Government-Owned Inventions; Availability for Licensing, 55855-55858 [E8-22610]
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anthrax vaccine. Proc Natl Acad Sci
USA. 2003 Jul 22;100(15):8945–8950.
Patent Status: U.S. Patent Application
No. 10/559,825 filed 02 Dec 2005,
claiming priority to 05 Jun 2003 (HHS
Reference No. E–343–2002/0–US–04).
Licensing Status: Available for
licensing.
Licensing Contact: Peter A. Soukas,
J.D.; 301/435–4646;
soukasp@mail.nih.gov.
and/or e-mail
apomerantsev@niaid.nih.gov for more
information.
Monoclonal Antibodies That Neutralize
B. anthracis Protective Antigen (PA),
Lethal Factor (LF) and Edema Factor
(EF)
Description of Invention: Anthrax,
whether resulting from natural or
bioterrorist-associated exposure, is a
Improved Bacterial Host for Production constant threat to human health. The
lethality of anthrax is primarily the
of Anthrax Toxin Proteins and
result of the effects of anthrax toxin,
Vaccines: Bacillus anthracis BH450
which has 3 components: a receptorDescription of Invention: Anthrax
binding protein known as ‘‘protective
toxin has previously been made from
antigen’’ (PA) and 2 catalytic proteins
various avirulent strains of Bacillus
known as ‘‘lethal factor’’ (LF) and
anthracis. The inventors have
‘‘edema factor’’ (EF). Although
genetically engineered a new strain of B. production of an efficient anthrax
anthracis with improved properties.
vaccine is an ultimate goal, the benefits
The strain, designated BH450, is totally
of vaccination can be expected only if
deficient in the ability to make spores
a large proportion of the population at
and to produce a major extracellular
risk is immunized. The low incidence of
protease designated Peptidase M4. The
anthrax suggests that large-scale
genetic lesions introduced are defined,
vaccination may not be the most
true deletions, so there is no possibility
efficient means of controlling this
of reversion. Inability to make spores
disease. In contrast, passive
assures that laboratories growing the
administration of neutralizing human or
strain will not become contaminated
chimpanzee monoclonal antibody to a
with the very stable anthrax spores.
subject at risk for anthrax or exposed to
Inability to make peptidase M4
anthrax could provide immediate
increases the stability of proteins such
efficacy for emergency prophylaxis
as anthrax toxin that are secreted to the
against or treatment of anthrax.
culture medium.
Four monoclonal antibodies (mAbs)
Applications and Modality: B.
against PA, three mAbs against LF and
anthracis vaccine/prophylactic and
four mAbs specific for EF of anthrax
therapeutic studies.
were isolated from a phage display
Market: Research tool useful for
library generated from immunized
biodefense/therapeutic studies.
chimpanzees. Two mAbs recognizing
Development Status: The technology
PA (W1 and W2), two anti-LF mAbs
is a research tool.
efficiently neutralized the cytotoxicity
Inventors: Andrei Pomerantsev, Dana
of lethal toxin in a macrophage lysis
Hsu, Ramakrishnan Sitaraman, Craig
assay. One anti-EF mAb efficiently
Galloway, Violetta Kivovich, Stephen
neutralized edema toxin in cell culture.
Leppla (NIAID).
All five neutralizing mAbs protected
Publication: AP Pomerantsev et al.
animals from anthrax toxin challenge.
Genome engineering in Bacillus
Application: Prophylactics or
anthracis using Cre recombinase. Infect
therapeutics against B. anthracis.
Immun. 2006 Jan;74(1):682–693.
Developmental Status: Preclinical
Patent Status: HHS Reference No. E–
studies have been performed.
127–2007/0—Research Tool.
Inventors: Zhaochun Chen, Robert
Licensing Status: This technology is
Purcell, Suzanne Emerson, Stephen
not patented. The strain will be
Leppla, Mahtab Moyeri (NIAID).
transferred through a Biological
Publication: Z Chen et al. Efficient
Materials License.
neutralization of anthrax toxin by
Licensing Contact: Peter A. Soukas,
chimpanzee monoclonal antibodies
J.D.; 301/435–4646;
against protective antigen. J Infect Dis.
soukasp@mail.nih.gov.
2006 Mar 1;193(5):625–633.
Collaborative Research Opportunity:
Patent Status: PCT Application No.
The National Institute of Allergy and
PCT/US2008/054609 filed 21 Feb 2008,
Infectious Diseases, Laboratory of
Bacterial Diseases, is seeking statements claiming priority to 23 Feb 2007 (HHS
Reference No. E–123–2007/0–PCT–02);
of capability or interest from parties
U.S. Patent Application No. 11/793,735
interested in collaborative research to
filed 22 Jun 2007 (HHS Reference No.
further develop, evaluate, or
commercialize Bacillus anthracis BH450 E–146–2004/0–US–03)
Licensing Status: Available for
strain. Please contact Dr. Andrei P.
exclusive or non-exclusive licensing.
Pomerantsev at phone 301/451–9817
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Licensing Contact: Peter A. Soukas,
J.D.; 301/435–4646;
soukasp@mail.nih.gov.
Collaborative Research Opportunity:
The National Institute of Allergy and
Infectious Diseases, Laboratory of
Infectious Diseases is seeking statements
of capability or interest from parties
interested in collaborative research to
further develop, evaluate, or
commercialize Chimpanzee/human
neutralizing monoclonal antibodies
against anthrax toxins. Please contact
Dr. Robert Purcell at 301/496–5090 for
more information.
