Federal Register / Vol. 67, No. 1 / Wednesday, January 2, 2002 / Notices 85

Subject city, state Effective 

date 

Robinson, Cynane Ann Yetta ... 12/20/2001

Southfield, MI 

Rodebaugh, Cheryl Lynn .......... 12/20/2001

Denver, CO 

Rose, Keith D ........................... 12/20/2001

Big Rapids, MI 

Roudebush, Mark D ................. 12/20/2001

Cordova, TN 

Rouselle, Dionne Marie ............ 12/20/2001

Memphis, TN 

Rubinstein, David M ................. 12/20/2001

Tamarac, FL 

Schwirian, Jay A ....................... 12/20/2001

White Oak, PA 

Smith, Terrance Herbert ........... 12/20/2001

Sioux Falls, SD 

Smith, William H III ................... 12/20/2001

Philadelphia, PA 

Sparks, Darlene V .................... 12/20/2001

Annandale, VA 

Stevens, Joanne K ................... 12/20/2001

Broadview Hgts, OH 

Strasser, Robert T .................... 12/20/2001

Lake Zurich, IL 

Thompson, Emma R ................ 12/20/2001

Lithonia, GA 

Van Brookhoven, Gloria ........... 12/20/2001

Atlanta, GA 

Vodvarka, James M .................. 12/20/2001

Steubenville, OH 

Webb, James R ........................ 12/20/2001

Shawnee Mission, KS 

Wohlschlaeger, Michael Alan ... 12/20/2001

Panama City Bch, FL 

Wolf, Jacob M ........................... 12/20/2001

Akron, OH 

Wright, Bill G ............................ 12/20/2001

Lincoln, NE 

Yoder, Patricia L ....................... 12/20/2001

Ocklawaha, FL 

Young-Cheney, Joan E ............ 12/20/2001

Creswell, OR 

Peer Review Organization Cases

Hinkley, Bruce Stanton ............. 11/14/2001

Dallas, TX 

Dated: December 3, 2001. 

Calvin Anderson, Jr., 

Director, Health Care Administrative 

Sanctions, Office of Inspector General.

[FR Doc. 01–32156 Filed 12–31–01; 8:45 am] 

BILLING CODE 4150–04–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, DHHS.

ACTION: Notice.

SUMMARY: The inventions listed below 

are owned by agencies 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 

contacting Peter A. Soukas, J.D., at the 

Office of Technology Transfer, National 

Institutes of Health, 6011 Executive 

Boulevard, Suite 325, Rockville, 

Maryland 20852–3804; telephone: 301/

496–7056 ext. 268; fax: 301/402–0220; 

e-mail: soukasp@od.nih.gov. A signed 

Confidential Disclosure Agreement will 

be required to receive copies of the 

patent applications. 

LL–37 is an Immunostimulant 

Oleg Chertov (NCI), Joost Oppenheim 

(NCI), De Yang (NCI), Qian Chen 

(NCI), Ji Wang (NCI), Mark Anderson 

(EM), Joseph Wooters (EM) 

Serial No. 09/960,876 filed 21 Sep 2001

This invention relates to use of an 

antimicrobial peptide as a vaccine 

adjuvant. LL–37 is the cleaved 

antimicrobial 37-residue C-terminal 

peptide of hCAP18, the only identified 

member in humans of a family of 

proteins called cathelicidins. LL–37/

hCAP18 is produced by neutrophils and 

various epithelial cells. LL–37 is well 

known as an antimicrobial peptide. 

However, although antimicrobial 

peptides have generally been considered 

to contribute to host innate 

antimicrobial defense, some of them 

may also contribute to adaptive 

immunity against microbial infection. 

The inventors have shown that LL–37 

utilizes formyl peptide receptor-like 1 

(FPLR1) as a receptor to activate human 

neutrophils, monocytes, and T cells. 

Since leukocytes participate in both 

innate and adaptive immunity, the fact 

that LL–37 can chemoattract human 

leukocytes may provide one additional 

mechanism by which LL–37 can 

contribute to host defense against 

microbial invasion, by participating in 

the recruitment of leukocytes to sites of 

infection. The invention claims methods 

of enhancing immune responses 

through the administration of LL–37 

alone, in conjunction with a vaccine, 

and methods of treating autoimmune 

diseases. The invention is further 

described in Chertov et. al., ‘‘LL–37, the 

neutrophil granule- and epithelial cellderived cathelicidin, utilizes formyl 

peptide receptor-like 1 (FPRL1) as a 

receptor to chemoattract human 

peripheral blood neutrophils, 

monocytes, and T cells,’’ J Exp. Med. 

