Government-Owned Inventions; Availability for Licensing, 46877-46879 [05-15939]

Download as PDF 46877 Federal Register / Vol. 70, No. 154 / Thursday, August 11, 2005 / Notices Effective date Subject, city, state FT LAUDERDALE, FL MIRO, AURELIO ...................... LUBBOCK, TX MOKARZEL, KATHRYN ........... AUSTIN, TX MOLINA, LUIS .......................... CORAL GABLES, FL MORGAN, JOANNE ................. WINTER PARK, FL MORRIS, JAMES ..................... KANSAS CITY, MO MOSLEY, THOMAS ................. RICHMOND, VA MURRAY, CLIFF ...................... COSTA MESA, CA NEWTON, STEPHEN ............... BIRMINGHAM, AL NIXON, ALLISON ..................... ASHDOWN, AR O’CONNELL, DENISE .............. WESTVIEW, KY OSUJI, GAD ............................. LOS ANGELES, CA PAIGE, ROBERT ...................... FLORENCE, AZ PEBENITO, KENNETH ............ DARIEN, IL PENDLETON, JAMES .............. DUBLIN, CA POWELL, ARLENE .................. PHOENIX, AZ PRESTON, TRISHA ................. PHOENIX, AZ RANNELS, MARK .................... NEW PROVIDENCE, PA REATH, ERIN ........................... KNOXVILLE, TN REYNOLDS, CONSTANCE ..... S DAYTONA, FL RIDDLE, SHEILA ...................... BURKESVILLE, KY RIDPATH, TRACY .................... HOLLISTER, MO ROLLINS, DONNA ................... MERIDIAN, MS ROMAN, YVONNE ................... HOLLYWOOD, FL ROSAS, IRENE ........................ PHOENIX, AZ ROSEN, TRUDI ........................ OVEIDO, FL RUFFIN, GARY ........................ TUCSON, AZ SALANGSANG, EDGARDO ..... HAYWARD, CA SALTER, KIM ........................... NEDERLAND, TX SCHLAGENHAUFF, SCOTT .... COLUMBIA, MO SCOTT-RODRIGUEZ, MIA ...... PROVIDENCE, RI SEALE, CINDY ......................... LOUISVILLE, KY SHANLEY, SUSAN .................. RIVERSIDE, RI SHERWIN, BOBBY .................. JERSEYVILLE, IL SIKES, LISA ............................. SAGINAW, TX SIMPSON, JODY ..................... HARWICH, MA SIMPSON, PAMELA ................ WINSTON SALEM, NC SMITH, CARRIE ....................... VerDate jul<14>2003 17:36 Aug 10, 2005 8/18/2005 8/18/2005 8/18/2005 8/18/2005 8/18/2005 8/18/2005 8/18/2005 8/18/2005 8/18/2005 8/18/2005 8/18/2005 8/18/2005 8/18/2005 8/18/2005 8/18/2005 8/18/2005 8/18/2005 8/18/2005 8/18/2005 8/18/2005 8/18/2005 8/18/2005 8/18/2005 8/18/2005 8/18/2005 8/18/2005 Subject, city, state SALEM, VA SMITH, STEPHEN ................... KAMUELA, HI STAVRON, JEFFREY .............. TROY, MO STONE, TAMATHA .................. LEWISVILLE, AR STORER, ARLICE .................... LOUISVILLE, KY SUMMER, JOANNE ................. DUTTON, VA SWITALA, JOANNE ................. SOUTHHAMPTON, PA TAYLOR, VICKIE ..................... CHARLOTTE, NC THOMPSON, PATRICIA .......... GARLAND, TX TINHORN, ALBERT ................. KAYENTA, AZ TKACH, MARY ......................... BUCKEYE, AZ TUCKER, LORI ........................ TUCSON, AZ TURNER, TERESA .................. LAKESIDE, CA VIDALES, ABIGAIL .................. LOS ANGELES, CA VILLEGAS, DEBRA .................. ESMONT, VA WEBBER, DAVID ..................... WEST HARTFORD, CT WEDDLE, KELLY ..................... ROANOKE, VA WILLIAMS, PRESTON ............. AURORA, CO WILSON, RHONDA .................. NASHVILLE, TN WITTE, GARY .......................... LAKE HAVASU, AZ WRIGHT, TERESA ................... RAYMORE, MO YI, STEVEN .............................. CENTREVILLE, VA YODER, SHARON ................... HOLLSOPPLE, PA ZITO, ALAINA ........................... CAPE MAY, NJ 8/18/2005 UMANSKY, MICHAEL LOS ANGELES, CA 8/18/2005 8/18/2005 8/18/2005 8/18/2005 8/18/2005 8/18/2005 BERGMAN, BARBARA ............ RHINELANDER, WI CARROLL, JO ANN ................. GLENCOE, MO DENNY, BRIAN ........................ MINNEAPOLIS, MN MERRIFIELD, JANET .............. BRYAN, TX SNYDER, TIMOTHY ................ 8/18/2005 Jkt 205001 PO 00000 Frm 00069 Fmt 4703 Sfmt 4703 Effective date MOORESVILLE, NC 8/18/2005 8/18/2005 OWNED/CONTROLLED BY CONVICTED ENTITIES HIALEAH GARDENS, FL DEFAULT ON HEAL LOAN 8/18/2005 8/18/2005 8/18/2005 8/18/2005 8/18/2005 8/18/2005 8/18/2005 ADONIZIO, CHARLES ............. WILKES BARRE, PA DILL, GREGORY ...................... ASHEVILLE, NC ERICSON, JAMES ................... MINNEAPOLIS, MN JACOBS, STEVEN ................... FLUSHING, NY NELSON, WILLIAM .................. BRUNSWICK, GA VARVA, CHRIS ........................ SWANSBORO, NC WRIGHT-BENFORD, SHEILA W BLOOMFIELD, MI 7/25/2005 8/18/2005 8/18/2005 8/18/2005 8/18/2005 8/18/2005 8/18/2005 8/18/2005 8/18/2005 8/18/2005 8/18/2005 Dated: July 28, 2005. Katherine B. Petrowski, Director, Exclusions Staff, Office of Inspector General. [FR Doc. 05–15888 Filed 8–10–05; 8:45 am] BILLING CODE 4152–01–U 8/18/2005 8/18/2005 DEPARTMENT OF HEALTH AND HUMAN SERVICES 8/18/2005 National Institutes of Health 8/18/2005 Government-Owned Inventions; Availability for Licensing 8/18/2005 National Institutes of Health, Public Health Service, DHHS. ACTION: Notice. AGENCY: 8/18/2005 8/18/2005 8/18/2005 8/18/2005 8/18/2005 FRAUD/KICKBACKS/PROHIBITED ACTS/ SETTLEMENT AGREEMENTS 8/18/2005 Subject, city, state 8/18/2005 FEDERAL/STATE EXCLUSION/ SUSPENSION 8/18/2005 8/18/2005 Effective date 3/21/2005 5/4/2005 4/12/2005 11/30/2004 12/13/2004 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. E:\FR\FM\11AUN1.SGM 11AUN1 46878 Federal Register / Vol. 70, No. 154 / Thursday, August 11, 2005 / Notices Chimeric Lentiviral Vectors Suresh K. Arya (NCI). HHS Reference No. E–191–2005/0— Research Tool. Licensing Contact: Susan Ano; 301/435– 5515; anos@mail.nih.gov. Lentiviral vectors have extensive application in the areas of gene therapy, functional genomics, and target validation, among others. Available for licensing as biological materials are chimeric HIV–1 and HIV–2 lentiviral transfer and packaging vectors. When using lentiviral vectors, it is important that the vectors incorporate as many safety features as possible to avoid the generation of recombinants or replication competent viruses. In other available vector systems derived from HIV–1 or HIV–2, viral genetic elements needed for vector production have been split into three parts to address safety concerns. In the chimeric vectors available herein, the safety is further enhanced by taking advantage of the sequence divergence of HIV–1 and HIV– 2 coupled with functionally complementary nature of the genetic elements. The chimeric packaging vectors primarily involve swapping of the gag-pol or tat-rev genes, while the transfer vectors involve swapping of the leader-gag sequences. These vectors are potential candidates for use in gene therapy, for cell therapy with genetically modifying stem cells ex vivo, for use of siRNA or RNA interference for therapeutics, for creation of transgenic animals, and for pathway analysis and target validation by introducing novel genes. In addition to licensing, the technology is available for further development through collaborative research opportunities with the inventors. Scytovirin Domain 1 (SD1) Related Polypeptide Barry R. O’Keefe et al. (NCI) U.S. Provisional Application No. 60/ 684,353 filed 25 May 2005 (HHS Reference No. E–180–2005/0–US–01). Licensing Contact: Sally Hu; 301/435– 5606; e-mail: hus@mail.nih.gov. The invention provides composition claims for a scytovirin domain 1 (SD1) antiviral polypeptide, nucleic acids encoding the polypeptide, related fusion proteins and conjugates, isolated cells, vectors, and antibodies that bind to the polypeptide. The polypeptide of this invention has the ability to bind to viral proteins, such as gp41 and gp120 of HIV, and exhibit anti-viral activity against type C and D retroviruses such as HIV–1 and HIV–2, Ebola, SARS, Influenza viruses and others. The VerDate jul<14>2003 16:14 Aug 10, 2005 Jkt 205001 invention also provides for methods of use to inhibit viral infections therapeutically and prophylactically as well as methods of inhibiting virus in biological samples or inanimate objects. Thus, further development of the invention may yield novel therapies and methods in the prevention of HIV and other retroviruses, and treatment of chronic infection in patients with resistance to current therapies. In addition to licensing, the technology is available for further development through collaborative research opportunities with the inventors. Recombinant MVA Viruses Expressing Clade A/G and Clade B Modified HIV Env, Gag and Pol Genes Useful for HIV Vaccine Development Bernard Moss and Linda S. Wyatt (NIAID) U.S. Provisional Application No. 60/ 604,918 filed 27 Aug 2004 (HHS Reference No. E–337–2004/0–US–01). Licensing Contact: Susan Ano; 301/435– 5515; anos@mail.nih.gov. The current technology relates to the construction, characterization and immunogenicity of modified vaccinia Ankara (MVA) recombinant viruses. The MVA double recombinant viruses express modified/truncated HIV–1 Env and mutated HIV Gag Pol under the control of vaccinia virus early/late promoters. This technology describes the MVA double recombinant viruses made by homologous recombination of single MVA recombinants, one expressing Env and one expressing Gag Pol. These single MVA recombinants are made using a transiently expressed GFP marker that is deleted in the final