Dated: September 18, 2008.
Richard U. Rodriguez,
Director, Division of Technology Development
and Transfer, Office of Technology Transfer,
National Institutes of Health.
[FR Doc. E8–22608 Filed 9–25–08; 8:45 am]
BILLING CODE 4140–01–P
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:
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.
Inhibitors of the Plasmodial Surface
Anion Channel as Antimalarials
Description of Technology: The
inventions described herein are
antimalarial small molecule inhibitors
of the plasmodial surface anion channel
(PSAC), an essential nutrient acquisition
ion channel expressed on human
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erythrocytes infected with malaria
parasites. These inhibitors were
discovered by high-throughput
screening of chemical libraries and
analysis of their ability to kill malaria
parasites in culture. Two separate
classes of inhibitors were found to work
synergistically in combination against
PSAC and killed malaria cultures at
markedly lower concentrations than
separately. These inhibitors have high
affinity and specificity for PSAC and
have acceptable cytotoxicity profiles.
Preliminary in vivo testing of these
compounds in a mouse malaria model is
currently ongoing.
Applications: Treatment of malarial
infections.
Advantages: Novel drug treatment for
malarial infections; Synergistic effect of
these compounds on PSAC.
Development Status: In vitro and in
vivo data can be provided upon request.
Market: Treatment of malarial
infection.
Inventor: Sanjay A. Desai (NIAID).
Publications:
1. Kang M, Lisk G, Hollingworth S,
Baylor SM, Desai SA. Malaria parasites
are rapidly killed by dantrolene
derivatives specific for the plasmodial
surface anion channel. Mol. Pharmacol.
2005 Jul;68(1):34–40.
2. Desai SA, Bezrukov SM,
Zimmerberg J. A voltage-dependent
channel involved in nutrient uptake by
red blood cells infected with the malaria
parasite. Nature. 2000 Aug
31;406(6799):1001–1005.
Patent Status: U.S. Provisional
Application No. 61/083,000 filed 23 Jul
2008 (HHS Reference No. E–202–2008/
0–US–01).
Licensing Status: Available for
exclusive or non-exclusive licensing.
Licensing Contact: Kevin W. Chang,
PhD; 301–435–5018;
changke@mail.nih.gov.
Collaborative Research Opportunity:
The NIAID Office of Technology
Development is seeking statements of
capability or interest from parties
interested in collaborative research to
further develop, evaluate, or
commercialize antimalarial drugs that
target PSAC or other parasite-specific
transporters. Please contact either
Charles Rainwater or Dana Hsu at 301–
496–2644 for more information.
Aerosolized Vaccines
Description of Technology: Vaccine
delivery to humans by mucosal routes
may offer some operational and
immunological advantages over
intramuscular administration by needleand-syringe. Potential targets include
the oral, nasal, rectal conjunctival, and
vaginal surfaces with the oral and nasal
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routes being the most practical to
consider for infants, children and adults
of both sexes. Needle-free delivery
methods may improve compliance,
reduce discomfort, and improve safety
of vaccines; particularly in the
developing world, needle-free delivery
could mitigate the risk of blood-borne
pathogen transmission by unsafe
injection practices or inadequately
sterilized equipment, and be easier and
safer to deploy by non-medical
personnel.
Mucosal vaccination may offer a
potential immunological advantage of
recruiting mucosal lymphoid tissues
that are important in mediation of
immune responses, particularly at the
entry site for infectious pathogens.
Optimally formulated and delivered
antigens may elicit a variety of
responses in these tissues including
secretory IgA, serum IgG capable of
neutralizing toxins or viruses, and cellmediated immunity as measured by
cytotoxic T-cell responses and cytokine
production.
In the case of respiratory delivery,
specific particle sizes can target
particular microenvironments within
the lung. Efficient penetration of the
lung parenchyma depends upon
optimizing the size of the droplet in
relation to the diameter of the
respiratory airways. It has been
recommended that school age children
and adults be immunized with
respiratory particles that are between 3
and 5 µm in diameter, since a larger
particle cannot effectively penetrate
deep into the lung.
This application claims aerosolized
immunogenic compositions comprising
aerosolized immunogenic particles
between 0.01 µm and 15 µm. The
application also claims methods for
delivering immunogenic compositions,
methods for generating immune
responses, and methods for treating
infections by producing and
administering aerosolized immunogenic
compositions. More specifically, the
invention claims replication-defective
recombinant adenoviruses encoding
human immunodeficiency virus (HIV),
simian immunodeficiency virus (SIV)
and tuberculosis (TB) genes delivered
by aerosolization into the lung. The
inventors have shown that this regimen
induces very high, stable cellular
immune responses localized to the lung,
as well as humoral responses in the
lung, systemically, and, importantly, at
distal mucosal sites. This regimen may
prove highly useful for vaccination
against respiratory infections such as
TB, influenza, and respiratory syncytial
virus, and provide a platform for
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generating mucosal antibody responses
against other pathogens.
Applications: Improved immunogenic
compositions and vaccine formulations,
delivery of viral vectors, plasmid DNA,
proteins, and adjuvants.
Development Status: Vaccines have
been formulated and preclinical studies
have been performed.
Inventors: Mario Roederer and
Srinivas Rao (NIAID).
