[Federal Register Volume 64, Number 179 (Thursday, September 16, 1999)]
[Notices]
[Pages 50288-50290]
From the Federal Register Online via the Government Publishing Office [www.gpo.gov]
[FR Doc No: 99-24122]
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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 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 John Peter Kim,
J.D., M.B.A., Technology Licensing Specialist, at the Office of
Technology Transfer, National Institutes of Health, 6011 Executive
Boulevard, Suite 325, Rockville, Maryland 20852-3804; telephone: 301/
496-7056 ext. 264; fax: 301/402-0220; e-mail: [email protected]. A signed
Confidential Disclosure Agreement will be required to receive copies of
the patent applications.
Oligonucleotides Which Specifically Bind Retroviral Nucleocapsid
Proteins
Alan Rein, Jose Casas-Finet, Robert Fisher, Matthew Fivash, Louis E.
Henderson (NCI)
Serial No. 09/180,903 filed 12 Jul 1999; PCT/US97/08936 filed 19 May
1997; Serial No. 60/017,128 filed 20 May 1996
The human immunodeficiency virus (HIV) is the causative agent of
acquired immunodeficiency syndrome (AIDS). A retroviral protein
species, the gag polyprotein, is involved in the assembly of retrovirus
particles and capable of specific interactions with nucleic acids.
After the virion is released from the cell, the polyprotein is cleaved
by the virus-encoded protease. One of the cleaved products, the
nucleocapsid (NC) protein, then binds to genomic RNA, forming the
ribonucleoprotein core of the mature particle. The interaction between
gag and genomic RNA is known to involve the NC domain of the
polyprotein. In addition, the NC protein plays crucial roles in both
the reverse transcription and integration steps in the viral life
cycle.
The present invention relates to retroviral nucleocapsid proteins,
such as NC and the gag precursor, and their ability of bind to specific
nucleic acid sequences with high affinity. The high affinity of this
interaction has potential applications in the design of new antiviral
approaches and in sensitive detection of HIV particles. Accordingly,
the invention provides for oligonucleotides which bind to
[[Page 50289]]
nucleocapsides proteins with high affinity, molecular decoys for
retroviral nucelocapsid proteins which inhibit viral replication,
targeted molecules comprising high affinity oligonucleotides, assays
for selecting test compounds, and related kits.
Human Monoclonal Antibodies to HIV-1 Envelope Glycoprotein gp120
Brynmor A. Watkins and Marvin S. Reitz, Jr. (NCI) Serial No. 60/141,701
filed 30 Jun 1999
The human immunodeficiency virus (HIV) is the causative agent of
acquired immunodeficiency syndrome (AIDS). Drug-resistance is a
critical factor contributing to the gradual loss of clinical benefit to
treatments for HIV infection. Accordingly, combination therapies have
further evolved to address the mutating resistance of HIV. However,
there has been great concern regarding the apparent growing resistance
of HIV strains to current therapies.
The present invention relates to human monoclonal antibodies to
type 1 human immunodeficiency virus (HIV-1) envelope glycoprotein
gp120, to phage display libraries, and to diagnostic methods and
pharmaceutical compositions which employ these antibodies
therapeutically and prophylactically.
Antiviral Genetic Target Within HIV gag-pol Transframe Region
Shizuko Sei and Hiroaki Mitsuya (NCI)
Serial No. 60/141,072 filed 25 Jun 1999
The human immunodeficiency virus type 1 (HIV-1) is a retrovirus
that infects CD4+ T-lymphocytes, causing immunosuppression and the
acquired immunodeficiency syndrome (AIDS). The subject invention
provides the methods for the potent inhibition of HIV-1 replication,
thus effective measure to treat HIV-1 infection, utilizing
oligonucleotides and oligonucleotide analogues, including peptide
nucleic acids, that can target either DNA or RNA sequences within the
HIV gag-pol transframe region. Blocking the expression of the sequences
mentioned in the subject invention leads to a decreased and
discoordinated synthesis of viral protease, resulting in a significant
reduction in the virion production from HIV-1-infected cells.
Identification and Use of High Efficacy Vaccine Antigens Which
Modulate Antigen Presenting Cells
Polly Matzinger and John P. Ridge (NIAID)
Serial No. 09/313,487 filed 17 May 1999
Through modulation of the activation state of an antigen presenting
cell (APC), the activation of a T cell is concordantly governed, e.g.,
the activation of a killer T cell. The subject invention accordingly
provides uses and applications in the field of immunology for novel
pharmaceuticals, therapeutic and prophylactic agents, and vaccine
components for the treatment and prevention of cancer, systemic
infection, and autoimmune responses.
Thiazepine Inhibitors of HIV-1 Integrase
Yves Pommier, Nouri Neamati, Antonio Garafalo, Vito Nacci (NCI)
Serial No. 60/133,726 filed 12 May 1999
The human immunodeficiency virus (HIV) is the causative agent of
acquired immunodeficiency syndrome (AIDS). Drug-resistance is a
critical factor contributing to the gradual loss of clinical benefit to
treatments for HIV infection. Accordingly, combination therapies have
further evolved to address the mutating resistance of HIV. However,
there has been great concern regarding the apparent growing resistance
of HIV strains to current therapies.