viruses. Two recombinant MVA viruses (MVA 65A/G and MVA 62B) made by this technology have been shown to produce HIV virus-like-particles that are immunogenic in mice. In addition, these two recombinant MVA viruses demonstrate stability through repeated passage of the LVD Seed Stock. This invention provides safe and stable immunogenic clade A/G and clade B vectors that may be tested as an AIDS vaccine candidate. Therefore, it is a promising technology to develop prophylactic and therapeutic AIDS vaccines for U.S. and for West Africa, particularly when used in combination with a DNA vaccine. Chondroitin Sulphate A Binding Domains: Potential Vaccine for Malaria Louis H. Miller (NIAID), et al. U.S. Provisional Application No. 60/ 615,300 filed 30 Sep 2004 (DHHS Reference No. E–221–2004/0–US–01). PO 00000 Frm 00070 Fmt 4703 Sfmt 4703 Licensing Contact: Robert M. Joynes; 301/594–6565; joynesr@mail.nih.gov. The subject invention is related to a potential vaccine against malaria, and in particular to a vaccine that can prevent malaria infection in pregnant women. The invention relates to the identification of chondroitin sulphate A (CSA) binding domains in var2CSA homologs from different parasite strains. Malaria in pregnancy is a serious complication associated with the parasitized erythrocyte (PE) sequestration in the placenta. With successive pregnancies, pregnant women develop antibodies that recognize placental variants worldwide suggesting these isolates express conserved determinants. Plasmodium falciparum encodes multiple copies of an erythrocyte surface adhesion ligands called var genes. Recent work suggests that two different var genes (var1CSA and var2CSA) could have an important role in PE binding to chondroitin sulphate A (CSA), a primary placental adherence receptor. It has now been shown that var2CSA is transcribed in CSA-binding parasites and that the disruption of var2CSA results in the inability of the parasites to recover the CSA-binding phenotype. Furthermore, when expressed in Chinese hamster ovary (CHO) cells, three Duffy bindinglike domains (DBL2–X, DBL3–X and DBL6-e) from var2CSA revealed strong and specific binding to CSA. The identification of multiple binding domains in var2CSA is envisioned as forming the basis of a vaccine against malaria, especially in pregnancy. In addition to licensing, the technology is available for further development through collaborative research opportunities with the inventors. Vaccines and Methods of Treating Drug-Resistant HIV–1 and Hepatitis B Viruses Andrew Catanzaro (NCI), Jay A. Berzofsky (NCI), Robert Yarchoan (NCI), Takahiro Okazaki (NCI), James T. Snyder II (NCI), Samuel Broder. U.S. Provisional Application No. 60/ 655,984 filed 22 Feb 2005 (DHHS Reference No. E–137–2003/1–US–01). Licensing Contact: Robert M. Joynes; 301/594–6565; joynesr@mail.nih.gov. This technology relates to methods for lowering a viral load of a virus where the virus causes a chronic viral infection and is resistant to an antiviral drug. The method comprises administering to a host a medicament comprising an antiviral drug to restrict the intracellular multiplication of the virus and that is capable of selecting for a predetermined E:\FR\FM\11AUN1.SGM 11AUN1 Federal Register / Vol. 70, No. 154 / Thursday, August 11, 2005 / Notices antiviral drug-resistant mutation in a viral protein. The medicament further comprises a synthetic peptide that comprises the predetermined antiviral drug-resistant mutation and at least six amino acid residues flanking that mutation that are identical to the amino acid sequence of the viral protein of the antiviral drug-resistant virus. The synthetic peptide induces a cytotoxic T lymphocyte (CTL) response specific for cells infected with the antiviral drugresistant virus. The immunostimulating peptide may be further improved by epitope-enhancement for inducing specific CTLs. The antiviral protection against drug-resistant virus shown by compositions of the present invention and mediated by human HLA-restricted CTL has not been previously achieved. Further, the compositions and methods of this technology are useful to target many viruses that can develop antiviral drug resistance, including HIV–1, HIV– 2, hepatitis B virus, hepatitis C virus, and human herpesviruses. Design of a Novel Peptide Inhibitor of HIV Fusion That Disrupts the Internal Trimeric Coiled-coil of gp41 Marius G. Clore, Carole A. Bewley, and John M. Louis (NIDDK). U.S. Provisional Application No. 60/446,225 filed 11 Feb 2003 (HHS Reference No. E–236–2002/0–US–01); PCT Application No. PCT/US04/03794 