Patent Status: U.S. Provisional
Application No. 61/038,534 filed 21 Mar
2008 (HHS Reference No. E–053–2008/
0–US–01).
Licensing Status: Available for
exclusive or non-exclusive licensing.
Licensing Contact: Peter A. Soukas,
J.D.; 301–435–4646;
soukasp@mail.nih.gov.
Use of Saccharides Cross-Reactive With
Bacillus anthracis Spore
Glycoprotein as a Vaccine Against
Anthrax
Description of Technology: Bacillus
anthracis is a spore-forming bacterium
that causes anthrax in humans and in
other mammals. The glycoprotein BclA
(Bacillus collagen-like protein of
anthracis) is a major constituent of the
exosporium, the outermost surface of B.
anthracis spores. The glycosyl part of
BclA is an oligosaccharide composed of
2-O-methyl-4-(3-hydroxy-3methylbutanamido)-4,6-dideoxy-dglucose, referred to as anthrose, and
three rhamnose residues. A structure
similar to anthrose, 4-(3-hydroxy-3methylbutanamido)-4,6-dideoxy-dglucose is found in the side chain of the
capsular polysaccharide (CPS) of
Shewanella spp. MR–4. Under certain
growth conditions the bacteria produce
a variant CPS lacking one methyl group
on the hydroxybutyrate, 4-(3hydroxybutanamido)-4,6-dideoxy-dglucose. Contrary to anthrose, neither of
the Shewanella CPSs is 2-O methylated.
The inventors have found that both
Shewanella CPS variants react with
anti-B. anthracis spore sera. The
inventors have also found that these
antisera reacted with flagellae of
Pseudomonas syringae, reported to be
glycosylated with a similar terminal
saccharide, 4-(3-hydroxybutanamido)4,6-dideoxy-2-O-methyl-d-glucose. Sera
produced by immunization with
Shewanella or P. syringae cells bound to
B. anthracis spores but not to Bacillus
cereus spores in a fluorescent
microscopy assay. The inventors’
experiments show that methylation of
the anthrose at the O–2 of the sugar ring
and at the C–3 of 3-hydroxybutyrate are
not essential for induction of crossreactive antibodies.
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The application claims the use of
Shewanella CPS conjugates as a
component of an anthrax vaccine. The
application also claims the use of
capsular polysaccharides from
Shewanella and compounds from the
flagella of Pseudomonas syringae for the
development of anthrax vaccines.
Application: Development of anthrax
vaccines, diagnostics and therapeutics.
Development Status: Conjugates have
been synthesized and preclinical studies
have been performed.
Inventors: Joanna Kubler-Kielb
(NICHD), Rachel Schneerson (NICHD),
Haijing Hu (NIAID), Stephen H. Leppla
(NIAID), John B. Robbins (NICHD), et al.
Publication: Kubler-Kielb J. et al.
Saccharides cross-reactive with Bacillus
anthracis spore glycoprotein as an
anthrax vaccine component. Proc Natl
Acad Sci USA. 2008 Jun
24;105(25):8709–8712. This publication
reports the preparation,
characterization, and antibody
responses to protein conjugates of the
two variants of Shewanella CPS.
Significantly, both conjugates induced
antibodies that bound to both
Shewanella CPS variants by ELISA and
to B. anthracis spores, as detected by
fluorescent microscopy.
Patent Status: U.S. Provisional
Application No. 61/066,509 filed 19 Feb
2008 (HHS Reference No. E–032–2008/
0-US–01).
Licensing Status: Available for
exclusive or non-exclusive licensing.
Licensing Contact: Peter A. Soukas,
J.D.; 301–435–4646;
soukasp@mail.nih.gov.
Modified Sugar Substrates and Methods
of Use
Description of Technology: Glycans
can be classified as linear or branched
sugars. The linear sugars are the
glycosaminoglycans comprising
polymers of sulfated disaccharide repeat
units that are O-linked to a core protein,
forming a proteoglycan aggregate. The
branched glycans are found as N-linked
and O-linked sugars on glycoproteins or
on glycolipids. These carbohydrate
moieties of the linear and branched
glycans are synthesized by a super
family of enzymes, the
glycosyltransferases (GTs), which
transfer a sugar moiety from a sugar
donor to an acceptor molecule.
Although GTs catalyze chemically
similar reactions in which a
monosaccharide is transferred from an
activated derivative, such as a UDPsugar, to an acceptor, very few GTs bear
similarity in primary structure.
Eukaryotic cells express several
classes of oligosaccharides attached to
proteins or lipids. Animal glycans can
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be N-linked via beta-GlcNAc to
Asparagine (N-glycans), O-linked via
UDP-GalNAc to Serine/Threonine (Oglycans), or can connect the carboxyl
end of a protein to a
phosphatidylinositol unit (GPI-anchors)
via a common core glycan structure.
Thus, there is potential to develop
carbohydrate substrates comprising
bioactive agents that can be used to
produce glycoconjugates carrying sugar
moieties with bioactive agents. Such
glycoconjugates have many therapeutic
and diagnostic uses, e.g. in labeling or
targeted delivery. Further, such
glycoconjugates can be used in the
assembly of bio-nanoparticles to
develop targeted-drug delivery systems
or contrast agents for medical uses.
This application claims methods and
compositions for making and using
functionalized sugars. Also claimed in
the application are methods for forming
a wide variety of products at a cell or
in an in vitro environment. More
specifically, the claimed compositions
of the invention comprise a sugar
nucleotide and one or more functional
groups.