2000 Oct 2;192(7):1069–74. 

A Method for Bioconjugation Using 

Diels-Alder Cycloaddition 

Vince Pozsgay (NICHD) 

Serial Number 09/919,637 filed 01 Aug 

2001

This invention relates to a new 

method for the synthesis of conjugate 

vaccines using the Diels-Alder 

cycloaddition reaction to covalently 

attach a carbohydrate antigen from a 

pathogen to a protein carrier. The DielsAlder reaction has not been extended to 

conjugation involving biopolymers or 

other types of polymeric materials. 

Advantages of this method are that 

cross-linking during conjugation is 

entirely avoided in addition to the mild 

chemical conditions under which this 

synthesis method proceeds. Diels-Alder 

reactions commonly take place in hightemperature environments; the method 

contemplated by this invention takes 

place at much lower temperatures. In 

addition to claiming methods of 

synthesis for conjugate vaccines using 

the Diels-Alder cycloaddition, the 

patent application claims vaccines 

produced utilizing the method, and 

methods of inducing antibodies which 

react with the polysaccharides 

contemplated by the invention. 

Identification of New Small RNAs and 

ORFs 

Susan Gottesman (NCI), Gisela Storz 

(NICHD), Karen Wassarman (NICHD), 

Francis Repoila (NCI), Carsten 

Rosenow (EM) 

Serial No. 60/266,402 filed 01 Feb 2001

The inventors have isolated a number 

of previously unknown sRNAs found in 

E. coli. Previous scientific publications 

by the inventors and others regarding 

sRNAs have shown these sRNAs to 

serve important regulatory roles in the 

cell, such as regulators of virulence and 

survival in host cells. Prediction of the 

presence of genes encoding sRNAs was 

accomplished by combining sequence 

information from highly conserved 

intergenic regions with information 

about the expected transcription of 

neighboring genes. Microarray analysis 

also was used to identify likely 

candidates. Northern blot analyses were 

then carried out to demonstrate the 

presence of the sRNAs. Three of the 

sRNAs claimed in the invention regulate 

(candidates 12 and 14, negatively and 

candidate 31, positively) expression of 

RpoS, a major transcription factor in 

bacteria that is important in many 

pathogens because it regulates (amongst 

other things) virulence. The inventors’

data show that these sRNAs are highly 

86 Federal Register / Vol. 67, No. 1 / Wednesday, January 2, 2002 / Notices 

conserved among closely related 

bacterial species, including Salmonella 

and Klebsiella, presenting a unique 

opportunity to develop both specific 

and broad-based antibiotic therapeutics. 

The invention contemplates a number of 

uses for the sRNAs, including, but not 

limited to, inhibition by antisense, 

manipulation of gene expression, and 

possible vaccine candidates. 

Peptides that Stabilize Protein Antigens 

and Enhance Presentation to CD8+ T 

Cells 

Roger Kurlander, Elizabeth Chao, Janet 

Fields (CC) 

DHHS Reference No. E–172–99/1 filed 

12 Dec 2000 (PCT/US00/33027, 

published as WO 01/40275), with 

priority to 06 Dec 1999

This invention relates to compositions 

and methods for stabilizing an antigen 

against proteolytic degradation and 

enhancing its presentation to CD8+ 

cells. The invention claims ‘‘fusion 

agents,’’ isolated molecules comprising 

a hydrophobic peptide joined to an 

epitope to which a CD8+ T cell response 

is desired. Also claimed in the 

invention are the nucleic acid sequences 

that encode the fusion agents. Recently, 

there has been great interest in 

developing vaccines to induce 

protective CD8+ T cell responses, 

however, there are practical obstacles to 

this goal. Although purified antigenic 

peptides are effectively presented in 

vitro, introduced in a purified form they 

often do not stimulate effective T cell 

responses in vivo because the antigens 

are insufficiently immunogenic and too 

easily degraded. Adjuvants or infectious 

‘‘carriers’’ often can enhance these 

immune responses, however, these 

added agents can cause unacceptable 

local or systemic side effects. The 

present invention increases antigen 

stability and promotes in vivo responses 

in the absence of an adjuvant or active 

infection. 