filed 10 Feb 2004, which published as WO 2004/072099 on 11 Aug 2004 (HHS Reference No. E–236–2002/0PCT–02). Licensing Contact: Sally Hu; 301/435– 5606; e-mail: hus@mail.nih.gov. This invention provides a peptide derived from the sequence of the Nterminal helix (residues 546–581) of the gp41 ectodomain of HIV–1. The peptide, called N36Mut(e,g), contains nine substitutions and disrupts interactions with the C-terminal region of the gp41 ectodomain. N36Mut(e,g) inhibits HIVenvelope mediated cell fusion about 50-fold more effectively than the native sequence (residues 546–581 of HIV–1 envelope) from which it was derived. Thus, N36Mut(e,g) and derivatives has potential as an anti-HIV therapeutic agent as a HIV fusion inhibitor. This research is described, in part, in CA Bewley et al., ‘‘Design of a novel peptide inhibitor of HIV fusion that disrupts the internal trimeric coiled-coil of gp41,’’ J. Biol. Chem. (2002 Apr 19) 277(16):14238–14245; Epub on 21 Feb 2002 as doi:10.1074/jbc.M201453200. VerDate jul<14>2003 16:14 Aug 10, 2005 Jkt 205001 Dated: August 8, 2005. Steven M. Ferguson, Director, Division of Technology Development and Transfer, Office of Technology Transfer, National Institutes of Health. [FR Doc. 05–15939 Filed 8–10–05; 8:45 am] 46879 DEPARTMENT OF HEALTH AND HUMAN SERVICES National Institutes of Health National Heart, Lung, and Blood Institute; Notice of Meeting BILLING CODE 4140–01–P DEPARTMENT OF HEALTH AND HUMAN SERVICES National Institutes of Health National Cancer Institute; Notice of Closed Meeting 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 meeting. The meeting 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 Cancer Institute Special Emphasis Panel, SPORE in Lung and Genitourinary Cancers. Date: September 13–15, 2005. Time: 8 a.m. to 5 p.m. Agenda: To review and evaluate grant applications. Place: Holiday Inn Georgetown, 2101 Wisconsin Avenue NW., Washington, DC 20007. Contact Person: Shamala K. Srinivas, PhD, Scientific Review Administrator, Grants Review Branch, Division of Extramural Activities, National Cancer Institute, National Institutes of Health, 6116 Executive Boulevard, Room 8133, Bethesda, MD 20892, 301–594–1224. (Catalogue of Federal Domestic Assistance Program Nos. 93.392, Cancer Construction; 93.393, Cancer Cause and Prevention Research; 93.394, Cancer Detection and Diagnosis Research; 93.395, Cancer Treatment Research; 93.396, Cancer Biology Research; 93.397, Cancer Centers Support; 93.398, Cancer Research Manpower; 93.399, Cancer Control, National Institutes of Health, HHS) Dated: August 4, 2005. Anthony M. Coelho, Jr., Acting Director, Office of Federal Advisory Committee Policy. [FR Doc. 05–15941 Filed 8–10–05; 8:45 am] BILLING CODE 4140–01–M PO 00000 Frm 00071 Fmt 4703 Sfmt 4703 Pursuant to section 10(d) of the Federal Advisory Committee Act, as amended (U.S.C. Appendix 2), notice is hereby given of the National Heart, Lung, and Blood Advisory Council. The meeting will be open to the public as indicated below, with attendance limited to space available. Individuals who plan to attend and need special assistance, such as sign language interpretation or other reasonable accommodations, should notify the Contact Person listed below in advance of the meeting. The meeting 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 Heart, Lung, and Blood Advisory Council. Date: September 16, 2005. Open: 8:30 a.m. to 12 p.m. Agenda: Discussion of program policies and issues. Place: National Institutes of Health, Natcher Building, 45 Center Drive, Room E1 and E2, Bethesda, MD 20892. Closed: 1 p.m. to 4 p.m. Agenda: To review and evaluate grant applications. Place: National Institutes of Health, Natcher Building, 45 Center Drive, Room E1 and E2, Bethesda, MD 20892. Contact Person: Deborah P. Beebe, PhD, Director, Division of Extramural Affairs, National Heart, Lung, and Blood Institute, National Institutes of Health, Two Rockledge Center, Room 7100, 6701 Rockledge Drive, Bethesda, MD 20892, (301) 435–0260. Any interested person may file written comments with the committee by forwarding the statement to the Contact Person listed on this notice. The statement should include the name, address, telephone number and when applicable, the business of professional affiliation of the interested person. In the interest of security, NIH has instituted stringent procedures for entrance into the building by nongovernment employees. Persons without a government I.D. will need to show a photo I.D. and sign-in at the security desk upon entering the building. E:\FR\FM\11AUN1.SGM 11AUN1

