Government-Owned Inventions; Availability for Licensing, 43149 [2019-17867]
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Federal Register / Vol. 84, No. 161 / Tuesday, August 20, 2019 / Notices
known as FM63 and the anti-CD22
binder known as M971. CD19 and CD22
are each expressed on the surface of B
cells in B cell malignancies and are
hallmark examples of antigen targeting
in CAR–T therapies, with CD19targeting CAR–T therapies being the
first FDA approved CAR–T, and CD22targeting CAR–T showing early promise
in clinical trials for ALL and NHL.
This Notice is made in accordance
with 35 U.S.C. 209 and 37 CFR part 404.
The prospective exclusive license will
be royalty bearing, and the prospective
exclusive license may be granted unless
within thirty (30) days from the date of
this published Notice, the National
Cancer Institute receives written
evidence and argument that establishes
that the grant of the license would not
be consistent with the requirements of
35 U.S.C. 209 and 37 CFR part 404.
In response to this Notice, the public
may file comments or objections.
Comments and objections, other than
those in the form of a license
application, will not be treated
confidentially, and may be made
publicly available.
License applications submitted in
response to this Notice will be
presumed to contain business
confidential information and any release
of information from these license
applications will be made only as
required and upon a request under the
Freedom of Information Act, 5 U.S.C.
552.
Dated: August 6, 2019.
Richard U. Rodriguez,
Associate Director, Technology Transfer
Center, National Cancer Institute.
[FR Doc. 2019–17866 Filed 8–19–19; 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.
jbell on DSK3GLQ082PROD with NOTICES
ACTION:
Notice.
SUMMARY: The invention listed below is
owned by an agency of the U.S.
Government and is available for
licensing 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.
VerDate Sep<11>2014
20:49 Aug 19, 2019
Jkt 247001
FOR FURTHER INFORMATION CONTACT:
Vince Contreras, Ph.D., 240–669–2823;
vince.contreras@nih.gov. Licensing
information and copies of the U.S.
patent application listed below may be
obtained by communicating with the
indicated licensing contact at the
Technology Transfer and Intellectual
Property Office, National Institute of
Allergy and Infectious Diseases, 5601
Fishers Lane, Rockville, MD, 20852; tel.
301–496–2644. A signed Confidential
Disclosure Agreement will be required
to receive copies of unpublished patent
applications.
SUPPLEMENTARY INFORMATION:
Technology description follows.
Recombinant Nipah F Proteins and
Their Use
Description of Technology
Nipah virus is an emerging
pathogenic paramyxovirus responsible
for sporadic and isolated outbreaks of
severe respiratory and neurologic
disease in Southern Asia. As a zoonotic
virus, disease can manifest in both
animals and human with indigenous
fruit bats acting as natural reservoirs of
the virus. The effects of viral infection
vary from acute respiratory distress to
fatal encephalitis. There are currently
no approved therapeutics or vaccines
against the virus, and growing concerns
that this highly pathogenic infection has
the potential to cause larger epidemics
capable of inflicting significant
mortality burden.
Like the RSV fusion (F) glycoprotein,
the Nipah fusion glycoprotein is a target
of neutralizing antibodies that mediate
protection against infection. Previous
studies of prefusion-stabilized F
glycoproteins from pneumoviruses and
other paramyxoviruses (e.g. RSV and
PIVs) have shown they elicit higher
titers of neutralizing antibodies in both
animals and humans than post-fusion F
proteins.
Researchers at the Vaccine Research
Center (VRC) of the National Institute of
Allergy and Infectious Diseases (NIAID)
designed disulfide, cavity-filling and
other mutations that stabilize the Nipah
F glycoprotein in the prefusion
conformation and bind prefusionspecific antibodies. These mutations
also increase protein expression yields
up to 50-fold making the recombinant
proteins easy to manufacture and
amenable to the use of genetic
immunization using nucleic acid or
vector-based applications.
The stabilized prefusion state of the
Nipah F glycoprotein may be an ideal
vaccine immunogen to elicit broad
potent Nipah neutralizing antibodies.
First and second generation prefusion
PO 00000
Frm 00051
Fmt 4703
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43149
molecules have been designed and
tested in small animals and results
(immunogenicity and stability) appear
promising.
This technology is available for
licensing for commercial development
in accordance with 35 U.S.C. 209 and 37
CFR part 404.
Potential Commercial Applications
• Vaccine—to elicit potent
neutralizing antibodies against the
Nipah Env glycoprotein.
Competitive Advantages
Nipah prefusion F design has the
following features compared to wildtype fusion glycoprotein:
• Robust stabilization.
• Up to 50-fold increase in expression
yields, making the recombinant proteins
easy to manufacture.
• Potential to link the recombinant
glycoprotein to nanoparticles or
oligomerization peptides.
Development Stage: In vivo testing
(rodents).
Inventors: Barney S. Graham (NIAID),
Rebecca J. Loomis (NIAID), Guillaume
Stewart-Jones (NIAID), John R. Mascola
(NIAID), and Jason McLellan (NIAID).
Intellectual Property: HHS Reference
Number E–050–2018 includes U.S.