Applications: Production of
therapeutic or diagnostic
glycoconjugates, assembly of bionanoparticles, development of contrast
agents.
Development Status: Enzymes have
been synthesized and initial studies
have been performed.
Inventors: Pradman K. Qasba and
Maria R. Manzoni (NCI).
Publications:
1. B Ramakrishnan et al. Applications
of glycosyltransferases in the sitespecific conjugation of biomolecules
and the development of a targeted drug
delivery system and contrast agents for
MRI. Expert Opin Drug Deliv. 2008
Feb;5(2):149–153. Review.
2. PK Qasba et al. Site-specific linking
of biomolecules via glycan residues
using glycosyltransferases. Biotechnol
Prog. 2008 May-Jun;24(3):520–526.
Patent Status: U.S. Patent Application
No. 61/027,782 filed 11 Feb 2008 (HHS
Reference No. E–016–2008/0–US–01).
Licensing Status: Available for
exclusive or non-exclusive licensing.
Licensing Contact: Peter A. Soukas,
J.D.; 301–435–4646;
soukasp@mail.nih.gov.
Collaborative Research Opportunity:
The National Cancer Institute’s
Nanobiology Program is seeking
statements of capability or interest from
parties interested in collaborative
research to further develop, evaluate, or
commercialize the synthesis of UDP
derivatives of C2 modified galactose for
use as donor substrates for
glycosyltransferases. Please contact John
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D. Hewes, Ph.D. at 301–435–3121 or
hewesj@mail.nih.gov for more
information.
Immunogenic Peptides Against
Influenza Virus
Description of Technology: The
invention described herein are peptides
and polypeptides derived from the HA,
NA, PB2, PB1, PA, M1, M2, NP, NS1,
and NS2 proteins of influenza virus that
elicit immunogenic responses;
particularly neutralizing antibodies,
against human and avian influenza
strains H1N1, H3N2, H5N1 and H7N7.
Materials in the form of immunogenic
compositions including these peptides
and polypeptides can also be inlicensed along with the patent rights.
Pharmaceutical compositions including
these peptides and polypeptides with or
without adjuvants are within the scope
of the invention. The inventors are
currently investigating the vaccine
potential of specific peptides and
polypeptides.
Applications:
• Vaccines against influenza virus
infection;
• Diagnostics for the detection of
influenza virus infection; and
• Generation of influenza virus
specific antibodies.
Advantages:
• Peptides can be expressed in a
number of different expression systems;
and
• Peptides were identified based on
the specificity of antibodies derived
from human and avian influenza virus
infected individuals.
Development Status: In vitro data can
be provided upon request.
Market:
• Preventative or treatment for
influenza virus infection; and
• Diagnostic for influenza virus
infection.
Inventors: Hana Golding and Surender
Khurana (FDA).
Publications:
1. Pandemic Influenza preparedness:
New molecular tools for evaluation of
influenza vaccines and identification of
serological epitopes for avian influenza
diagnostic assays at ‘‘Options for the
Control of Influenza VI’’ June 17–23,
2007, Toronto, Canada. (oral
presentation)
2. Pandemic Influenza preparedness:
Identification of serological epitopes for
use in development of broadly crossreactive influenza vaccines at ‘‘National
Foundation for Infectious Diseases—
11th Annual Conference on Vaccine
Research’’, Baltimore: May 5–7, 2008.
(oral presentation).
3. Analysis of antibody repertoires in
H5N1 infected and vaccinated
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individuals using influenza whole
genome phage display at
‘‘Immunobiology and Pathogenesis of
Influenza Infection’’, Atlanta: June 1–3,
2008. (poster presentation).
Patent Status: International Patent
Application PCT/US2008/067001 filed
13 Jun 2008 (HHS Reference No. E–236–
2007/3–PCT–01).
Licensing Status: Available for
exclusive or non-exclusive licensing.
Licensing Contact: Kevin W. Chang,
Ph.D.; 301–435–5018;
changke@mail.nih.gov.
Collaborative Research Opportunity:
The FDA, Center for Biologics
Evaluation and Research (CBER),
Division of Viral Products, is seeking
statements of capability or interest from
parties interested in collaborative
research to further develop, evaluate, or
commercialize these peptides as vaccine
candidates or diagnostics. Please contact
Alice Welch at alice.welch@fda.hhs.gov
or 301–827–0359 for more information.
A Rapid Ultrasensitive Assay for
Detecting Prions Based on the Seeded
Polymerization of Recombinant Normal
Prion Protein (rPrP-sen)
Description of Technology: Prion
diseases are neurodegenerative diseases
of great public concern because humans
may be infected from hoofed animals
used as food, food products such as
milk, or blood products. Currently
available tests for disease-causing prions
are either incapable of detecting low
concentrations of prions and must be
used post-mortem or are incapable of
detecting low concentrations of prions
economically or accurately. This
technology enables rapid and
economical detection of sub-lethal
concentrations of prions by using
recombinant, normal, prion protein
(rPrP-sen) as a marker or indicator of
infectious prions in a sample.
Specifically, prions (contained in a
sample) seed the polymerization of
rPrP-sen, and polymerized rPrP-sen is
detected as an amplified indicator of
prions in the sample. This assay differs
from the protein-misfolding cyclic
amplification assay (PMCA) because it
enables the effective use of rPrP-sen and
does not require multiple amplification
cycles unless a higher degree of
sensitivity is required. It is anticipated
that this technology can be combined
with additional prion-detection
technologies to further improve the
sensitivity of the assay. In its current
embodiment, this assay has been used to
detect prions in brain tissue or cerebral
spinal fluid (CSF) from humans (variant
CJD), sheep (scrapie), and hamsters
(scrapie).