It has been found that a certain class of compounds including
thiazepines and analogs and derivatives thereof are effective and
selective anti-integrase inhibitors. These compounds have been found to
inhibit both viral replication and the activity of purified HIV-1
integrase. The subject invention provides for such compounds and for
methods of inhibiting HIV integrase.
Acetylated and Related Analogues of Chicoric Acid as HIV Integrase
Inhibitors
Terrence R. Burke, Jr., Zhaiwei Lin, He Zhao, Nouri Neamati, Yves
Pommier (NCI)
Serial No. 60/121,127 filed 22 Feb 1999
The human immunodeficiency virus (HIV) is the causative agent of
acquired immunodeficiency syndrome (AIDS). Drug-resistance is a
critical factor contributing to the gradual loss of clinical benefit to
treatments for HIV infection. Accordingly, combination therapies have
further evolved to address the mutating resistance of HIV. However,
there has been great concern regarding the apparent growing resistance
of HIV strains to current therapies.
Chicoric acid has been found to have potential in HIV therapies.
The subject invention provides for new chicoric acid analogues and
derivatives that inhibit HIV-1 integrase, as well as improved synthetic
methods for enantiomers of chicoric acid itself as well as its
analogues and derivatives. Also provided are methods for inhibiting the
replication of HIV-1 either alone or in combination therapies.
Identification of Globotriaosylceramide as a Promoter of HIV-1
Entry Into Cells
Robert Blumenthal, Anu Puri, Peter Jug (NCI)
Serial No. 60/108,903 filed 17 Nov 1998
The human immunodeficiency virus (HIV) is the causative agent of
acquired immunodeficiency syndrome (AIDS). It has been noted that human
immunodeficiency virus type 1 (HIV-1) enters permissive cells by
binding to the cellular receptor, CD4, and chemokine receptors specific
for the envelope glycoprotein (gp120-g41) of a given HIV-1 isolate,
followed by gp120-gp41 mediated fusion of the viral and target cell
membranes.
The subject invention relates to the discovery of glycosphingolipid
cofactors which are essential for entry of a broad range of HIV-1
isolates into cells expressing CD4 and appropriate chemokine receptors.
The invention provides for diagnostics, prophylactics, therapeutics,
and methods of use for the treatment and prevention of HIV-1 infection
and/or AIDS.
Inhibition of Retroviral LTR Promoters by Calcium Response
Modifiers
Elise C. Kohn, Kevin Gardner, Lance A. Liotta (NCI)
Serial No. 09/103,519 filed 23 Jun 1998; Serial No. 08/353,765 filed 12
Dec 1994
The human immunodeficiency virus (HIV) LTR is synergistically
activated by the phorbol ester 12-myristic 13-acetate (PMA) and T cell
specific mitogenic lectin phytohemagglutinin A (PHA). This reflects the
activation of the HIV LTR by endogenous T cell mechanisms in vitro. A
class of non-voltage-gated calcium influx inhibitor compounds is
disclosed which is newly discovered to inhibit the activation of
retroviral LTR promoters, including HIV-LTR, by PHA and PMA. This class
of compounds can be used to delay or suppress the transition of HIV
infection from a latent to a virulent condition, thereby preventing or
ameliorating retroviral diseases such as Acquired Immune Deficiency
Syndrome (AIDS). The compounds are also useful in cancer treatment,
allowing for coordinated therapeutic approaches to retroviral diseases
and related cancers such Kaposi's Sarcoma. The compounds can also be
used to standardize in vitro assays of commercial importance for
clinical and experimental application.
[[Page 50290]]
Inhibition of HIV Replication Using Soluble Tat Peptide Analogs
Fatah Kashanchi (NCI), M.R. Sadaie (FDA), John M. Brady (NCI)
Serial No. 09/269,991 filed 02 Oct 1997; PCT/US97/17704 filed 02 Oct
1997; Serial No. 60/027,658 filed 04 Oct 1996
The subject invention embodies the identification of a domain
within the transactivator Tat protein of HIV-1, a protein which is
necessary for replication of the virus. A number of peptide derivatives
of this domain have been constructed. It has been demonstrated that
some of these derivatives inhibit Tat transactivation of the human
immunodeficiency virus (HIV) LTR (long terminal repeat) promoter. Most
importantly, the peptide derivatives also inhibit virus replication and
thus provide the basis for potential therapeutic antiviral agents for
the treatment of HIV infections.
Dated: September 8, 1999.
Jack Spiegel,
Director, Division of Technology Development and Transfer, Office of
Technology Transfer, National Institutes of Health.
[FR Doc. 99-24122 Filed 9-15-99; 8:45 am]
BILLING CODE 4140-01-M