[Federal Register: August 11, 2005 (Volume 70, Number 154)]
[Notices]
[Page 46877-46879]
From the Federal Register Online via GPO Access [wais.access.gpo.gov]
[DOCID:fr11au05-87]
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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, DHHS.
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.
[[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