Government-Owned Inventions; Availability for Licensing, 43149 [2019-17867]

Download as PDF 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 Sfmt 4703 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] BILLING CODE 4140–01–P 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, Wilson Hall, 1 Center Drive, Bethesda, 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]


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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


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