Advantages:
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• Uses a consistent, concentrated
source of normal prion protein (rPrPsen)
• Prions are detectable to low levels
after a single amplification round
• May be combined with
complimentary detection technologies
to improve sensitivity
• Demonstrated to be effective at
detecting prions from different species
• May be applicable to blood
products
• Economical
Applications:
• A test for live animals or food
products
• A human diagnostic for early
detection of prion diseases
• Monitor for effectiveness of
treatments or disease progression
Inventors: Byron W. Caughey,
Ryuichiro Atarashi, Roger A. Moore,
and Suzette A. Priola (NIAID).
Related Publications:
1. R Atarashi et al. Simplified
ultrasensitive prion detection by
recombinant PrP conversion with
shaking. Nat Methods 2008
Mar;5(3):211–212.
2. R Atarashi et al. Ultrasensitive
detection of scrapie prion protein using
seeded conversion of recombinant prion
protein. Nat Methods 2007
Aug;4(8):645–650.
Patent Status:
• PCT Application No. PCT/US2008/
070656 filed 21 Jul 2008 (HHS
Reference No. E–109–2007/1–PCT–01).
• U.S. Application No. 12/177,012
filed 21 Jul 2008 (HHS Reference No. E–
109–2007/1–US–02).
Licensing Status: Available for
exclusive and non-exclusive licensing.
Licensing Contact: RC Tang, JD, LLM;
301–435–5031; tangrc@mail.nih.gov.
Collaborative Research Opportunity:
The NIAID Laboratory of Persistent
Viral Diseases, TSE/Prion Biochemistry
Section, is seeking statements of
capability or interest from parties
interested in collaborative research to
further develop, evaluate, or
commercialize this technology. Please
contact Rosemary Walsh at 301–451–
3528 or rcwalsh@niaid.nih.gov.
Dated: September 18, 2008.
Richard U. Rodriguez,
Director, Division of Technology Development
and Transfer, Office of Technology Transfer,
National Institutes of Health.
[FR Doc. E8–22610 Filed 9–25–08; 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;
Amended Notice of Meeting
Notice is hereby given of a change in
the meeting of the National Institute of
Diabetes and Digestive and Kidney
Diseases Special Emphasis Panel,
October 17, 2008, 2:30 p.m. to 3:30 p.m.,
National Institutes of Health, Two
Democracy Plaza, 6707 Democracy
Boulevard, Bethesda, MD 20892 which
was published in the Federal Register
on September 11, 2008, 73 FR 0177.
This meeting will be held October 22,
2008 instead of October 17, 2008. The
meeting is closed to the public.
Dated: September 18, 2008.
Jennifer Spaeth,
Director, Office of Federal Advisory
Committee Policy.
[FR Doc. E8–22604 Filed 9–25–08; 8:45 am]
BILLING CODE 4140–01–P
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. Appendix 2), 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, Molecular Therapy
Core Centers.
Date: October 21, 2008.
Time: 8 a.m. to 5 p.m.
Agenda: To review and evaluate grant
applications.
Place: Bethesda Marriott Suites, 6711
Democracy Boulevard, Bethesda, MD 20817.
Contact Person: Michele L. Barnard, PhD,
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DEA, NIDDK, National Institutes of Health,
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[Federal Register Volume 73, Number 188 (Friday, September 26, 2008)]
[Notices]
[Pages 55855-55858]
From the Federal Register Online via the Government Printing Office [www.gpo.gov]
[FR Doc No: E8-22610]
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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, Public Health Service, HHS.
ACTION: Notice.
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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.
Inhibitors of the Plasmodial Surface Anion Channel as Antimalarials
Description of Technology: The inventions described herein are
antimalarial small molecule inhibitors of the plasmodial surface anion
channel (PSAC), an essential nutrient acquisition ion channel expressed
on human
[[Page 55856]]
erythrocytes infected with malaria parasites. These inhibitors were
discovered by high-throughput screening of chemical libraries and
analysis of their ability to kill malaria parasites in culture. Two
separate classes of inhibitors were found to work synergistically in
combination against PSAC and killed malaria cultures at markedly lower
concentrations than separately. These inhibitors have high affinity and
specificity for PSAC and have acceptable cytotoxicity profiles.
Preliminary in vivo testing of these compounds in a mouse malaria model
is currently ongoing.
Applications: Treatment of malarial infections.
Advantages: Novel drug treatment for malarial infections;
Synergistic effect of these compounds on PSAC.
Development Status: In vitro and in vivo data can be provided upon
request.
Market: Treatment of malarial infection.
Inventor: Sanjay A. Desai (NIAID).
Publications:
1. Kang M, Lisk G, Hollingworth S, Baylor SM, Desai SA. Malaria
parasites are rapidly killed by dantrolene derivatives specific for the
plasmodial surface anion channel. Mol. Pharmacol. 2005 Jul;68(1):34-40.
2. Desai SA, Bezrukov SM, Zimmerberg J. A voltage-dependent channel
involved in nutrient uptake by red blood cells infected with the
malaria parasite. Nature. 2000 Aug 31;406(6799):1001-1005.
