Federal Register / Vol. 73, No. 188 / Friday, September 26, 2008 / Notices 55855 

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. 

Improved Bacterial Host for Production 

of Anthrax Toxin Proteins and 

Vaccines: Bacillus anthracis BH450 

Description of Invention: Anthrax 

toxin has previously been made from 

various avirulent strains of Bacillus 

anthracis. The inventors have 

genetically engineered a new strain of B. 

anthracis with improved properties. 

The strain, designated BH450, is totally 

deficient in the ability to make spores 

and to produce a major extracellular 

protease designated Peptidase M4. The 

genetic lesions introduced are defined, 

true deletions, so there is no possibility 

of reversion. Inability to make spores 

assures that laboratories growing the 

strain will not become contaminated 

with the very stable anthrax spores. 

Inability to make peptidase M4 

increases the stability of proteins such 

as anthrax toxin that are secreted to the 

culture medium. 

Applications and Modality: B. 

anthracis vaccine/prophylactic and 

therapeutic studies. 

Market: Research tool useful for 

biodefense/therapeutic studies. 

Development Status: The technology 

is a research tool. 

Inventors: Andrei Pomerantsev, Dana 

Hsu, Ramakrishnan Sitaraman, Craig 

Galloway, Violetta Kivovich, Stephen 

Leppla (NIAID). 

Publication: AP Pomerantsev et al. 

Genome engineering in Bacillus 

anthracis using Cre recombinase. Infect 

Immun. 2006 Jan;74(1):682–693. 

Patent Status: HHS Reference No. E– 

127–2007/0—Research Tool. 

Licensing Status: This technology is 

not patented. The strain will be 

transferred through a Biological 

Materials License. 

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 

Bacterial Diseases, is seeking statements 

of capability or interest from parties 

interested in collaborative research to 

further develop, evaluate, or 

commercialize Bacillus anthracis BH450 

strain. Please contact Dr. Andrei P. 

Pomerantsev at phone 301/451–9817 

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 

constant threat to human health. The 

lethality of anthrax is primarily the 

result of the effects of anthrax toxin, 

which has 3 components: a receptorbinding protein known as ‘‘protective 

antigen’’ (PA) and 2 catalytic proteins 

known as ‘‘lethal factor’’ (LF) and 

‘‘edema factor’’ (EF). Although 

production of an efficient anthrax 

vaccine is an ultimate goal, the benefits 

of vaccination can be expected only if 

a large proportion of the population at 

risk is immunized. The low incidence of 

anthrax suggests that large-scale 

vaccination may not be the most 

efficient means of controlling this 

disease. In contrast, passive 

administration of neutralizing human or 

chimpanzee monoclonal antibody to a 

subject at risk for anthrax or exposed to 

anthrax could provide immediate 

efficacy for emergency prophylaxis 

against or treatment of anthrax. 

Four monoclonal antibodies (mAbs) 

against PA, three mAbs against LF and 

four mAbs specific for EF of anthrax 

were isolated from a phage display 

library generated from immunized 

chimpanzees. Two mAbs recognizing 

PA (W1 and W2), two anti-LF mAbs 

efficiently neutralized the cytotoxicity 

of lethal toxin in a macrophage lysis 

assay. One anti-EF mAb efficiently 

neutralized edema toxin in cell culture. 

All five neutralizing mAbs protected 

animals from anthrax toxin challenge. 

Application: Prophylactics or 

therapeutics against B. anthracis. 

Developmental Status: Preclinical 

studies have been performed. 

Inventors: Zhaochun Chen, Robert 

Purcell, Suzanne Emerson, Stephen 

Leppla, Mahtab Moyeri (NIAID). 

Publication: Z Chen et al. Efficient 

neutralization of anthrax toxin by 

chimpanzee monoclonal antibodies 

against protective antigen. J Infect Dis. 

2006 Mar 1;193(5):625–633. 

Patent Status: PCT Application No. 

PCT/US2008/054609 filed 21 Feb 2008, 

claiming priority to 23 Feb 2007 (HHS 

Reference No. E–123–2007/0–PCT–02); 

U.S. Patent Application No. 11/793,735 

filed 22 Jun 2007 (HHS Reference No. 

E–146–2004/0–US–03) 

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 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 

AGENCY: National Institutes of Health, 

Public Health Service, HHS. 

ACTION: Notice. 

SUMMARY: The inventions listed below 

are owned by an agency of the U.S. 

Government and are available for 

licensing in the U.S. in accordance with 

35 U.S.C. 207 to achieve expeditious 

commercialization of results of 

federally-funded research and 

development. Foreign patent 

applications are filed on selected 

inventions to extend market coverage 

for companies and may also be available 

for licensing. 

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 


jlentini on PROD1PC65 with NOTICES
55856 Federal Register / Vol. 73, No. 188 / Friday, September 26, 2008 / Notices 

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 

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 

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-dglucose, referred to as anthrose, and 

three rhamnose residues. A structure 

similar to anthrose, 4-(3-hydroxy-3- 

methylbutanamido)-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-(3- 

hydroxybutanamido)-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. 


jlentini on PROD1PC65 with NOTICES
Federal Register / Vol. 73, No. 188 / Friday, September 26, 2008 / Notices 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 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 

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 

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 


jlentini on PROD1PC65 with NOTICES
55858 Federal Register / Vol. 73, No. 188 / Friday, September 26, 2008 / Notices 

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 (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 

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, 

Scientific Review Officer, Review Branch, 

DEA, NIDDK, National Institutes of Health, 

Room 753, 6707 Democracy Boulevard, 


jlentini on PROD1PC65 with NOTICES