING CODE 4140–01–P
Dated: February 19, 2014.
Richard U. Rodriguez,
Director, Division of Technology Development
and Transfer, Office of Technology Transfer,
National Institutes of Health.
[FR Doc. 2014–03957 Filed 2–24–14; 8:45 am]
BILLING CODE 4140–01–P
DEPARTMENT OF HEALTH AND
HUMAN SERVICES
National Institutes of Health
National Institute of Neurological
Disorders and Stroke; Amended Notice
of Meeting
Center for Scientific Review; 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.
Notice is hereby given of a change in
the meeting of the National Institute of
Neurological Disorders and Stroke
Special Emphasis Panel, January 9,
2014, 09:00 a.m. to January 9, 2014,
01:00 p.m., National Institutes of Health,
Neuroscience Center, 6001 Executive
Boulevard, Rockville, MD 20852 which
was published in the Federal Register
on February 13, 2014, 79FRN8727.
The meeting date has been changed to
March 7, 2014. The time and meeting
location remain the same. The meeting
is closed to the public.
Dated: February 19, 2014.
Carolyn Baum,
Program Analyst, Office of Federal Advisory
Committee Policy.
DEPARTMENT OF HEALTH AND
HUMAN SERVICES
emcdonald on DSK67QTVN1PROD with NOTICES
National Institutes of Health
[FR Doc. 2014–03939 Filed 2–24–14; 8:45 am]
BILLING CODE 4140–01–P
Name of Committee: Center for Scientific
Review Special Emphasis Panel,
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10539
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, Chronic Kidney
Disease (CKD) Biomarkers Consortium Data
Coordinating Center.
Date: March 18, 2014.
Time: 10:00 a.m. to 11:00 a.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: Paul A. Rushing, Ph.D.,
Scientific Review Officer, Review Branch,
DEA, NIDDK, National Institutes Of Health,
Room 747, 6707 Democracy Boulevard,
Bethesda, MD 20892–5452, (301) 594–8895,
rushingp@extra.niddk.nih.gov.
Name of Committee: National Institute of
Diabetes and Digestive and Kidney Diseases
Special Emphasis Panel, Customized Stem
Cells for Clinical Application in Blood
Disorders (R24).
Date: March 25, 2014.
Time: 1:30 p.m. to 2:30 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: Paul A. Rushing, Ph.D.,
Scientific Review Officer, Review Branch,
DEA, NIDDK, National Institutes Of Health,
Room 747, 6707 Democracy Boulevard,
Bethesda, MD 20892–5452, (301) 594–8895,
rushingp@extra.niddk.nih.gov.
Name of Committee: National Institute of
Diabetes and Digestive and Kidney Diseases
Special Emphasis Panel, Cell and Molecular
Dynamics of Hematopoiesis in Vivo (R24).
Date: March 25, 2014.
Time: 12:00 p.m. to 1:00 p.m.
Agenda: To review and evaluate grant
applications.
Place: National Institutes of Health, Two
Democracy Plaza, 6707 Democracy
E:\FR\FM\25FEN1.SGM
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]]>Agencies
[Federal Register Volume 79, Number 37 (Tuesday, February 25, 2014)]
[Notices]
[Pages 10537-10539]
From the Federal Register Online via the Government Printing Office [www.gpo.gov]
[FR Doc No: 2014-03957]
-----------------------------------------------------------------------
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. 209 and 37 CFR Part 404 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.
Methods for Amelioration and Treatment of Pathogen-Associated
Inflammatory Response
Description of Technology: This CDC invention provides methods for
preventing or treating inflammatory response-linked, infection induced
pathologies, which are mediated by endogenous substance P. Substance P
is a naturally-occurring and major pro-inflammatory neuromediator or
neuromodulator, and elevated levels of substance P have been implicated
in numerous inflammation-associated diseases. More specifically, this
technology entails administration of anti-substance P antibodies or
anti-substance P antibody fragments to a subject in need, thereby
inhibiting the activity of endogenous substance P.
Small molecule anti-inflammatory agents currently employed to treat
inflammation frequently cause adverse side effects, such as
gastrointestinal discomfort and decreased blood clotting efficiency.
Use of steroid-based anti-inflammatory drugs may result in reduced
adrenal gland function and generalized immune system inhibition. This
technology specifically targets and alleviates substance P-induced
hyper-inflammatory diseases, potentially avoiding the complications
associated with other anti-inflammatory compounds. Blocking the
activity of endogenous substance P potentially can be employed to
prevent or treat a wide variety of diseases or syndromes caused in
whole or part by an inflammatory response mediated by substance P.