Patent Status: U.S. Provisional Application No. 61/083,000 filed 23
Jul 2008 (HHS Reference No. E-202-2008/0-US-01).
Licensing Status: Available for exclusive or non-exclusive
licensing.
Licensing Contact: Kevin W. Chang, PhD; 301-435-5018;
changke@mail.nih.gov.
Collaborative Research Opportunity: The NIAID Office of Technology
Development is seeking statements of capability or interest from
parties interested in collaborative research to further develop,
evaluate, or commercialize antimalarial drugs that target PSAC or other
parasite-specific transporters. Please contact either Charles Rainwater
or Dana Hsu at 301-496-2644 for more information.
Aerosolized Vaccines
Description of Technology: Vaccine delivery to humans by mucosal
routes may offer some operational and immunological advantages over
intramuscular administration by needle-and-syringe. Potential targets
include the oral, nasal, rectal conjunctival, and vaginal surfaces with
the oral and nasal routes being the most practical to consider for
infants, children and adults of both sexes. Needle-free delivery
methods may improve compliance, reduce discomfort, and improve safety
of vaccines; particularly in the developing world, needle-free delivery
could mitigate the risk of blood-borne pathogen transmission by unsafe
injection practices or inadequately sterilized equipment, and be easier
and safer to deploy by non-medical personnel.
Mucosal vaccination may offer a potential immunological advantage
of recruiting mucosal lymphoid tissues that are important in mediation
of immune responses, particularly at the entry site for infectious
pathogens. Optimally formulated and delivered antigens may elicit a
variety of responses in these tissues including secretory IgA, serum
IgG capable of neutralizing toxins or viruses, and cell-mediated
immunity as measured by cytotoxic T-cell responses and cytokine
production.
In the case of respiratory delivery, specific particle sizes can
target particular microenvironments within the lung. Efficient
penetration of the lung parenchyma depends upon optimizing the size of
the droplet in relation to the diameter of the respiratory airways. It
has been recommended that school age children and adults be immunized
with respiratory particles that are between 3 and 5 [mu]m in diameter,
since a larger particle cannot effectively penetrate deep into the
lung.
This application claims aerosolized immunogenic compositions
comprising aerosolized immunogenic particles between 0.01 [mu]m and 15
[mu]m. The application also claims methods for delivering immunogenic
compositions, methods for generating immune responses, and methods for
treating infections by producing and administering aerosolized
immunogenic compositions. More specifically, the invention claims
replication-defective recombinant adenoviruses encoding human
immunodeficiency virus (HIV), simian immunodeficiency virus (SIV) and
tuberculosis (TB) genes delivered by aerosolization into the lung. The
inventors have shown that this regimen induces very high, stable
cellular immune responses localized to the lung, as well as humoral
responses in the lung, systemically, and, importantly, at distal
mucosal sites. This regimen may prove highly useful for vaccination
against respiratory infections such as TB, influenza, and respiratory
syncytial virus, and provide a platform for generating mucosal antibody
responses against other pathogens.
Applications: Improved immunogenic compositions and vaccine
formulations, delivery of viral vectors, plasmid DNA, proteins, and
adjuvants.
Development Status: Vaccines have been formulated and preclinical
studies have been performed.
Inventors: Mario Roederer and Srinivas Rao (NIAID).
Patent Status: U.S. Provisional Application No. 61/038,534 filed 21
Mar 2008 (HHS Reference No. E-053-2008/0-US-01).
Licensing Status: Available for exclusive or non-exclusive
licensing.
Licensing Contact: Peter A. Soukas, J.D.; 301-435-4646;
soukasp@mail.nih.gov.
Use of Saccharides Cross-Reactive With Bacillus anthracis Spore
Glycoprotein as a Vaccine Against Anthrax
Description of Technology: Bacillus anthracis is a spore-forming
bacterium that causes anthrax in humans and in other mammals. The
glycoprotein BclA (Bacillus collagen-like protein of anthracis) is a
major constituent of the exosporium, the outermost surface of B.
anthracis spores. The glycosyl part of BclA is an oligosaccharide
composed of 2-O-methyl-4-(3-hydroxy-3-methylbutanamido)-4,6-dideoxy-d-
glucose, referred to as anthrose, and three rhamnose residues. A
structure similar to anthrose, 4-(3-hydroxy-3-methylbutanamido)-4,6-
dideoxy-d-glucose is found in the side chain of the capsular
polysaccharide (CPS) of Shewanella spp. MR-4. Under certain growth
conditions the bacteria produce a variant CPS lacking one methyl group
on the hydroxybutyrate, 4-(3-hydroxybutanamido)-4,6-dideoxy-d-glucose.
Contrary to anthrose, neither of the Shewanella CPSs is 2-O methylated.
The inventors have found that both Shewanella CPS variants react
with anti-B. anthracis spore sera. The inventors have also found that
these antisera reacted with flagellae of Pseudomonas syringae, reported
to be glycosylated with a similar terminal saccharide, 4-(3-
hydroxybutanamido)-4,6-dideoxy-2-O-methyl-d-glucose. Sera produced by
immunization with Shewanella or P. syringae cells bound to B. anthracis
spores but not to Bacillus cereus spores in a fluorescent microscopy
assay. The inventors' experiments show that methylation of the anthrose
at the O-2 of the sugar ring and at the C-3 of 3-hydroxybutyrate are
not essential for induction of cross-reactive antibodies.