Agencies

[Federal Register Volume 70, Number 154 (Thursday, August 11, 2005)]
[Notices]
[Pages 46877-46879]
From the Federal Register Online via the Government Printing Office [www.gpo.gov]
[FR Doc No: 05-15939]


-----------------------------------------------------------------------

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 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.

[[Page 46878]]

Chimeric Lentiviral Vectors

Suresh K. Arya (NCI).
HHS Reference No. E-191-2005/0--Research Tool.
Licensing Contact: Susan Ano; 301/435-5515; anos@mail.nih.gov.

    Lentiviral vectors have extensive application in the areas of gene 
therapy, functional genomics, and target validation, among others. 
Available for licensing as biological materials are chimeric HIV-1 and 
HIV-2 lentiviral transfer and packaging vectors. When using lentiviral 
vectors, it is important that the vectors incorporate as many safety 
features as possible to avoid the generation of recombinants or 
replication competent viruses. In other available vector systems 
derived from HIV-1 or HIV-2, viral genetic elements needed for vector 
production have been split into three parts to address safety concerns. 
In the chimeric vectors available herein, the safety is further 
enhanced by taking advantage of the sequence divergence of HIV-1 and 
HIV-2 coupled with functionally complementary nature of the genetic 
elements. The chimeric packaging vectors primarily involve swapping of 
the gag-pol or tat-rev genes, while the transfer vectors involve 
swapping of the leader-gag sequences. These vectors are potential 
candidates for use in gene therapy, for cell therapy with genetically 
modifying stem cells ex vivo, for use of siRNA or RNA interference for 
therapeutics, for creation of transgenic animals, and for pathway 
analysis and target validation by introducing novel genes.
    In addition to licensing, the technology is available for further 
development through collaborative research opportunities with the 
inventors.