These include, but are not limited to, virus-mediated bronchiolitis
including that mediated by respiratory syncytial virus, bacterial
colitis, inflammation associated with chlamydial diseases, lung injury
associated with staphylococcal enterotoxin B, inflammation due to
cytomegalovirus or hepatitis B virus, sepsis, allergic diseases such as
asthma, autoimmune diseases such as rheumatoid arthritis, pancreatitis,
inflammatory bowel disease, inflammation associated with multiple
sclerosis, and rejection of allografts and other transplanted tissues
or organs.
Potential Commercial Applications:
Treatment of pathogen induced inflammation, especially
bronchiolitis
Prevention or lessening of adverse effects associated with
other anti-inflammatory agents
Amelioration of pain
Competitive Advantages:
Useful for management of numerous inflammatory-related
viral and/or bacterial infections
May reduce or circumvent adverse side effects associated
with other small-molecule and/or steroid-based anti-inflammatory
treatments
Development Stage:
In vitro data available
In vivo data available (animal)
Inventors:
Ralph A. Tripp, Larry J. Anderson, Deborah D. Moore (all of CDC)
Publication:
Tripp RA, et al. Respiratory syncytial virus infection and G and/or
SH protein expression contribute to substance P, which mediates
inflammation and enhanced pulmonary disease in BALB/c
[[Page 10538]]
mice. J Virol. 2000 Feb;74(4):1614-22. [PMID 10644330]
Intellectual Property: HHS Reference No. E-236-2013/0--
PCT Application No. PCT/US2000/001032 filed 14 Jan 2000
US Patent No. 7,101,547 issued 05 Sep 2006
Various international patent applications pending or
issued
Licensing Contact: Whitney Blair, J.D., M.P.H.; 301-435-4937;
whitney.blair@nih.gov
Recombinant Sulfated HIV Envelope Protein and Methods for Making
Protein
Description of Technology: This technology comprises sulfated
recombinant gp120 proteins and peptides. Also included are methods for
producing sulfated recombinant gp120 proteins. The focus of this
technology is on sulfation of two tyrosines in the V2 loop of the HIV
major envelope glycoprotein, gp120, which increase the stability of
gp120 and promote the synthesis of gp120 protein in its native
``closed'' conformation. Gp120 in its native form is highly sulfated;
however, recombinant gp120 produced for vaccines or structural analyses
typically display low levels of V2 tyrosine sulfation. Sulfation of the
V2 loop results in increased binding to trimer-recognizing anti-HIV
antibodies specific to the V2 loop region of gp120 (PG9, PG16, CH01,
PGT145) and decreased binding of CD4. The sulfation of recombinant
gp120 is accomplished by over expression of a tyrosyl sulfotransferase
in the producing cell line. Preliminary experiments indicate the
recombinant sulfated gp120 proteins can be used to elicit the formation
of HIV neutralizing antibodies in immunized animals.
Potential Commercial Applications:
Design of HIV vaccines
Production of HIV vaccines
Induction of Neutralizing Antibodies
HIV vaccine booster protein
Competitive Advantages:
Consistent sulfation/production of gp120
Gp120 vaccine component with improved stability and
immunogenicity
Recombinant gp120 vaccine component in native conformation
Development Stage:
Early-stage
In vitro data available
In vivo data available (animal)
Prototype
Inventors: Paolo Lusso and Raffaello Cimbro (NIAID)
Publication:
Cimbro R, et al. Tyrosine sulfation in the second variable loop (V2)
of HIV-1 gp120 stabilizes V2-V3 interaction and modulates
neutralization sensitivity. Proc Natl Acad Sci USA. E-pub before
print, 2014 Feb 03. [doi:10.1073/pnas.1314718111]
Intellectual Property: HHS Reference No. E-067-2012/0--PCT
Application No. PCT/US2013/074801, claiming priority to U.S.
Provisional Application No. 61/736,350 filed 12 Dec 2012
Related Technology: Unpublished modifications to recombinant GP120.
Licensing Contact: Cristina Thalhammer-Reyero, Ph.D., M.B.A.; 301-
435-4507; thalhamc@mail.nih.gov
Collaborative Research Opportunity: The National Institute of
Allergy and Infectious Diseases is seeking statements of capability or
interest from parties interested in collaborative research to further
develop, evaluate or commercialize this technology as a HIV vaccine
component or a therapeutic for treating HIV. For collaboration
opportunities, please contact Bill Ronnenberg at
wronnenberg@niaid.nih.gov or 301-451-3522.
Novel Host Target for Treatment of Hepatitis C Virus Infection
Description of Technology: The subject technology is a newly
discovered Interferon-lambda 4 (IFNL4) protein found through analysis
of genomic data derived from primary human hepatocytes, molecular
cloning and functional annotation. The IFNL4 protein is related to but
distinct from other known IFNs and its expression is inducible in
conditions that mimic viral infection. Preliminary studies indicate
that this protein may play a role in impaired natural and treatment
induced clearance of HCV. These findings suggest that the protein can
potentially be a new target for treating HCV infection.
