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Government-Owned Inventions; Availability for Licensing

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National Institutes of Health, Public Health Service, DHHS.




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.


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. Start Printed 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;

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:

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;

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;

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-ε) 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;

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 Start Printed Page 46879antiviral 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:

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.

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Dated: August 8, 2005.

Steven M. Ferguson,

Director, Division of Technology Development and Transfer, Office of Technology Transfer, National Institutes of Health.

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[FR Doc. 05-15939 Filed 8-10-05; 8:45 am]