Scytovirin Domain 1 (SD1) Related Polypeptide

Barry R. O'Keefe et al. (NCI)
U.S. Provisional Application No. 60/684,353 filed 25 May 2005 (HHS 
Reference No. E-180-2005/0-US-01).
Licensing Contact: Sally Hu; 301/435-5606; e-mail: hus@mail.nih.gov.

    The invention provides composition claims for a scytovirin domain 1 
(SD1) antiviral polypeptide, nucleic acids encoding the polypeptide, 
related fusion proteins and conjugates, isolated cells, vectors, and 
antibodies that bind to the polypeptide. The polypeptide of this 
invention has the ability to bind to viral proteins, such as gp41 and 
gp120 of HIV, and exhibit anti-viral activity against type C and D 
retroviruses such as HIV-1 and HIV-2, Ebola, SARS, Influenza viruses 
and others. The invention also provides for methods of use to inhibit 
viral infections therapeutically and prophylactically as well as 
methods of inhibiting virus in biological samples or inanimate objects. 
Thus, further development of the invention may yield novel therapies 
and methods in the prevention of HIV and other retroviruses, and 
treatment of chronic infection in patients with resistance to current 
therapies.
    In addition to licensing, the technology is available for further 
development through collaborative research opportunities with the 
inventors.

Recombinant MVA Viruses Expressing Clade A/G and Clade B Modified HIV 
Env, Gag and Pol Genes Useful for HIV Vaccine Development

Bernard Moss and Linda S. Wyatt (NIAID)
U.S. Provisional Application No. 60/604,918 filed 27 Aug 2004 (HHS 
Reference No. E-337-2004/0-US-01).
Licensing Contact: Susan Ano; 301/435-5515; anos@mail.nih.gov.

    The current technology relates to the construction, 
characterization and immunogenicity of modified vaccinia Ankara (MVA) 
recombinant viruses. The MVA double recombinant viruses express 
modified/truncated HIV-1 Env and mutated HIV Gag Pol under the control 
of vaccinia virus early/late promoters. This technology describes the 
MVA double recombinant viruses made by homologous recombination of 
single MVA recombinants, one expressing Env and one expressing Gag Pol. 
These single MVA recombinants are made using a transiently expressed 
GFP marker that is deleted in the final viruses. Two recombinant MVA 
viruses (MVA 65A/G and MVA 62B) made by this technology have been shown 
to produce HIV virus-like-particles that are immunogenic in mice. In 
addition, these two recombinant MVA viruses demonstrate stability 
through repeated passage of the LVD Seed Stock. This invention provides 
safe and stable immunogenic clade A/G and clade B vectors that may be 
tested as an AIDS vaccine candidate. Therefore, it is a promising 
technology to develop prophylactic and therapeutic AIDS vaccines for 
U.S. and for West Africa, particularly when used in combination with a 
DNA vaccine.

Chondroitin Sulphate A Binding Domains: Potential Vaccine for Malaria

Louis H. Miller (NIAID), et al.
U.S. Provisional Application No. 60/615,300 filed 30 Sep 2004 (DHHS 
Reference No. E-221-2004/0-US-01).
Licensing Contact: Robert M. Joynes; 301/594-6565; 
joynesr@mail.nih.gov.

    The subject invention is related to a potential vaccine against 
malaria, and in particular to a vaccine that can prevent malaria 
infection in pregnant women. The invention relates to the 
identification of chondroitin sulphate A (CSA) binding domains in 
var2CSA homologs from different parasite strains. Malaria in pregnancy 
is a serious complication associated with the parasitized erythrocyte 
(PE) sequestration in the placenta. With successive pregnancies, 
pregnant women develop antibodies that recognize placental variants 
worldwide suggesting these isolates express conserved determinants. 
Plasmodium falciparum encodes multiple copies of an erythrocyte surface 
adhesion ligands called var genes. Recent work suggests that two 
different var genes (var1CSA and var2CSA) could have an important role 
in PE binding to chondroitin sulphate A (CSA), a primary placental 
adherence receptor. It has now been shown that var2CSA is transcribed 
in CSA-binding parasites and that the disruption of var2CSA results in 
the inability of the parasites to recover the CSA-binding phenotype. 
Furthermore, when expressed in Chinese hamster ovary (CHO) cells, three 
Duffy binding-like domains (DBL2-X, DBL3-X and DBL6-[egr]) from var2CSA 
revealed strong and specific binding to CSA. The identification of 
multiple binding domains in var2CSA is envisioned as forming the basis 
of a vaccine against malaria, especially in pregnancy.
    In addition to licensing, the technology is available for further 
development through collaborative research opportunities with the 
inventors.