[[Page 55857]]
The application claims the use of Shewanella CPS conjugates as a
component of an anthrax vaccine. The application also claims the use of
capsular polysaccharides from Shewanella and compounds from the
flagella of Pseudomonas syringae for the development of anthrax
vaccines.
Application: Development of anthrax vaccines, diagnostics and
therapeutics.
Development Status: Conjugates have been synthesized and
preclinical studies have been performed.
Inventors: Joanna Kubler-Kielb (NICHD), Rachel Schneerson (NICHD),
Haijing Hu (NIAID), Stephen H. Leppla (NIAID), John B. Robbins (NICHD),
et al.
Publication: Kubler-Kielb J. et al. Saccharides cross-reactive with
Bacillus anthracis spore glycoprotein as an anthrax vaccine component.
Proc Natl Acad Sci USA. 2008 Jun 24;105(25):8709-8712. This publication
reports the preparation, characterization, and antibody responses to
protein conjugates of the two variants of Shewanella CPS.
Significantly, both conjugates induced antibodies that bound to both
Shewanella CPS variants by ELISA and to B. anthracis spores, as
detected by fluorescent microscopy.
Patent Status: U.S. Provisional Application No. 61/066,509 filed 19
Feb 2008 (HHS Reference No. E-032-2008/0-US-01).
Licensing Status: Available for exclusive or non-exclusive
licensing.
Licensing Contact: Peter A. Soukas, J.D.; 301-435-4646;
soukasp@mail.nih.gov.
Modified Sugar Substrates and Methods of Use
Description of Technology: Glycans can be classified as linear or
branched sugars. The linear sugars are the glycosaminoglycans
comprising polymers of sulfated disaccharide repeat units that are O-
linked to a core protein, forming a proteoglycan aggregate. The
branched glycans are found as N-linked and O-linked sugars on
glycoproteins or on glycolipids. These carbohydrate moieties of the
linear and branched glycans are synthesized by a super family of
enzymes, the glycosyltransferases (GTs), which transfer a sugar moiety
from a sugar donor to an acceptor molecule. Although GTs catalyze
chemically similar reactions in which a monosaccharide is transferred
from an activated derivative, such as a UDP-sugar, to an acceptor, very
few GTs bear similarity in primary structure.
Eukaryotic cells express several classes of oligosaccharides
attached to proteins or lipids. Animal glycans can be N-linked via
beta-GlcNAc to Asparagine (N-glycans), O-linked via UDP-GalNAc to
Serine/Threonine (O-glycans), or can connect the carboxyl end of a
protein to a phosphatidylinositol unit (GPI-anchors) via a common core
glycan structure. Thus, there is potential to develop carbohydrate
substrates comprising bioactive agents that can be used to produce
glycoconjugates carrying sugar moieties with bioactive agents. Such
glycoconjugates have many therapeutic and diagnostic uses, e.g. in
labeling or targeted delivery. Further, such glycoconjugates can be
used in the assembly of bio-nanoparticles to develop targeted-drug
delivery systems or contrast agents for medical uses.
This application claims methods and compositions for making and
using functionalized sugars. Also claimed in the application are
methods for forming a wide variety of products at a cell or in an in
vitro environment. More specifically, the claimed compositions of the
invention comprise a sugar nucleotide and one or more functional
groups.
Applications: Production of therapeutic or diagnostic
glycoconjugates, assembly of bio-nanoparticles, development of contrast
agents.
Development Status: Enzymes have been synthesized and initial
studies have been performed.
Inventors: Pradman K. Qasba and Maria R. Manzoni (NCI).
Publications:
1. B Ramakrishnan et al. Applications of glycosyltransferases in
the site-specific conjugation of biomolecules and the development of a
targeted drug delivery system and contrast agents for MRI. Expert Opin
Drug Deliv. 2008 Feb;5(2):149-153. Review.
2. PK Qasba et al. Site-specific linking of biomolecules via glycan
residues using glycosyltransferases. Biotechnol Prog. 2008 May-
Jun;24(3):520-526.
Patent Status: U.S. Patent Application No. 61/027,782 filed 11 Feb
2008 (HHS Reference No. E-016-2008/0-US-01).
Licensing Status: Available for exclusive or non-exclusive
licensing.
Licensing Contact: Peter A. Soukas, J.D.; 301-435-4646;
soukasp@mail.nih.gov.
Collaborative Research Opportunity: The National Cancer Institute's
Nanobiology Program is seeking statements of capability or interest
from parties interested in collaborative research to further develop,
evaluate, or commercialize the synthesis of UDP derivatives of C2
modified galactose for use as donor substrates for
glycosyltransferases. Please contact John D. Hewes, Ph.D. at 301-435-
3121 or hewesj@mail.nih.gov for more information.
Immunogenic Peptides Against Influenza Virus
Description of Technology: The invention described herein are
peptides and polypeptides derived from the HA, NA, PB2, PB1, PA, M1,
M2, NP, NS1, and NS2 proteins of influenza virus that elicit
immunogenic responses; particularly neutralizing antibodies, against
human and avian influenza strains H1N1, H3N2, H5N1 and H7N7. Materials
in the form of immunogenic compositions including these peptides and
polypeptides can also be in-licensed along with the patent rights.
Pharmaceutical compositions including these peptides and polypeptides
with or without adjuvants are within the scope of the invention. The
inventors are currently investigating the vaccine potential of specific
peptides and polypeptides.
