[Federal Register Volume 61, Number 207 (Thursday, October 24, 1996)]
[Notices]
[Pages 55161-55162]
From the Federal Register Online via the Government Publishing Office [www.gpo.gov]
[FR Doc No: 96-27331]


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DEPARTMENT OF HEALTH AND HUMAN SERVICES

Government-Owned Inventions; Availability for Licensing

AGENCY: National Institutes of Health, HHS.

ACTION: Notice.

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    The inventions referenced 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 U.S. companies and may also be available for licensing.

ADDRESSES: Licensing information and a copy of the patent application 
and issued patents may be obtained by contacting Elaine Gese at the 
Office of Technology Transfer, National Institutes of Health, 6011 
Executive Boulevard, Suite 325, Rockville, Maryland 20852-3804 
(telephone 301/496-7056 ext 282; fax 301/402-0220). A signed 
Confidential Disclosure Agreement will be required to receive a copy of 
the patent application.

Plant Protein Useful for Treating Tumors and HIV Infection

Sylvia Lee-Huang, et al.
U.S. Patent 5,484,889 issued January 16, 1996

    MAP 30, a 30 kDa basic protein, which may be purified from 
Momordica charantia fruit or seed extracts or produced by recombinant 
DNA technology, is useful in treating HIV infection and cancer. M. 
charantia, commonly known as bitter melon, is a medicinal plant whose 
extracts have been used for centuries in China and Southeast Asia as 
antiinfection and antitumor agents. MAP 30 is capable of inhibiting 
HIV-1 infection in T lymphocytes and monocytes as well as replication 
of HIV-1 in infected cells, yet is not toxic to normal uninfected 
cells. The biological properties of MAP 30 include: (1) N-glycosidase 
activity on 28S ribosomal RNA; (2) topological activity on plasmid and 
viral DNAs including HIV-1 LTRs; and (3) dose-dependent inhibition of 
HIV-1 integrase. Three recent publications describing MAP 30 are: Lee-
Huang, et al., ``Proteolytic fragments of anti-HIV proteins MAP30 and 
GAP31 are biologically active,'' XI International Conference on AIDS 
(abstract); Lee-Huang, S., et al., ``Inhibition of the integrase of 
human immunodeficiency virus (HIV) by anti-HIV plant proteins MAP30 and 
GAP31,'' Proc. Natl. Acad. Sci. 92: 8818-8822 (1995); and Lee-Huang, 
S., et al., ``Anti-HIV and anti-tumor activities of recombinant MAP30 
from bitter melon,'' Gene 161: 151-156 (1995). The cloning and 
expression of the gene encoding biologically active recombinant MAP30 
provides an abundant source of homogeneous material for clinical 
investigations. The patent discloses purified natural and recombinant 
protein, processes for purifying the protein, DNA sequences encoding 
the protein, and recombinant methods for expressing the protein. 
Foreign patent rights are available in Australia, Canada, Europe, and 
Japan. (portfolios: Infectious Diseases--Therapeutics, anti-virals, 
AIDS; Cancer--Therapeutics, other)

Anti-HIV Proteins GAP 31, DAP 30 and DAP 32 and Therapeutic Uses 
Thereof

Sylvia Lee-Huang, et al.
U.S. Patent 5,317,009 issued May 31, 1995

    GAP 31, a 31 kDa protein, and DAP 30 and 32, 30 and 32 kDa 
proteins, respectively, which may be purified from extracts of Gelonium 
multiflorum (a medicinal plant) and Dianthus caryophyllus (carnation), 
respectively, or produced by recombinant DNA technology, are useful in 
treating HIV infection. GAP 31 also exhibits anti-tumor activity. These 
proteins belong to the family of single-chain ribosome-inactivating 
proteins (SCRIPS), which inactive ribosomes in cell-free systems but 
are relatively nontoxic to intact cells. The biological properties of 
GAP 31 include: (1) N-glycosidase activity on 28S ribosomal RNA; (2) 
topological activity on plasmid and viral DNAs including HIV-1 LTRs; 
and (3) dose-dependent inhibition of HIV-1 integrase. Two recent 
publications concerning GAP 31 are: Lee-Huang, et al., ``Proteolytic 
fragments of anti-HIV proteins MAP30 and GAP31 are biologically 
active,'' XI International Conference on AIDS (abstract) and Lee-Huang, 
S., et al., ``Inhibition of the integrase of human immunodeficiency 
virus (HIV) by anti-HIV plant proteins MAP30 and GAP31,'' Proc. Natl. 
Acad. Sci. 92: 8818-8822 (1995). The cloning and expression of the 
genes encoding biologically active recombinant GAP31, and DAP 30 and 32 
provides an abundant source of homogeneous material for clinical 
investigations. The patent discloses purified natural and recombinant 
proteins, processes for purifying the proteins, DNA sequences encoding 
the proteins, and recombinant methods for expressing the proteins. 
Foreign patent rights are available in Australia, Canada, Europe, and 
Japan. (portfolio: Infectious Diseases--Therapeutics, anti-virals, 
AIDS)

An Anti-HIV Protein, TAP 29, From Trichosanthes, DNA Coding Therefor 
and Therapeutic Uses Thereof

Sylvia Lee-Huang, et al.
U.S. Patent Application 08/275,327 filed October 26, 1992

    TAP 29, a 29 kDA protein which may be purified from the root tuber 
of the plant Trichosanthes kirilowii or produced by recombinant DNA 
technology, is useful in treating HIV infection and also exhibits anti-
tumor activity. TAP 29 is a single-chain ribosome-inactivating protein 
(SCRIP) which inactivates ribosomes in cell-free systems but is 
relatively nontoxic to intact cells. TAP 29 has anti-HIV activity 
equivalent to trichosanthin but has a lower in vitro toxicity with a 
therapeutic index of approximately 5000. The cloning and expression of 
the gene encoding biologically active recombinant TAP 29 provides an 
abundant source of homogeneous material for clinical investigations. 
TAP 29 is further described in ``TAP 29: An anti-human immunodeficiency 
virus protein from Trichosanthes kirilowii that is nontoxic to intact 
cells,'' Proc. Natl. Acad. Sci. 88: 6570 (1991) and ``Plant proteins 
with antiviral activity against human immunodeficiency virus,'' in 
Natural Products as Antiviral Agents (C.K. Chu, ed., 1992). The natural 
protein, the DNA coding therefore, an antibody specific therefore, a 
method for purifying the natural protein, and the recombinant protein 
are provided. Foreign patent rights are available in Australia, Canada, 
Europe, and Japan. (portfolio: Infectious Diseases--Therapeutics, anti-
virals, AIDS)


[[Page 55162]]


    Dated: October 11, 1996.
Barbara M. McGarey,
Deputy Director, Office of Technology Transfer.
[FR Doc. 96-27331 Filed 10-23-96; 8:45 am]
BILLING CODE 4140-01-M