Vaccines and Methods of Treating Drug-Resistant HIV-1 and Hepatitis B 
Viruses

Andrew Catanzaro (NCI), Jay A. Berzofsky (NCI), Robert Yarchoan (NCI), 
Takahiro Okazaki (NCI), James T. Snyder II (NCI), Samuel Broder.
U.S. Provisional Application No. 60/655,984 filed 22 Feb 2005 (DHHS 
Reference No. E-137-2003/1-US-01).
Licensing Contact: Robert M. Joynes; 301/594-6565; 
joynesr@mail.nih.gov.

    This technology relates to methods for lowering a viral load of a 
virus where the virus causes a chronic viral infection and is resistant 
to an antiviral drug. The method comprises administering to a host a 
medicament comprising an antiviral drug to restrict the intracellular 
multiplication of the virus and that is capable of selecting for a 
predetermined

[[Page 46879]]

antiviral drug-resistant mutation in a viral protein. The medicament 
further comprises a synthetic peptide that comprises the predetermined 
antiviral drug-resistant mutation and at least six amino acid residues 
flanking that mutation that are identical to the amino acid sequence of 
the viral protein of the antiviral drug-resistant virus. The synthetic 
peptide induces a cytotoxic T lymphocyte (CTL) response specific for 
cells infected with the antiviral drug-resistant virus. The 
immunostimulating peptide may be further improved by epitope-
enhancement for inducing specific CTLs. The antiviral protection 
against drug-resistant virus shown by compositions of the present 
invention and mediated by human HLA-restricted CTL has not been 
previously achieved. Further, the compositions and methods of this 
technology are useful to target many viruses that can develop antiviral 
drug resistance, including HIV-1, HIV-2, hepatitis B virus, hepatitis C 
virus, and human herpesviruses.

Design of a Novel Peptide Inhibitor of HIV Fusion That Disrupts the 
Internal Trimeric Coiled-coil of gp41

Marius G. Clore, Carole A. Bewley, and John M. Louis (NIDDK).
U.S. Provisional Application No. 60/446,225 filed 11 Feb 2003 (HHS 
Reference No. E-236-2002/0-US-01);
PCT Application No. PCT/US04/03794 filed 10 Feb 2004, which published 
as WO 2004/072099 on 11 Aug 2004 (HHS Reference No. E-236-2002/0-PCT-
02).
Licensing Contact: Sally Hu; 301/435-5606; e-mail: hus@mail.nih.gov.

    This invention provides a peptide derived from the sequence of the 
N-terminal helix (residues 546-581) of the gp41 ectodomain of HIV-1. 
The peptide, called N36Mut(e,g), contains nine substitutions 
and disrupts interactions with the C-terminal region of the gp41 
ectodomain. N36Mut(e,g) inhibits HIV-envelope mediated cell 
fusion about 50-fold more effectively than the native sequence 
(residues 546-581 of HIV-1 envelope) from which it was derived. Thus, 
N36Mut(e,g) and derivatives has potential as an anti-HIV 
therapeutic agent as a HIV fusion inhibitor.
    This research is described, in part, in CA Bewley et al., ``Design 
of a novel peptide inhibitor of HIV fusion that disrupts the internal 
trimeric coiled-coil of gp41,'' J. Biol. Chem. (2002 Apr 19) 
277(16):14238-14245; Epub on 21 Feb 2002 as doi:10.1074/jbc.M201453200.

    Dated: August 8, 2005.
Steven M. Ferguson,
Director, Division of Technology Development and Transfer, Office of 
Technology Transfer, National Institutes of Health.
[FR Doc. 05-15939 Filed 8-10-05; 8:45 am]
BILLING CODE 4140-01-P
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