Potential Commercial Applications:
Novel target for treatment of HCV infection.
Diagnostics can be developed for detection of IFNL4 mRNA
or protein.
Existing biological reagents for detection of IFNL4--
expression assays, antibodies and protein.
Competitive Advantages: IFNL4 is created by a genetic variant
IFNL4-deltaG, which is present only in a subset of individuals,
suggesting that IFNL4 is not an essential protein and its functional
inactivation may be well-tolerated.
Development Stage:
Early-stage
Pre-clinical
In vitro data available
Inventors: Liudmila Prokunina (NCI), Thomas R. O'Brien (NCI), Brian
P. Muchmore (NCI), Raymond P. Donnelly (FDA)
Publication:
Prokunina-Olsson L, et al. A variant upstream of IFNL3 (IL28B)
creating novel interferon gene IFNL4 is associated with impaired
clearance of hepatitis C virus. Nat Genet. 2013 Feb;45(2):164-71.
[PMID 23291588]
Intellectual Property: HHS Reference No. E-217-2011/1--
U.S. Provisional Patent Application No. 61/616,664 filed
28 Mar 2012
International PCT Application No. PCT/US13/31624 filed 14
Mar 2013, which published as WO 2013/148272 on 03 Oct 2013
Related Technology: HHS Reference No. E-217-2011/0--
U.S. Provisional Patent Application No. 61/543,620 filed
05 Oct 2011
International PCT Application No. PCT/US2012/59048 filed
05 Oct 2012, which published as WO 2013/052862 on 11 Apr 2013
Licensing Contact: Kevin W. Chang, Ph.D.; 301-435-5018;
changke@mail.nih.gov
Collaborative Research Opportunity: The NCI Division of Cancer
Epidemiology & Genetics, Laboratory of Translational Genomics, is
seeking statements of capability or interest from parties interested in
collaborative research to further develop, evaluate or commercialize
development of tools for detection of IFNL4 mRNA and protein and
modulation of its function. For collaboration opportunities, please
contact John Hewes, Ph.D. at hewesj@mail.nih.gov.
Knockout Mouse Models for Study of Cholesterol Biosynthesis and
Metabolic Diseases
Description of Technology: The farnesoid X receptor (FXR), also
known as the bile acid receptor (BAR), is expressed in high levels in
the liver and intestine, and controls the synthesis and transport of
bile acids, which are degradation products of cholesterol. As such, FXR
is a potential drug target for a number of metabolic disorders, such as
dyslipidemia, diabetes and atherosclerosis.
Available for licensing are mouse models with a total deletion of
the FXR gene (FXR-null mouse), as well as mice with tissue-specific
deletions of the FXR gene in the liver or in the intestine. These mice
may be useful for the study of cholesterol and bile acid synthesis and
their role in metabolic disease, as well as for the development of
drugs targeting FXR.
Potential Commercial Applications:
Development of FXR/BAR-based drugs for the treatment of
cholesterol
[[Page 10539]]
disorders and metabolic diseases including dyslipidemia, diabetes and
atherosclerosis.
Study of the role of FXR in cholesterol biosynthesis and
metabolic disease.
Development Stage: Early-stage
Inventor: Frank J. Gonzalez (NCI)
Publications:
1. Sinal C, et al. Targeted disruption of the nuclear receptor FXR/
BAR impairs bile acid and lipid homeostasis. Cell. 2000 Sep
15;102(6):731-44. [PMID 11030617]
2. Kim I, et al. Differential regulation of bile acid homeostasis by
the farnesoid X receptor in liver and intestine. J Lipid Res. 2007
Dec;48(12):2664-72. [PMID 17720959]
Intellectual Property: Research Tools--Patent protection is not
being pursued for this technology:
HHS Reference No. E-323-2001/0--a mouse line lacking the
nuclear receptor FXR/BAR
HHS Reference No. E-323-2001/1--a mouse line lacking FXR/
BAR expression in the liver
HHS Reference No. E-323-2001/2--a mouse line lacking FXR/
BAR expression in the intestine
Licensing Contact: Tara L. Kirby, Ph.D.; 301-435-4426;
tarak@mail.nih.gov
Dated: February 19, 2014.
Richard U. Rodriguez,
Director, Division of Technology Development and Transfer, Office of
Technology Transfer, National Institutes of Health.
[FR Doc. 2014-03957 Filed 2-24-14; 8:45 am]
BILLING CODE 4140-01-P