Applications:
Vaccines against influenza virus infection;
Diagnostics for the detection of influenza virus
infection; and
Generation of influenza virus specific antibodies.
Advantages:
Peptides can be expressed in a number of different
expression systems; and
Peptides were identified based on the specificity of
antibodies derived from human and avian influenza virus infected
individuals.
Development Status: In vitro data can be provided upon request.
Market:
Preventative or treatment for influenza virus infection;
and
Diagnostic for influenza virus infection.
Inventors: Hana Golding and Surender Khurana (FDA).
Publications:
1. Pandemic Influenza preparedness: New molecular tools for
evaluation of influenza vaccines and identification of serological
epitopes for avian influenza diagnostic assays at ``Options for the
Control of Influenza VI'' June 17-23, 2007, Toronto, Canada. (oral
presentation)
2. Pandemic Influenza preparedness: Identification of serological
epitopes for use in development of broadly cross-reactive influenza
vaccines at ``National Foundation for Infectious Diseases--11th Annual
Conference on Vaccine Research'', Baltimore: May 5-7, 2008. (oral
presentation).
3. Analysis of antibody repertoires in H5N1 infected and vaccinated
[[Page 55858]]
individuals using influenza whole genome phage display at
``Immunobiology and Pathogenesis of Influenza Infection'', Atlanta:
June 1-3, 2008. (poster presentation).
Patent Status: International Patent Application PCT/US2008/067001
filed 13 Jun 2008 (HHS Reference No. E-236-2007/3-PCT-01).
Licensing Status: Available for exclusive or non-exclusive
licensing.
Licensing Contact: Kevin W. Chang, Ph.D.; 301-435-5018;
changke@mail.nih.gov.
Collaborative Research Opportunity: The FDA, Center for Biologics
Evaluation and Research (CBER), Division of Viral Products, is seeking
statements of capability or interest from parties interested in
collaborative research to further develop, evaluate, or commercialize
these peptides as vaccine candidates or diagnostics. Please contact
Alice Welch at alice.welch@fda.hhs.gov or 301-827-0359 for more
information.
A Rapid Ultrasensitive Assay for Detecting Prions Based on the Seeded
Polymerization of Recombinant Normal Prion Protein (rPrP-sen)
Description of Technology: Prion diseases are neurodegenerative
diseases of great public concern because humans may be infected from
hoofed animals used as food, food products such as milk, or blood
products. Currently available tests for disease-causing prions are
either incapable of detecting low concentrations of prions and must be
used post-mortem or are incapable of detecting low concentrations of
prions economically or accurately. This technology enables rapid and
economical detection of sub-lethal concentrations of prions by using
recombinant, normal, prion protein (rPrP-sen) as a marker or indicator
of infectious prions in a sample. Specifically, prions (contained in a
sample) seed the polymerization of rPrP-sen, and polymerized rPrP-sen
is detected as an amplified indicator of prions in the sample. This
assay differs from the protein-misfolding cyclic amplification assay
(PMCA) because it enables the effective use of rPrP-sen and does not
require multiple amplification cycles unless a higher degree of
sensitivity is required. It is anticipated that this technology can be
combined with additional prion-detection technologies to further
improve the sensitivity of the assay. In its current embodiment, this
assay has been used to detect prions in brain tissue or cerebral spinal
fluid (CSF) from humans (variant CJD), sheep (scrapie), and hamsters
(scrapie).
Advantages:
Uses a consistent, concentrated source of normal prion
protein (rPrP-sen)
Prions are detectable to low levels after a single
amplification round
May be combined with complimentary detection technologies
to improve sensitivity
Demonstrated to be effective at detecting prions from
different species
May be applicable to blood products
Economical
Applications:
A test for live animals or food products
A human diagnostic for early detection of prion diseases
Monitor for effectiveness of treatments or disease
progression
Inventors: Byron W. Caughey, Ryuichiro Atarashi, Roger A. Moore,
and Suzette A. Priola (NIAID).
Related Publications:
1. R Atarashi et al. Simplified ultrasensitive prion detection by
recombinant PrP conversion with shaking. Nat Methods 2008 Mar;5(3):211-
212.
2. R Atarashi et al. Ultrasensitive detection of scrapie prion
protein using seeded conversion of recombinant prion protein. Nat
Methods 2007 Aug;4(8):645-650.
Patent Status:
PCT Application No. PCT/US2008/070656 filed 21 Jul 2008
(HHS Reference No. E-109-2007/1-PCT-01).
U.S. Application No. 12/177,012 filed 21 Jul 2008 (HHS
Reference No. E-109-2007/1-US-02).
Licensing Status: Available for exclusive and non-exclusive
licensing.
Licensing Contact: RC Tang, JD, LLM; 301-435-5031;
tangrc@mail.nih.gov.
Collaborative Research Opportunity: The NIAID Laboratory of
Persistent Viral Diseases, TSE/Prion Biochemistry Section, is seeking
statements of capability or interest from parties interested in
collaborative research to further develop, evaluate, or commercialize
this technology. Please contact Rosemary Walsh at 301-451-3528 or
rcwalsh@niaid.nih.gov.
Dated: September 18, 2008.
Richard U. Rodriguez,
Director, Division of Technology Development and Transfer, Office of
Technology Transfer, National Institutes of Health.
[FR Doc. E8-22610 Filed 9-25-08; 8:45 am]
BILLING CODE 4140-01-P