Provisional Patent Application Number
62/714,230 filed 08/03/2018.
Related Intellectual Property: PCT
Application No. PCT/US2008/087719
filed 19/12/2008.
Licensing Contact: Vince Contreras,
Ph.D., 240–669–2823; vince.contreras@
nih.gov.
Dated: August 7, 2019.
Suzanne M. Frisbie,
Deputy Director, Technology Transfer and
Intellectual Property Office, National Institute
of Allergy and Infectious Diseases.
[FR Doc. 2019–17867 Filed 8–19–19; 8:45 am]
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DEPARTMENT OF HEALTH AND
HUMAN SERVICES
National Institutes of Health
Office of the Director, National
Institutes of Health; Amended Notice
of Meeting
Notice is hereby given of a time and
room change in the meeting of the
HEAL (Helping to End Addiction Longterm) Multi-Disciplinary Working
Group, August 21, 2019, 08:30 a.m., to
August 22, 2019, 03:45 p.m., Building 1,
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MD 20892 which was published in the
Federal Register on July 23, 2019,
84FR35402.
E:\FR\FM\20AUN1.SGM
20AUN1
]]>Agencies
[Federal Register Volume 84, Number 161 (Tuesday, August 20, 2019)]
[Notices]
[Page 43149]
From the Federal Register Online via the Government Publishing Office [www.gpo.gov]
[FR Doc No: 2019-17867]
-----------------------------------------------------------------------
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 invention listed below is owned by an agency of the U.S.
Government and is available for licensing 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: Vince Contreras, Ph.D., 240-669-2823;
[email protected]. Licensing information and copies of the U.S.
patent application listed below may be obtained by communicating with
the indicated licensing contact at the Technology Transfer and
Intellectual Property Office, National Institute of Allergy and
Infectious Diseases, 5601 Fishers Lane, Rockville, MD, 20852; tel. 301-
496-2644. A signed Confidential Disclosure Agreement will be required
to receive copies of unpublished patent applications.
SUPPLEMENTARY INFORMATION: Technology description follows.
Recombinant Nipah F Proteins and Their Use
Description of Technology
Nipah virus is an emerging pathogenic paramyxovirus responsible for
sporadic and isolated outbreaks of severe respiratory and neurologic
disease in Southern Asia. As a zoonotic virus, disease can manifest in
both animals and human with indigenous fruit bats acting as natural
reservoirs of the virus. The effects of viral infection vary from acute
respiratory distress to fatal encephalitis. There are currently no
approved therapeutics or vaccines against the virus, and growing
concerns that this highly pathogenic infection has the potential to
cause larger epidemics capable of inflicting significant mortality
burden.
Like the RSV fusion (F) glycoprotein, the Nipah fusion glycoprotein
is a target of neutralizing antibodies that mediate protection against
infection. Previous studies of prefusion-stabilized F glycoproteins
from pneumoviruses and other paramyxoviruses (e.g. RSV and PIVs) have
shown they elicit higher titers of neutralizing antibodies in both
animals and humans than post-fusion F proteins.
Researchers at the Vaccine Research Center (VRC) of the National
Institute of Allergy and Infectious Diseases (NIAID) designed
disulfide, cavity-filling and other mutations that stabilize the Nipah
F glycoprotein in the prefusion conformation and bind prefusion-
specific antibodies. These mutations also increase protein expression
yields up to 50-fold making the recombinant proteins easy to
manufacture and amenable to the use of genetic immunization using
nucleic acid or vector-based applications.
The stabilized prefusion state of the Nipah F glycoprotein may be
an ideal vaccine immunogen to elicit broad potent Nipah neutralizing
antibodies. First and second generation prefusion molecules have been
designed and tested in small animals and results (immunogenicity and
stability) appear promising.
This technology is available for licensing for commercial
development in accordance with 35 U.S.C. 209 and 37 CFR part 404.
Potential Commercial Applications
Vaccine--to elicit potent neutralizing antibodies against
the Nipah Env glycoprotein.
Competitive Advantages
Nipah prefusion F design has the following features compared to
wild-type fusion glycoprotein:
Robust stabilization.
Up to 50-fold increase in expression yields, making the
recombinant proteins easy to manufacture.
Potential to link the recombinant glycoprotein to
nanoparticles or oligomerization peptides.
Development Stage: In vivo testing (rodents).
Inventors: Barney S. Graham (NIAID), Rebecca J. Loomis (NIAID),
Guillaume Stewart-Jones (NIAID), John R. Mascola (NIAID), and Jason
McLellan (NIAID).
Intellectual Property: HHS Reference Number E-050-2018 includes
U.S. Provisional Patent Application Number 62/714,230 filed 08/03/2018.
Related Intellectual Property: PCT Application No. PCT/US2008/
087719 filed 19/12/2008.
Licensing Contact: Vince Contreras, Ph.D., 240-669-2823;
[email protected].
Dated: August 7, 2019.
Suzanne M. Frisbie,
Deputy Director, Technology Transfer and Intellectual Property Office,
National Institute of Allergy and Infectious Diseases.
[FR Doc. 2019-17867 Filed 8-19-19; 8:45 am]
BILLING CODE 4140-01-P