The invention describes three variants 

of lemA, an antigen recognized by CD8+ 

cells in mice infected with Listeria 

monocytogenes. The antigenic and 

stabilizing properties of lemA can be 

accounted for by the covalent 

association of the immunogenic 

aminoterminal hexapeptide with the 

protease resistant scaffolding provided 

by amino acids 7 to 33 of the lemA 

sequence (lemA(7–33)). Variants t-lemA, 

and s-lemA bearing an antigenic 

sequence immediately preceding 

lemA(7–33), and lemS containing an 

immunogenic sequence immediately 

after lemA(7–33), each induce a CD8+ T 

cell response and protect the crucial 

immunogenic oligopeptide from 

protease degradation. The site of antigen 

insertion relative to lemA(7–33) can 

influence antigen processing by 

preferentially promoting processing 

either in the cytoplasm or endosomal 

compartment. Therefore, several 

embodiments of the invention involve 

the construction of antigen processing 

protein molecules and their methods of 

use. Alternatively, a DNA sequence 

coding lemA(7–33) may be inserted at 

an appropriate site to enhance the 

immunogenicity of the antigenic 

element coded by a DNA vaccine. In 

sum, this invention is an attractive, 

nontoxic alternative to protein/adjuvant 

combinations in eliciting CD8 responses 

in vivo and a useful element for 

enhancing the efficiency with which 

products coded by DNA vaccines are 

processed and presented in vivo. 

Because lemA(7–33) is particularly 

effective in protecting oligopeptides 

from proteases, this invention may have 

particular usefulness in enhancing local 

T cell at sites such as mucosal surfaces 

where there may be high proteolytic 

activity. 

For more specific information about 

the invention or to request a copy of the 

patent application, please contact Peter 

Soukas at the telephone number or email listed above. Additionally, please 

see a related article published in the 

Journal of Immunology at: 

1999;163:6741–6747. 

Vibrio cholerae O139 Conjugate 

Vaccines 

Shousun Szu, Zuzana Kossaczka, John 

Robbins (NICHD) 

DHHS Reference No. E–274–00/0 filed 

01 Sep 2000 (PCT/US00/24119) 

Cholera remains an important public 

health problem. Epidemic cholera is 

caused by two Vibrio cholerae serotypes 

O1 and O139. The disease is spread 

through contaminated water. According 

to information reported to the World 

Health Organization in 1999, nearly 

8,500 people died and another 223,000 

were sickened with cholera worldwide. 

This invention is a polysaccharideprotein conjugate vaccine to prevent 

and treat infection by Vibrio cholerae 

O139 comprising the capsular 

polysaccharide (CPS) of V. cholerae 

O139 conjugated through a dicarboxylic 

acid dihydrazide linker to a mutant 

diphtheria toxin carrier. In addition to 

the conjugation methods, also claimed 

in the invention are methods of 

immunization against V. cholerae O139 

using the conjugates of the invention. 

The inventors have shown that the 

conjugates of the invention elicited in 

mice high levels of serum antibodies to 

CPS, a surface antigen of Vibrio cholerae 

O139, that have vibriocidal activity. 

Clinical trials of the two most 

immunogenic conjugates have been 

planned by the inventors. This 

invention is further described in 

Infection and Immunity 68(9), 5037–

5043, Sept. 2000.

Dated: December 19, 2001. 

Jack Spiegel, 

Director, Division of Technology Development 

and Transfer, Office of Technology Transfer, 

National Institutes of Health.

[FR Doc. 01–32170 Filed 12–31–01; 8:45 am] 

BILLING CODE 4140–01–P

DEPARTMENT OF HEALTH AND 

HUMAN SERVICES 

National Institutes of Health 

National Institute of Arthritis and 

Musculoskeletal and Skin 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 552(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 

Arthritis and Musculoskeletal and Skin 

Diseases Special Emphasis Panel. 

Date: December 21, 2001. 

Time: 8:30 am to 3:00 pm. 

Agenda: To review and evaluate grant 

applications. 

Place: Natcher Building, 45 Center Drive, 

Conference Rooms E1/E2, Bethesda, MD 

20892. (Telephone Conference Call) 

Contact Person: Tracy A. Shahan, PhD, 

Scientific Review Administrator, National 

Institute of Arthritis and Musculoskeletal and 

Skin Diseases, Natcher Building, MSC 6500, 

45 Center Drive, 5AS–25H, Bethesda, MD 

20892, (301) 594–4952. 

This notice is being published less than 15 

days prior to the meeting due to the timing 

limitations imposed by the review and 

funding cycle.

Name of Committee: National Institute of 

Arthritis and Musculoskeletal and Skin 

Diseases Special Emphasis Panel. 

Date: December 21, 2001. 

Time: 3:30 pm to 4:30 pm. 

Agenda: To review and evaluate grant 

applications. 

Place: Natcher Building, 45 Center Drive, 

Conference Rooms E1/E2, Bethesda, MD 

20892. (Telephone Conference Call)